wanglab/gogpt-training-data huggingface dataset:
Protein: GM04645p (RE18708p) (UDP-glycosyltransferase family 302 member C1) (Q9VGT3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKPTAGQTGFLALLLFCLLSCVSAYNYLVVLHTAARSHYHVGSALAKGLAAAGHQVTIISPFELKKPIKNIKDVPAKSILTSMQGRIANLLQSSKEPIIKQIINFHEMGIEITELLLKEPSVIELMKSNQTFDAVISEVFLNEAHFGFAEHFKAPLIGLGTFGAISWNTDLVGSPSPPSYVPSALLKFSDRMSLVERVGNQAFLTYEYIFLNYFYLPRQEVLYRKYFPNNKQDFYDMRKNTALVLLNQHVSLSFPRPYSPNMIEVGGMHINRKRQPLPKDILEFIEGAEHGVIYFSMGSNLKSKTLPLEKRQALIDTFAQLKQRVLWKFEDTDLPGKPANVFISDWFPQDDILAHDNVLAFITHGGLLSTTESIYHRKPFVGIPIFGDQFLNMARAEQNGYGVTVHYEELSSAKLLAAIQKIINNPEATQRVRDMSDRYRDQQQTPLERAVYWVEHVSRHKGAKYLRSASQDLNFIQYHNLDAMLILYGGIIFVLYCIFLLIRLVWRLLQELFIKKDTSKPKQKAKRN
Protein: Chaperone Ric-8A (Synembryn-A) (Q80ZG1)
Organism: Rattus norvegicus (Rat)
Function: Guanine nucleotide exchange factor (GEF), which can activate some, but not all, G-alpha proteins. Able to activate GNAI1, GNAO1 and GNAQ, but not GNAS by exchanging bound GDP for free GTP. Involved in regulation of microtubule pulling forces during mitotic movement of chromosomes by stimulating G(i)-alpha protein, possibly leading to release G(i)-alpha-GTP and NuMA proteins from the NuMA-GPSM2-G(i)-alpha-GDP complex. Also acts as an activator for G(q)-alpha (GNAQ) protein by enhancing the G(q)-coupled receptor-mediated ERK activation.
Subcellular location: Cytoplasm, cell cortex {ECO:0000269|PubMed:21158412}. Cytoplasm {ECO:0000269|PubMed:21158412}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- G protein subunit alpha transducin 1
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- G protein subunit alpha transducin 2
- Guanine nucleotide-binding protein subunit alpha-13
- Guanine nucleotide-binding protein G
- Regulator of G-protein signaling 7
- Guanine nucleotide-binding protein G
Sequence:
MEPRAVADALETGEEDAVTEALRSFNREHSQSFTFDDAQQEDRKRLAKLLVSVLEQGLSPKHRVTWLQTIRILSRDRSCLDSFASRQSLHALACYADIAISEEPIPQPPDMDVLLESLKCLCNLVLSSPTAQMLAAEARLVVRLAERVGLYRKRSYPHEVQFFDLRLLFLLTALRTDVRQQLFQELHGVRLLTDALELTLGVAPKENPLVILPAQETERAMEILKVLFNITYDSVKREVDEEDAALYRYLGTLLRHCVMADAAGDRTEEFHGHTVNLLGNLPLKCLDVLLALELHEGSLEFMGVNMDVINALLAFLEKRLHQTHRLKECVAPVLSVLTECARMHRPARKFLKAQVLPPLRDVRTRPEVGDLLRNKLVRLMTHLDTDVKRVAAEFLFVLCSESVPRFIKYTGYGNAAGLLAARGLMAGGRPEGQYSEDEDTDTEEYREAKASINPVTGRVEEKPPNPMEGMTEEQKEHEAMKLVNMFDKLSRHRLIQPMGMSPRGHLTSLQDAMCETMEGQLSSDPDSDPD
Protein: MB2p protein (P70238)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MAALWLLLLVLSLDCMGAGGFVAHVESTCVLDDAGTPQDFTYCVSFNKDLLACWDPDVGKIVPCEFGVLSRLAEIISMILNEQESLIQRLQNGLQDCATHTQPFWDVLTHRTRAPSVRVAQTTPFNTREPVMLACYVWGFYPADVTITWMKNGQLVPSHSNKEKTAQPNGDWTYQTVSYLALTPSYGDVYTCVVQHSGTSEPIRGDWTPGLSPIQTVKVSVSAATLGLGFIIFCVGFFRWRKSHSSSYTPLPGSTYPEGRH
Protein: Amylo-1,6-glucosidase, 4-alpha-glucanotransferase (F6XXE6)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
XHQISVVAEERFYTKWNPGASPADTGDVNVHSGIIAARCAINRLHQELGAKGFIQVYVDQVDEDIVAVTRHSPSIHQSVVAVSRTAFRNPKTSFYSKEVPQMCIPGKIEEVVLEARTIERNTKPYKKDENSINGMPNMTVELREHIQLHESKIVRQAGVATKGPNEYIQEIEFENLSPGSVIIFRVSLDPHAQVAVGILRNHLTQFSSHFKSGSLAVDNADPILKIPFASIASKLTLAELNQVLYRCESEEQEDGGGCYDIPNWSSLKYAGLQGLMSVLAEIRPKNDLGHPFCENLRSGDWMIDYVSGRLISRSGSIAEVGKWLQAMFFYLKQIPRYLIPCYFDAILIGAYTTLLDVAWKQMSSFVQNGSTFVKHLSLGSVQMCGVGKCPCLPLLSPSLLDVPCRLNEITKEKEQCCASLAAGLPHFSSGLFRCWGRDTFIALRGMLLVTGRYLEARNIILAFASTLRHGLIPNLLGEGTYARYNCRDAVWWWLQCIQDYCRTVPNGLDILKCPVSRMYPTDDSAPLPAGTLDQPLFEVIQEAMQRHMQGIQFRERNAGPQIDRNMKDEGFNITAGIDEETGFVYGGNRFNCGTWMDKMGESDRARNRGIPATPRDGSAVEIVGLCKSAVRWLLELSKKNIFPYHEVRVKRHGKVVAVSYDEWNRKIQNNFEKLFHVSEDPSDPNEKHPNLVHKRGIYKDSYGASSPWCDYQLRPNFTIAMVVAPELFTAEKAWKALEIAEKKLLGPLGMKTLDPDDMVYCGVYDNALDNDNYNLARGFNYHQGPEWLWPIGYFLRAKLYFSKMMGPETAAKTVFLVKNVLSRHYVHLER
Protein: Cysteine protease RD19A (EC 3.4.22.-) (Protein RESPONSIVE TO DEHYDRATION 19) (RD19) (P43296)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable thiol protease (By similarity). Required for RRS1-mediated resistance against Ralstonia solanacearum. Plays a crucial role as host factor for PopP2-triggered RRS1-mediated resistance. Interacts with the R.solanacearum type III effector PopP2 to form a nuclear complex that is required for activation of the RRS1-mediated resistance response.
Subcellular location: Lytic vacuole {ECO:0000269|PubMed:18708476}. Nucleus {ECO:0000269|PubMed:18708476}. Note=Predominantly vacuolar. From the Golgi apparatus, probably transported to the lytic vacuole (LV) in clathrin-coated vesicles (CCVs) via the prevacuolar compartment (PVC). Relocalizes to the nucleus when associated in a complex with the Ralstonia solanacearum type III effector PopP2. {ECO:0000269|PubMed:18708476}.
Interaction partners:
- Disease resistance protein RRS1
- UPF0235 protein At5g63440
- Vacuolar-processing enzyme gamma-isozyme
- Cysteine proteinase RD21A
- Vacuolar-processing enzyme beta-isozyme
- Probable cysteine protease RD21B
- Thiamine thiazole synthase, chloroplastic
- At1g09850
- Aspartyl protease UND
- Probable cysteine protease RD21C
Sequence:
MDRLKLYFSVFVLSFFIVSVSSSDVNDGDDLVIRQVVGGAEPQVLTSEDHFSLFKRKFGKVYASNEEHDYRFSVFKANLRRARRHQKLDPSATHGVTQFSDLTRSEFRKKHLGVRSGFKLPKDANKAPILPTENLPEDFDWRDHGAVTPVKNQGSCGSCWSFSATGALEGANFLATGKLVSLSEQQLVDCDHECDPEEADSCDSGCNGGLMNSAFEYTLKTGGLMKEEDYPYTGKDGKTCKLDKSKIVASVSNFSVISIDEEQIAANLVKNGPLAVAINAGYMQTYIGGVSCPYICTRRLNHGVLLVGYGAAGYAPARFKEKPYWIIKNSWGETWGENGFYKICKGRNICGVDSMVSTVAATVSTTAH
Protein: D-lactate dehydratase (EC 4.2.1.130) (Q6FX51)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Candida glabrata strain CBS138 chromosome L complete sequence
- Lactoylglutathione lyase
- Candida glabrata strain CBS138 chromosome J complete sequence
- hydroxyacylglutathione hydrolase
- Candida glabrata strain CBS138 chromosome E complete sequence
- Candida glabrata strain CBS138 chromosome E complete sequence
- D-2-hydroxyglutarate dehydrogenase, mitochondrial
- D-lactate dehydrogenase
- Threonine dehydratase
- L-serine dehydratase
Sequence:
MAAKKVLLALTSYNGDFYEDGAKTGVFVVEAMHPFNLFTEKGFEVDFVSETGKYGWDEHSLIPDFLSGKDKEDFDNENSSFHKALKNVKAAKDVKASDYDIFFASAGHGTLFDYPKAKELQGLAEDIYANGGVVAAVCHGPAIFDGLKDKKTGKPLIEGKAITGFTDIGEVVLNVDKIMKDKGLLSVEDIAKKYGAKYLAPIGPWDDFSITDGKLVTGVNPASAHSTAQRAIDALN
Protein: Mitochondrial amidoxime reducing component 2 (mARC2) (EC 1.7.-.-) (Molybdenum cofactor sulfurase C-terminal domain-containing protein 2) (MOSC domain-containing protein 2) (Moco sulfurase C-terminal domain-containing protein 2) (Q969Z3)
Organism: Homo sapiens (Human)
Function: Catalyzes the reduction of N-oxygenated molecules, acting as a counterpart of cytochrome P450 and flavin-containing monooxygenases in metabolic cycles. As a component of prodrug-converting system, reduces a multitude of N-hydroxylated prodrugs particularly amidoximes, leading to increased drug bioavailability. May be involved in mitochondrial N(omega)-hydroxy-L-arginine (NOHA) reduction, regulating endogenous nitric oxide levels and biosynthesis. Postulated to cleave the N-OH bond of N-hydroxylated substrates in concert with electron transfer from NADH to cytochrome b5 reductase then to cytochrome b5, the ultimate electron donor that primes the active site for substrate reduction.
Subcellular location: Mitochondrion outer membrane; Peripheral membrane protein. Peroxisome {ECO:0000250}.
Interaction partners:
- Molybdopterin synthase catalytic subunit
- Molybdenum cofactor biosynthesis protein 1
- Gephyrin
- Cytochrome b5 type B
- NADH-cytochrome b5 reductase 3
Sequence:
MGASSSSALARLGLPARPWPRWLGVAALGLAAVALGTVAWRRAWPRRRRRLQQVGTVAKLWIYPVKSCKGVPVSEAECTAMGLRSGNLRDRFWLVIKEDGHMVTARQEPRLVLISIIYENNCLIFRAPDMDQLVLPSKQPSSNKLHNCRIFGLDIKGRDCGNEAAKWFTNFLKTEAYRLVQFETNMKGRTSRKLLPTLDQNFQVAYPDYCPLLIMTDASLVDLNTRMEKKMKMENFRPNIVVTGCDAFEEDTWDELLIGSVEVKKVMACPRCILTTVDPDTGVIDRKQPLDTLKSYRLCDPSERELYKLSPLFGIYYSVEKIGSLRVGDPVYRMV
Protein: Zinc finger protein 212 (Q6P238)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
PTRHRRKRRATPLAPATPPSQTTEKSPYFQTTEISLWTVVAAIQAVEKKMESQAARLQSLEGRAGSAEKKLADFEKTAVEFSNQLEGKWAVLGTLLQEYGLLQRRLENVENLLRNKNFWVLRLPPGSKGETPKVSGSLENDGVCFSEQEWENLEDWQKELYRNVMESNYETLVSLKVLGQPEEEVELGAEMVGDLVEEGTHLDRAMVKQEMLYKQEGPAGLPNMFSSAVEQQAFFGAEQAMFWNSPGDSALLESGPGDSNPESVETSRDPAPGRNLDCPRKQKSHRQVQLGQECGQGLKVKRDSSPYKCPECQISFRYKQQLTAHLQSHAGRESYSATEPEESLRPRPRLKPQAKRSKLHQCDVCHRSFSCKVSLVTHQRCHQQEGPSTSPQIQERFSPNSLVALPGHIPWRKSRSSLICGYCGKSFSHPSDLVRHQRIHTGERPYSCPECEKSFVQKQHLLQHQKIHQRERGGLASESARPNGLL
Protein: E3 ubiquitin-protein ligase RNF152 (EC 2.3.2.27) (RING finger protein 152) (RING-type E3 ubiquitin transferase RNF152) (Q8N8N0)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase mediating 'Lys-63'-linked polyubiquitination of RRAGA in response to amino acid starvation. Thereby, regulates mTORC1 signaling and plays a role in the cellular response to amino acid availability. Also mediates 'Lys-48'-linked polyubiquitination of target proteins and their subsequent targeting to the proteasome for degradation. Induces apoptosis when overexpressed.
Subcellular location: Lysosome membrane {ECO:0000269|PubMed:25936802, ECO:0000305|PubMed:21203937}; Single-pass membrane protein {ECO:0000269|PubMed:25936802, ECO:0000305|PubMed:21203937}.
Interaction partners:
- Ras-related GTP-binding protein A
- Ras-related GTP-binding protein B
Sequence:
METLSQDSLLECQICFNYYSPRRRPKLLDCKHTCCSVCLQQMRTSQKDVRCPWCRGVTKLPPGFSVSQLPDDPEVLAVIAIPHTSEHTPVFIKLPSNGCYMLPLPISKERALLPGDMGCRLLPGSQQKSVTVVTIPAEQQPLQGGAPQEAVEEEQDRRGVVKSSTWSGVCTVILVACVLVFLLGIVLHNMSCISKRFTVISCG
Protein: Ras guanine nucleotide exchange factor efc25 (Exchange factor cdc25p-like protein) (Q9USU1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in chromosome segregation and cell morphology upstream of the ras1-scd1 pathway. Promotes the exchange of ras1-bound GDP by GTP leading to its activation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Ras-like protein 1
- Protein csh3
- Protein sts5
- Cell division control protein 42 homolog
- GTP-binding protein rhb1
- Rho guanine nucleotide exchange factor gef1
Sequence:
MRRPNLDRLRLKSRQGFETSVSKPSTPSYSTYSLSPTFSDKSVLSPSTMSDSYALSSTYTAGSSYQNGESDYFGSLPTPSSDKSSTSPFPYLKGSFDDRFSSTHSLTRQPSPRSPLTPLKGNTRASPEIRYVSDFTPPSSPFEDMQASVHSLPLSGCSIGPVRTNHSSSLSNSSNSLLQTESSLRPNSSFVNSPFFPLPSSDDLFLNDRVINLFLFYEKFSYLFTHLLSAIKSRDALSIPSLVLSLQEELFNLCQQTGTFYLLQHNLLQNFEFENPIKLHFDKIIPYFSRLTVLTFSNRAFIFPDHTFPRLQQSAEDFLYHLQFFFTLCANNSLYLSRFCYYPSFVPNTPFGGKWTNNGLSAVSSAYRTRLLEPCLPELDKCVWFLLKNCDEFIENFSDFADEEYVFEICSTITSHSEQIFNKLESWDMSIYFDKDLSECEQATNFAVQSYFVTKQRCYDLLTDLVCSSQDLMMEHSNDFSTMPTMIASIAVAFQTLFENVCDFLKVRAALVDEMQELATKEFENKFSNANTAKDDEPARQTNKGTTRISRSSDFTAVSEMSKDTLTLGRNSLQSILMLDNLLTNKVVQSDNNVKGGTLPALVHYLVQNVHLNKDFRHSFLLTYKTFTTPQELFTLLVILFHELPPPGLDATAYSSWEKGDNFVTKKNVCTVMNLWVQKYFFEDLKARNTLYLISEMRTFLRDHVVPSFHIGSVILSEIDNLWTEEPPDSLTQRLLSSPMATFISLNVYAYTPEEFASQMTLLEFDYLKQIPSREWIFRSWVSRDSRSAVRNYINFSNCFTYWIINCILEKKNTKARTAVISFFIQTAYKCLSLQNFSTLMSIVSALNSAPIYRLHAAYKLVKAEDIICLSGLREIVETKKNFSTYRALLRKAELPCVPFLGVILSDLTFIDEGNPDVLDSSPHLLSFNKRHRLADVVADVCRFQSSSYEMQSNTDLQSYILHRCRFVNQDLSYLFDKSLSLEPRSS
Protein: Ras GTPase-activating-like protein rng2 (Ring assembly protein 2) (O14188)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for cytokinesis. Component of the contractile F-actin ring; required for its construction following assembly of F-actin at the division site.
Subcellular location: Cytoplasm, cytoskeleton. Nucleus envelope. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Note=Localized to the F-actin ring and spindle pole body during interphase and mitosis. Also found in septum.
Interaction partners:
- Myosin regulatory light chain cdc4
- Anillin-related medial ring protein mid1
- Cell division control protein 15
- Myosin type-2 heavy chain 1
- Cell division control protein 12
- Myosin regulatory light chain 1
- Actin
- Cell division control protein 42 homolog
- Myosin type-2 heavy chain 2
- Alpha-actinin-like protein 1
Sequence:
MDVNVGLSRLQSQAGAPVGTKGSNTRLAAKQRETLQAYDYLCRVDEAKKWIEECLGTDLGPTSTFEQSLRNGVVLALLVQKFQPDKLIKIFYSNELQFRHSDNINKFLDFIHGIGLPEIFHFELTDIYEGKNLPKVIYCIHALSYFLSMQDLAPPLIKSDENLSFTDEDVSIIVRRLRQSNVILPNFKALSADFMLRASPVSSRTPSPTRFPKHARFQTLNSSDSASIYSSPYTSPTLEFSKKDASARSDILKMHRRTKSATPSLEQFNEPYKQTLPSHSIEFEDSFFQPPSQKGHMQRSFLTTFSAPTRRREALFSTTSGLSQRSPVDEKIVNAIQACGRGVLVRLRLVDMLQSLVEQSSSVVLLQAVIRGYISRNTYRIRKKAYDELVNWVTSIQSISRAYLIRAQYRKVVLQEEATKSIQTLQSIIRGGFYRRKYHSLIERLDLFTPSFVLIQSSALGFLTRHAIVNMLDNLYNYIPLFNRMQSILRANMFRNEWSNFLDSVQSFPVSFHSICKGRLIRDSINRLNGSLLGELDNFIKLQNLSRGFMIRRAFKEKLEKLKASTSSFIALQAIVRAFLLRKNLESIYDSFQKSHLSVIKAQSLYRGFITRTKIDYCNDYLLKRLPDIVFMQSAVRAILLRDDVNYTEVQLDSFIPEIVLLQSLIRGYLSRNKFSRKLQNFHKNMENPIVAKSIFRGRQEGLAYRELATAKNPPVMTVKNFVHLLDDTNFDFEEEVLLEKMRKEIVQQVRDNEEIEVHINELDVKIALLVKNKISLDDVLKHHNKYKFGKQSTEYLKINTLSMKSLNNSSRKFLELYQCFFYVLQTNEMYLANYFQALKTEGTSSVKIRHAVYLVLQIFGHGSNRREEVLLLRFISQVIKLEAALVNSSQDLLSDDCVWKLLFTGYRGDVREVKLWKTILGRIHKVLVADNHLDFEINPLTLFKSFNPEVASQTDSPKLTLSLAMQHPPTRNLYVSRLRELRKLCQSFLVALSKNIENIPYALCYTAAQLKNSLQRYFPAAHKEEIFGVIGKFVYWAYVAPVLVSPDNFKLVDGSITALQRKNLYTLSSILSEIFSIESCDSKQLGFFRPLSEFIEVSKQDTMLMLERLVDVVDPEVYFEFDAFEDLVNTKRPVIYMKRDDILGIYSSIAYVIDSIAPPDVNDPLRAVVNSLGPVSEQDNDFVQDETDVKLELNPKFCTIENPVAQERTLIVQTKRYILFIIRIQNGLNLLEILVKPVTDSDEAAWQNLLAEESEKNARNYDLFDDSIFSMSFAELKYTALSNIVEMEKLGFANRRNNYQDMVNSIALDIRNKSRRRMQRQRELDAGHQSLLNLREKRAFLDSQLKSYNEYIEQAMETLQSKKGKKKLIPFSKQYFHMRDLRKSGRVPRFGSFKYPALKLYDRGVLVSISHMPQKEKLYITISADEVGKFILEATSPTVKVSSPRCELHLDDLLSAQYNKVLTLDVLDGRLKLNTNMFLHLIFSKFYS
Protein: NAD(P)H-hydrate epimerase (EC 5.1.99.6) (Apolipoprotein A-I-binding protein) (AI-BP) (NAD(P)HX epimerase) (Q8K4Z3)
Organism: Mus musculus (Mouse)
Function: Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX. Accelerates cholesterol efflux from endothelial cells to high-density lipoprotein (HDL) and thereby regulates angiogenesis (By similarity).
Subcellular location: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03159}. Secreted {ECO:0000255|HAMAP-Rule:MF_03159, ECO:0000269|PubMed:18202122, ECO:0000269|PubMed:18614015}. Note=In sperm, secretion gradually increases during capacitation.
Interaction partners:
- Pyridoxine-5'-phosphate oxidase
- ATP-dependent
- m7GpppN-mRNA hydrolase
- Apolipoprotein A-I
- Uridine diphosphate glucose pyrophosphatase NUDT14
- KIF-binding protein
- Probable ATP-dependent RNA helicase DDX6
- mRNA-decapping enzyme 1A
- mRNA-decapping enzyme 1B
- NADH dehydrogenase iron-sulfur protein 2, mitochondrial
Sequence:
MSGLRTLLGLGLLVAGSRLPRVISQQSVCRARPIWWGTQRRGSETMAGAAVKYLSQEEAQAVDQELFNEYQFSVDQLMELAGLSCATAIAKAYPPTSMSKSPPTVLVICGPGNNGGDGLVCARHLKLFGYQPTIYYPKRPNKPLFTGLVTQCQKMDIPFLGEMPPEPMMVDELYELVVDAIFGFSFKGDVREPFHSILSVLSGLTVPIASIDIPSGWDVEKGNPSGIQPDLLISLTAPKKSATHFTGRYHYLGGRFVPPALEKKYQLNLPSYPDTECVYRLQ
Protein: LIM and senescent cell antigen-like-containing domain protein (A0A8I5ZKY9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell junction, focal adhesion {ECO:0000256|PIRNR:PIRNR038003}. Cell membrane {ECO:0000256|PIRNR:PIRNR038003}; Peripheral membrane protein {ECO:0000256|PIRNR:PIRNR038003}.
Interaction partners:
Sequence:
MTALQLKELSQSGLYRRRRERPDSLRVNGLPEEELSSSVMITPFVFLLLFSPNLRRITLHIYSAVKTKTSNMANALASATCERCKGGFDPAEKIVNSNGELYHEQCFVCAQCFQQFPEGLFYEFEGRKYCEHDFQMLFAPCCHQCGEFIIGRVIKAMNNSWHPECFRCDLCQEVLADIGFVKNAGRHLCRPCHNREKARGLGKYICQKCHAIIDEQPLIFKNDPYHPDHFNCANCGKELTADARELKGELYCLPCHDKMGVPICGACRRPIEGRVVNAMGKQWHVEHFVCAKCEKPFLGHRHYERKGLAYCETHYNQLFGDVCFHCNRVIEGDVVSALNKAWCVSCFACSTCNTKLTLKNKFVEFDMKPVCKKCYEKFPLELKKRLKKLSETLGRK
Protein: ERCC excision repair 8, CSA ubiquitin ligase complex subunit (A0A8I6A7R7)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MLSFLSARQSGLEDPLRLRRAQSTRRVLGLELNKDRDVERVHCSGVNTLDIEPVEGRYMLSGGSDGVIVLYDLENASRQPYYTCKAVCSVGRSHPDVHKYSVETVQWYPHDTGMFTSSSFDKTLKVWDTNTLQAADVFNFEETVYSHHMSPAATKHCLVAVGTRGPKVQLCDLKSGSCSHILQGIFVKYGTTITL
Protein: T. brucei spp.-specific protein (Q57XU2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSTSSSIFFEVDTEGNEAAEEEECHSLREVPNPAANTNAVACNTSDDVMAAGGALYRPCVSALSVPRSSSSGDATSEEMQQDVRLMLQRNVGLEIPASDQNEEQSMSWVTAETVEQMTDVDDPEGTGERLRGQEVKVVKDLKRESSGELKRGDGREYETESDTDLAGISRPHNHSMIADKVNALNPARSPRFLPIPSGNAKHRDIERGNNSLSVANSNRSGNNNAEQQVHSNGNNAMTASTSPPPKASVEGPASAPAEKGADAQLKREKKCDASFPQPEEAGAVNPEQVCDQPAIPVHPSAARAAPEAKQVKQTAKEKKKGGFFKRIKGLFSCCGTRNVVGKNNSKELRTAGGGAPIAASGKAERAVALNAAVAEGERGKNGKAGCSLKHEHDETTPQGRKCGGEHSDNEGTTANSNGKDRKGEPKVSRSKHDGMKPDGITKEAEKNIGKVTVNKIAERGATTRAQERGSLRSERDIGLKGNDDGGVDDTETDCFSTIPNEEQDSFATGVLPQPSAQAAYDEGKNSGDARRDVSDTLVGDDVTDETLKERQKPASESEMHDERDQTWRAAGAGQTEDANTDPSGAFSPQSISLCPYCNCTGNKQCNCRRDGEPGDSKGGNGSGQAPPVGRRKPRPKWSIGPKKDTDGASQVNKESNVVRSGGGSYVQLAEKRREYLKNTKRGQQNIGRVRNNSSSKGTSGGARQQAAPMQQLQQYQLDQTSQQRSLKHTPVQQQQHAEGDGSETGNRTPVKKMADEERATCGSRSATPPRLPPPKNIPEFMNSLKTLDNAFNHLNNPPKLPCSSEENFSWEHFKKHFYLAGQQFPSEVMNDEELREVLADLSTKMRPSCSACRSTPSELWLLELLTGVKSSQLLVRLEKKSLYETPAETALRGTASRGGEVVTSAVPASHEQ
Protein: Large ribosomal subunit protein eL21 (60S ribosomal protein L21) (O09167)
Organism: Mus musculus (Mouse)
Function: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P46778}. Cytoplasm {ECO:0000269|PubMed:36517592}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P49666}. Note=Detected on cytosolic polysomes (By similarity). Detected in ribosomes that are associated with the rough endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:P46778, ECO:0000250|UniProtKB:P49666}.
Interaction partners:
- Large ribosomal subunit protein eL34
- Large ribosomal subunit protein eL15
- Large ribosomal subunit protein uL13
- Small ribosomal subunit protein eS21
- Large ribosomal subunit protein uL11
- Small ribosomal subunit protein eS1
- Large ribosomal subunit protein uL4
- Ubiquitin-ribosomal protein eS31 fusion protein
- Large ribosomal subunit protein uL10
- Large ribosomal subunit protein uL3
Sequence:
MTNTKGKRRGTRYMFSRPFRKHGVVPLATYMRIYKKGDIVDIKGMGTVQKGMPHKCYHGKTGRVYNVTQHAVGIIVNKQVKGKILAKRINVRIEHIKHSKSRDSFLKRVKENDQKKKEAKEKGTWVQLKRQPAPPREAHFVRTNGKEPELLEPIPYEFMA
Protein: Tricorn protease (EC 3.4.21.-) (P96086)
Organism: Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Function: Tricorn degrades oligopeptides (probably derived from the proteasome) and channels the products to F1, F2 and F3 proteases, which then catalyze the terminal degradation step, yielding free amino acids.
Subcellular location: Cytoplasm.
Interaction partners:
Sequence:
MPSLMSFGSCQWIDQGRFSRSLYRNFKTFKLHEMHGLCMPNLLLNPDIHGDRIIFVCCDDLWEHDLKSGSTRKIVSNLGVINNARFFPDGRKIAIRVMRGSSLNTADLYFYNGENGEIKRITYFSGKSTGRRMFTDVAGFDPDGNLIISTDAMQPFSSMTCLYRVENDGINFVPLNLGPATHILFADGRRVIGRNTFELPHWKGYRGGTRGKIWIEVNSGAFKKIVDMSTHVSSPVIVGHRIYFITDIDGFGQIYSTDLDGKDLRKHTSFTDYYPRHLNTDGRRILFSKGGSIYIFNPDTEKIEKIEIGDLESPEDRIISIPSKFAEDFSPLDGDLIAFVSRGQAFIQDVSGTYVLKVPEPLRIRYVRRGGDTKVAFIHGTREGDFLGIYDYRTGKAEKFEENLGNVFAMGVDRNGKFAVVANDRFEIMTVDLETGKPTVIERSREAMITDFTISDNSRFIAYGFPLKHGETDGYVMQAIHVYDMEGRKIFAATTENSHDYAPAFDADSKNLYYLSYRSLDPSPDRVVLNFSFEVVSKPFVIPLIPGSPNPTKLVPRSMTSEAGEYDLNDMYKRSSPINVDPGDYRMIIPLESSILIYSVPVHGEFAAYYQGAPEKGVLLKYDVKTRKVTEVKNNLTDLRLSADRKTVMVRKDDGKIYTFPLEKPEDERTVETDKRPLVSSIHEEFLQMYDEAWKLARDNYWNEAVAKEISERIYEKYRNLVPLCKTRYDLSNVIVEMQGEYRTSHSYEMGGTFTDKDPFRSGRIACDFKLDGDHYVVAKAYAGDYSNEGEKSPIFEYGIDPTGYLIEDIDGETVGAGSNIYRVLSEKAGTSARIRLSGKGGDKRDLMIDILDDDRFIRYRSWVEANRRYVHERSKGTIGYIHIPDMGMMGLNEFYRLFINESSYQGLIVDVRFNGGGFVSQLIIEKLMNKRIGYDNPRRGTLSPYPTNSVRGKIIAITNEYAGSDGDIFSFSFKKLGLGKLIGTRTWGGVVGITPKRRLIDGTVLTQPEFAFWFRDAGFGVENYGVDPDVEIEYAPHDYLSGKDPQIDYAIDALIEELRNWNEELPQRPS
Protein: U6 snRNA phosphodiesterase 1 (3'-5' RNA exonuclease USB1) (EC 4.6.1.-) (Q6DEF6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: 3'-5' RNA exonuclease that trims the 3' end of oligo(U) and oligo(A) tracts of the pre-U6 small nuclear RNA (snRNA) molecule, leading to the formation of a mature U6 snRNA 3' end-terminated with a 2',3'-cyclic phosphate. Participates in the U6 snRNA 3' end processing that prevents U6 snRNA degradation. In addition also removes uridines from the 3' end of U6atac snRNA and possibly the vault RNA VTRNA1-1.
Subcellular location: Nucleus {ECO:0000255|HAMAP-Rule:MF_03040}.
Interaction partners:
- Pre-mRNA-processing factor 19
- U6 snRNA-associated Sm-like protein LSm8
- RecQ helicase-like 4.
- Spliceosome associated factor 3, U4/U6 recycling protein
Sequence:
MIVNYSSSSSEEESGSSSSPSGKRQKLDTETSEALDHGSAQRKVCKSSHLTPRLPLPESVKEMFRDSEELWTDKSEEHGGRLRSFQHERGNWATYVFFPYDPEEAFLEVLNKMMAAAEAHDIPLTVSEEFHLSLSKTVVLRHHWIQPFVQSIRTSLTHFQKFYCVAYKLKVYSNAEKTRTFLGMEVSTGTPHLLELSKIVDETMKEFNLSTFYEDPSFHISLAWCVGDQTERLKKACLLELQGLIDAHEDGPFHARLNCNELRCKTGNKVFVFPLQ
Protein: SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 2 (A0A8I5ZRE0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEEEVRLKKRKRRRNVDKDPVKEDVEKAKKRRGRPPAEKLSPNPPKLTKQMNAIIDTVINYKDRCNVEKVPCNSQLEIEGNSSGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLGDLEKDVMLLCHNAQTFNLEGSQIYEDSIVLQSVFKSARQKIAKEEESEEESNEEEEEEDEEESEAEAKSVKVKIKLNKKEEKGRDTGKGKKRPNRGKAKPVVSDFDSDEEQDENEQSEASGTDDE
Protein: ERF1_PODAN Eukaryotic peptide chain release factor subunit 1 (ERF1) (Eukaryotic release factor 1)Eukaryotic polypeptide releasing factor (C8V9C7)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Elongation factor 1-alpha
- RNase L inhibitor of the ABC superfamily, putative
- Elongation factor 1-alpha
- Methyltransferase small domain-containing protein
- Small ribosomal subunit protein uS2
- Upf1 domain-containing protein
- Large ribosomal subunit protein uL2 C-terminal domain-containing protein
- 40S ribosomal protein S3
- Small ribosomal subunit protein uS5
- 60S ribosomal protein L12
Sequence:
MSTVQQANEAEKNIEIWKIKKLIKRLEAARGNGTSMISLIIPPKDQVSRAAKMLAEEFGTASNIKSRVNRLSVLSAITSTQQRLKLYNKVPPNGLVVYCGEIITSEGKERKINIDFEPFKPINTSLYLCDNKFHTEALSELLESDQKFGFIIMDGNGALFGTLSGNTREILQKLSVDLPKKHGRGGQSALRFARLREEKRHNYVRKIAELAVQNFITNDKVNVAGIILAGSADFKNDLNQSDMFDQRLQAKVIKVVDVSYGGENGFNQAIELSAETLSNVKFVQEKKLIGKYFEEISQDTGKVCYGVEDTLKALELGACETLIVYENLDVTRWVLKNSEGNEVVVHTTKAQEENKEFFLDKDTGAEMEVVDQSSFLEWLAENYKDFGATLEFVSDKSSEGNQFVKGFGGIGAILRYKVNFEQLADYSDEDEFYDD
Protein: L-gulonolactone oxidase (LGO) (EC 1.1.3.8) (L-gulono-gamma-lactone oxidase) (GLO) (P58710)
Organism: Mus musculus (Mouse)
Function: Oxidizes L-gulono-1,4-lactone to hydrogen peroxide and L-xylo-hexulonolactone which spontaneously isomerizes to L-ascorbate.
Subcellular location: Microsome membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
Interaction partners:
- Regucalcin
- 3-ketodihydrosphingosine reductase
- Lactoylglutathione lyase
Sequence:
MVHGYKGVQFQNWAKTYGCSPEMYYQPTSVGEVREVLALARQQNKKVKVVGGGHSPSDIACTDGFMIHMGKMNRVLQVDKEKKQVTVEAGILLTDLHPQLDKHGLALSNLGAVSDVTVGGVIGSGTHNTGIKHGILATQVVALTLMKADGTVLECSESSNADVFQAARVHLGCLGVILTVTLQCVPQFHLLETSFPSTLKEVLDNLDSHLKKSEYFRFLWFPHSENVSIIYQDHTNKEPSSASNWFWDYAIGFYLLEFLLWTSTYLPRLVGWINRFFFWLLFNCKKESSNLSHKIFSYECRFKQHVQDWAIPREKTKEALLELKAMLEAHPKVVAHYPVEVRFTRGDDILLSPCFQRDSCYMNIIMYRPYGKDVPRLDYWLAYETIMKKFGGRPHWAKAHNCTRKDFEKMYPAFHKFCDIREKLDPTGMFLNSYLEKVFY