wanglab/gogpt-training-data huggingface dataset:
Protein: Programmed cell death protein 4 (Death up-regulated gene protein) (Q9JID1)
Organism: Rattus norvegicus (Rat)
Function: Inhibits translation initiation and cap-dependent translation. May excert its function by hindering the interaction between EIF4A1 and EIF4G. Inhibits the helicase activity of EIF4A. Modulates the activation of JUN kinase. Down-regulates the expression of MAP4K1, thus inhibiting events important in driving invasion, namely, MAPK85 activation and consequent JUN-dependent transcription. May play a role in apoptosis. Tumor suppressor. Inhibits tumor promoter-induced neoplastic transformation. Binds RNA (By similarity).
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Shuttles between the nucleus and cytoplasm. Predominantly nuclear under normal growth conditions, and when phosphorylated at Ser-457 (By similarity). {ECO:0000250}.
Interaction partners:
- RNA helicase
- Eukaryotic initiation factor 4A-II
- Reversion-inducing cysteine-rich protein with Kazal motifs
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- Eukaryotic translation initiation factor 4B
- Ribonuclease 3
- Beta-transducin repeat containing E3 ubiquitin protein ligase
Sequence:
MDVENEQILNVNPTDPDNLSDSLFSGDEENAGTEEIKNEINGNWISASTINEARINAKAKRRLRKNSSRDSGRGDSVSDNGSEAVRSGVAVPTSPKGRLLDRRSRSGKGRGLPKKGGAGGKGVWGTPGQVYDVEEVDVKDPNYDDDQENCVYETVVLPLDETAFEKTLTPIIQEYFEHGDTNEVAEMLRDLNLGEMKSGVPVLAVSLALEGKASHREMTSKLLSDLCGTVMSTNDVEKSFDKLLKDLPELALDTPRAPQLVGQFIARAVGDGILCNTYIDSYKGTVDCVQARAALDKATVLLSMSKGGKRKDSVWGSGGGQQPVNHLVKEIDMLLKEYLLSGDMSEAEHCLKELEVPHFHHELVYEAIVMVLESTGESAFKMMLDLLKSLWKSSTITIDQMKRGYERIYNEIPDINLDVPHSYSVLERFVEECFQAGIISKQLRDLCPSRGRKRFVSEGDGGRLKPESY
Protein: Plasma membrane calcium-transporting ATPase 4 (PMCA4) (EC 7.2.2.10) (Plasma membrane calcium ATPase isoform 4) (Plasma membrane calcium pump isoform 4) (Q64542)
Organism: Rattus norvegicus (Rat)
Function: Calcium/calmodulin-regulated and magnesium-dependent enzyme that catalyzes the hydrolysis of ATP coupled with the transport of calcium out of the cell (By similarity). By regulating sperm cell calcium homeostasis, may play a role in sperm motility (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P23634}; Multi-pass membrane protein {ECO:0000255}. Cell projection, cilium, flagellum membrane {ECO:0000250|UniProtKB:Q6Q477}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Nitric oxide synthase 1
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit alpha
- cGMP-dependent protein kinase 2
- Plasma membrane calcium-transporting ATPase 1
- Plasma membrane calcium-transporting ATPase 3
- Phospholamban
- Troponin I, cardiac muscle
Sequence:
MTNPSGHNLPANSVAESYEGEFGCTLMDLRKLMELRAADAVTQISAHYGSVQEICARLKTSPVEGLSGNPADLEKRRLVFGKNMIPPKKPKTFLELVWEALQDVTLIILEIAAIISLVLSFYRPPGGENEICGHIVSNPEEDEEGETGWIEGAAILASVIIVVFVTAFNDWSKEKQFRGLQSRIELEQKFSIIRNGQLIQLPVAEIVVGDIAQVKYGDLLPADGILIQGNDLKIDESSLTGESDHVKKTLDKDPMLLSGTHVMEGSGRMVVTAVGINSQTGIIFTLLGANEEEDDEKKKKGKKQGVSENRNKAKTQDGVALEIQPLNSQEGLDSEEKEKKASKGPKKEKSVLQGKLTRLAVQIGKAGLIMSILTVLILILYFVVDNFVIQRRAWLPECTPVYIQYFVKFFIIGVTVLVVAVPEGLPLAVTISLAYSVKKMMKDNNLVRHLDACETMGNATAICSDKTGTLTMNRMTVVQAYIGGTHYRQIPKPDDLPPNVLDLIVNSICINSAYTSKILPPEKEGGLPRQVGNKTECGLLGFVTDLKQDYQAVRSEMPEEKLFKVYTFNSVRKSMSTVIRKPEGGFRVFSKGASEIMLRKCDRILNKEGGIVPFKTKDRDNMVRNVIEPMASEGLRTIGIAYRDFDGEEPSWENENEIFTGLVCIAVVGIEDPVRPEVPDAINKCKRAGITVRMVTGDNVNTARAIATKCGILTPGDDFLCLEGKEFNRLIRNEKGEVEQEKLDKVWPRLRVLARSSPTDKHTLVKGIIDSNIGEQRQVVAVTGDGTNDGPALKKADVGFAMGIAGTDVAKEASDIILTDDNFTSIVKAVMWGRNVYDSISKFLQFQLTVNVVAVIVAFSGACITQDSPLKAVQMLWVNLIMDTFASLALATEPPTDSLLRRRPYGRNKPLISRTMMKNILGHAVYQLGIVFLLVFAGDKLFDIDSGRKAPLNSPPSQHYTIVFNTFVLMQLFNEINSRKIHGEKNVFAGVYRNIIFCSVVLGTFFCQILIVEVGGKPFSCTNLTMEQWMWCLFIGIGELLWGQVISAIPTKSLKFLKEAGHGSDKEEISKDAEGLEEIDHAEMELRRGQILWVRGLNRIQTQIRVVKVFHSFRDVIHKSKNQVSIHSFMTQPEYAADDEMSQSFLNQEESPSLASKSRITKRLSDAETVSQNNTNNNAVDCHQVQIVASHPNSPLQSQETPV
Protein: Ornithine carbamoyltransferase, mitochondrial (EC 2.1.3.3) (Ornithine transcarbamylase) (Q4WNW5)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Subcellular location: Mitochondrion matrix {ECO:0000256|ARBA:ARBA00004305}.
Interaction partners:
- Argininosuccinate synthase
- Acetylglutamate kinase, putative
- Arginine biosynthesis bifunctional protein ArgJ
- Arginase
- Carbamoyl phosphate synthase arginine-specific large chain, mitochondrial
- 1,4-alpha-glucan-branching enzyme
- Pyrimidine-specific carbamoyl phosphate synthase-aspartate carbamoyl transferase
- acetylornithine transaminase
- Probable carboxypeptidase AFUA_6G06800
- Carbamoyl phosphate synthase arginine-specific small chain
Sequence:
MACGLKLAAARFGALNGQHLRQRVSLNGLRQYSSQTTPPISPFAPRHFLSIADLTPTEFATLVRNASSYKRSIKSGSVPQNLLGALNGKTVAMMFSKRSTRTRISTEGAVVRMGGHPMFLGKDDIQLGVNESLYDTAVVVSSMVSCIVARVGQHAEVADLAKHSTVPVINALCDSFHPLQAIADFQTMHETFTPKAHGLSSLGLEGLKIAWVGDANNVLFDMAIAAAKMGIDLAVATPKGYEIPAHMLEIIEKAGEGVSSPGKLIQTNVPEEAVKGADVLVTDTWVSMGQEAESIKRLKDFEGFQITADLAKRGGAKEGWKFMHCLPRHPEEVNDEVFYSQRSLVFPEAENRLWAAISAIEAFVVNKGKIL
Protein: R-linalool synthase (bLinS) (EC 4.2.3.26) (Monoterpene synthase) (Sesquiterpene synthase) (D5SL78)
Organism: Streptomyces clavuligerus
Function: In vitro, catalyzes the formation of R-linalool from geranyl diphosphate (GPP). Can also accept farnesyl diphosphate (FPP) as substrate to produce trans-nerolidol.
Interaction partners:
Sequence:
MQEFEFAVPAPSRVSPDLARARARHLDWVHAMDLVRGEEARRRYEFSCVADIGAYGYPHATGADLDLCVDVLGWTFLFDDQFDAGDGRERDALAVCAELTDLLWKGTAATAASPPIVVAFSDCWERMRAGMSDAWRRRTVHEWVDYLAGWPTKLADRAHGAVLDPAAHLRARHRTICCRPLFALAERVGGYEVPRRAWHSSRLDGMRFTTSDAVIGMNELHSFEKDRAQGHANLVLSLVHHGGLTGPEAVTRVCDLVQGSIESFLRLRSGLPELGRALGVEGAVLDRYADALSAFCRGYHDWGRGASRYTTRDHPGDLGLENLVARSSG
Protein: Microtubule-associated protein 2 (MAP-2) (P11137)
Organism: Homo sapiens (Human)
Function: The exact function of MAP2 is unknown but MAPs may stabilize the microtubules against depolymerization. They also seem to have a stiffening effect on microtubules.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305}. Cell projection, dendrite {ECO:0000250|UniProtKB:P20357}.
Interaction partners:
- Synaptophysin
- Neurofilament light polypeptide
- Glial fibrillary acidic protein
- Disks large homolog 4
- Neuromodulin
- RNA binding protein fox-1 homolog 3
- Nestin
- cAMP-dependent protein kinase catalytic subunit alpha
- Myelin basic protein
- Synapsin-1
Sequence:
MADERKDEAKAPHWTSAPLTEASAHSHPPEIKDQGGAGEGLVRSANGFPYREDEEGAFGEHGSQGTYSNTKENGINGELTSADRETAEEVSARIVQVVTAEAVAVLKGEQEKEAQHKDQTAALPLAAEETANLPPSPPPSPASEQTVTVEEDLLTASKMEFHDQQELTPSTAEPSDQKEKESEKQSKPGEDLKHAALVSQPETTKTYPDKKDMQGTEEEKAPLALFGHTLVASLEDMKQKTEPSLVVPGIDLPKEPPTPKEQKDWFIEMPTEAKKDEWGLVAPISPGPLTPMREKDVFDDIPKWEGKQFDSPMPSPFQGGSFTLPLDVMKNEIVTETSPFAPAFLQPDDKKSLQQTSGPATAKDSFKIEEPHEAKPDKMAEAPPSEAMTLPKDAHIPVVEEHVMGKVLEEEKEAINQETVQQRDTFTPSGQEPILTEKETELKLEEKTTISDKEAVPKESKPPKPADEEIGIIQTSTEHTFSEQKDQEPTTDMLKQDSFPVSLEQAVTDSAMTSKTLEKAMTEPSALIEKSSIQELFEMRVDDKDKIEGVGAATSAELDMPFYEDKSGMSKYFETSALKEEATKSIEPGSDYYELSDTRESVHESIDTMSPMHKNGDKEFQTGKESQPSPPAQEAGYSTLAQSYPSDLPEEPSSPQERMFTIDPKVYGEKRDLHSKNKDDLTLSRSLGLGGRSAIEQRSMSINLPMSCLDSIALGFNFGRGHDLSPLASDILTNTSGSMDEGDDYLPATTPALEKAPCFPVESKEEEQIEKVKATGEESTQAEISCESPFLAKDFYKNGTVMAPDLPEMLDLAGTRSRLASVSADAEVARRKSVPSETVVEDSRTGLPPVTDENHVIVKTDSQLEDLGYCVFNKYTVPLPSPVQDSENLSGESGTFYEGTDDKVRRDLATDLSLIEVKLAAAGRVKDEFSVDKEASAHISGDKSGLSKEFDQEKKANDRLDTVLEKSEEHADSKEHAKKTEEAGDEIETFGLGVTYEQALAKDLSIPTDASSEKAEKGLSSVPEIAEVEPSKKVEQGLDFAVQGQLDVKISDFGQMASGLNIDDRRATELKLEATQDMTPSSKAPQEADAFMGVESGHMKEGTKVSETEVKEKVAKPDLVHQEAVDKEESYESSGEHESLTMESLKADEGKKETSPESSLIQDEIAVKLSVEIPCPPAVSEADLATDERADVQMEFIQGPKEESKETPDISITPSDVAEPLHETIVSEPAEIQSEEEEIEAQGEYDKLLFRSDTLQITDLGVSGAREEFVETCPSEHKGVIESVVTIEDDFITVVQTTTDEGESGSHSVRFAALEQPEVERRPSPHDEEEFEVEEAAEAQAEPKDGSPEAPASPEREEVALSEYKTETYDDYKDETTIDDSIMDADSLWVDTQDDDRSIMTEQLETIPKEEKAEKEARRSSLEKHRKEKPFKTGRGRISTPERKVAKKEPSTVSRDEVRRKKAVYKKAELAKKTEVQAHSPSRKFILKPAIKYTRPTHLSCVKRKTTAAGGESALAPSVFKQAKDKVSDGVTKSPEKRSSLPRPSSILPPRRGVSGDRDENSFSLNSSISSSARRTTRSEPIRRAGKSGTSTPTTPGSTAITPGTPPSYSSRTPGTPGTPSYPRTPHTPGTPKSAILVPSEKKVAIIRTPPKSPATPKQLRLINQPLPDLKNVKSKIGSTDNIKYQPKGGQVQIVTKKIDLSHVTSKCGSLKNIRHRPGGGRVKIESVKLDFKEKAQAKVGSLDNAHHVPGGGNVKIDSQKLNFREHAKARVDHGAEIITQSPGRSSVASPRRLSNVSSSGSINLLESPQLATLAEDVTAALAKQGL
Protein: Potassium channel toxin alpha-KTx 9.6 (BjTx-1) (P83405)
Organism: Hottentotta judaicus (Black scorpion) (Buthotus judaicus)
Function: Calcium channel activator. Rapidly and reversibly activates ryanodine receptor 1 (RYR1).
Subcellular location: Secreted {ECO:0000269|PubMed:15067003}.
Interaction partners:
Sequence:
VGCEECPAHCKGKNAKPTCDDGVCNCNV
Protein: histidine kinase (EC 2.7.13.3) (A0A0H3CDI6)
Organism: Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus)
Interaction partners:
Sequence:
MTSYDLILAAAAGAVCLAISVALWSHGQRRNLEARIVALKTRLIQQGGSDDAPAWLDAFDTAVIAVEGGRANLVAGGEGLIACAKALGADAEVSAVVAALSDADPNYAQKLTALFERGEPCVFEARGPHGLVSVEGRAAGALAWLRLAPIDRADSGLPTAARFAAFVDSVVEPCWIAGADGQAIWGNAAFVRAVGAASAQAPALAGKSFDRGADAVVVEAAGKGERREALRWINVEGRRRAFRLSAQPLDGGGVGVFCADVTEIEDVRDAFKKHVEAHDETLNHIAEAVAIFSQTRRLSYHNTAFAELWGLEPAWLADRPTHGEVLDRLRQRRRLPETIDYAGWKAAELARYEDLGPQADDLWDLPDGRTLKVVRQPHPLGGMLLIYSDITGELRLKAQYNALIQVQQATLDKLNDAVAVFGSDGRLRLHNEAFETFWNVTPHALEAAGDFEGVVELCVPRLHDLSFWRELKGRVADPDPQMRAPTSGEVRTSDSRIVLYQSRPLPDGATLIAFADVTDTRDLQSALADRSAALAEAERLKRDFVGNVSYELRTPLTTIIGYSELLERADGISERGRNHVAAVRAAATQLARSIDDVLDMAQIDAGEMALEIEDIRVSDLLLNAQERALKDAQLGGVTLAVECEEDVGLIRGDGKRLAQTLDHLVENALRQTPPGGRVTLSARRALGEVRLDVSDTGRGVPFHVQAHIFDRFVGRDRGGPGLGLALVKALVELHGGWVALESEPGNGSTFTCHLPETQQPGAMQPELGF
Protein: Thioredoxin 2 (PfTRX2) (Q8IDP4)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. As part of the translocon PTEX complex, plays a role in the export of parasite proteins into the host erythrocyte (By similarity). The translocon PTEX complex is a multi-protein machinery resident in the parasite parasitophorous vacuolar membrane, responsible for protein secretion into host cells. May contribute to the unfolding of proteins containing the PEXEL localization motif before their passage through the translocon or regulate the PTEX complex function.
Subcellular location: Parasitophorous vacuole membrane {ECO:0000269|PubMed:22355694}; Peripheral membrane protein {ECO:0000305}. Note=Appears to localize to other uncharacterized organelles. {ECO:0000269|PubMed:22355694}.
Interaction partners:
- Heat shock protein 101
- Exported protein 2
- Translocon component PTEX150
- Translocon component PTEX88
Sequence:
MKKYIFFFLFSFINFFFVYDVTCTKEVTSTNDDPLTPLNRFDKYYLRMFKKVPRLQQNGSNIINGVNMKNTVIVLYFFAKWCQACTMQSTEMDKLQKYYGKRIYLLKVDLDKNESLARKFSVKSLPTIILLKNKTMLARKDHFVSSNDLIALIKKHL
Protein: Protein sidekick-1 (Q7Z5N4)
Organism: Homo sapiens (Human)
Function: Adhesion molecule that promotes lamina-specific synaptic connections in the retina. Expressed in specific subsets of interneurons and retinal ganglion cells (RGCs) and promotes synaptic connectivity via homophilic interactions.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q8AV58}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q8AV58}. Synapse {ECO:0000250|UniProtKB:Q8AV58}.
Interaction partners:
Sequence:
MARGARPSAAGGGGGGAEPPERAGPGRPRGSPPGRARPSLAPRPGPEPSRPRAAPETSGGDTAGAGRCGGRRAAKLGPGRRGWWALLALQLHLLRALAQDDVAPYFKTEPGLPQIHLEGNRLVLTCLAEGSWPLEFKWMRDDSELTTYSSEYKYIIPSLQKLDAGFYRCVVRNRMGALLQRKSEVQVAYMGSFMDTDQRKTVSQGRAAILNLLPITSYPRPQVTWFREGHKIIPSNRIAITLENQLVILATTTSDAGAYYVQAVNEKNGENKTSPFIHLSIARDVGTPETMAPTIVVPPGNRSVVAGSSETTLECIASARPVEDLSVTWKRNGVRITSGLHSFGRRLTISNPTSADTGPYVCEAALPGSAFEPARATAFLFIIEPPYFTAEPESRISAEVEETVDIGCQAMGVPLPTLQWYKDAISISRLQNPRYKVLASGGLRIQKLRPEDSGIFQCFASNEGGEIQTHTYLDVTNIAPVFTQRPVDTTVTDGMTAILRCEVSGAPKPAITWKRENHILASGSVRIPRFMLLESGGLQIAPVFIQDAGNYTCYAANTEGSLNASATLTVWNRTSIVHPPEDHVVIKGTTATLHCGATHDPRVSLRYVWKKDNVALTPSSTSRIVVEKDGSLLISQTWSGDIGDYSCEIVSEGGNDSRMARLEVIELPHSPQNLLVSPNSSHSHAVVLSWVRPFDGNSPILYYIVELSENNSPWKVHLSNVGPEMTGVTVSGLTPARTYQFRVCAVNEVGRGQYSAETSRLMLPEEPPSAPPKNIVASGRTNQSIMVQWQPPPETEHNGVLRGYILRYRLAGLPGEYQQRNITSPEVNYCLVTDLIIWTQYEIQVAAYNGAGLGVFSRAVTEYTLQGVPTAPPQNVQTEAVNSTTIQFLWNPPPQQFINGINQGYKLLAWPADAPEAVTVVTIAPDFHGVHHGHITNLKKFTAYFTSVLCFTTPGDGPPSTPQLVWTQEDKPGAVGHLSFTEILDTSLKVSWQEPLEKNGIITGYQISWEVYGRNDSRLTHTLNSTTHEYKIQGLSSLTTYTIDVAAVTAVGTGLVTSSTISSGVPPDLPGAPSNLVISNISPRSATLQFRPGYDGKTSISRWIVEGQVGAIGDEEEWVTLYEEENEPDAQMLEIPNLTPYTHYRFRMKQVNIVGPSPYSPSSRVIQTLQAPPDVAPTSVTVRTASETSLRLRWVPLPDSQYNGNPESVGYRIKYWRSDLQSSAVAQVVSDRLEREFTIEELEEWMEYELQMQAFNAVGAGPWSEVVRGRTRESVPSAAPENVSAEAVSSTQILLTWTSVPEQDQNGLILGYKILFRAKDLDPEPRSHIVRGNHTQSALLAGLRKFVLYELQVLAFTRIGNGVPSTPLILERTKDDAPGPPVRLVFPEVRLTSVRIVWQPPEEPNGIILGYQIAYRLASSSPHTFTTVEVGATVRQFTATDLAPESAYIFRLSAKTRQGWGEPLEATVITTEKRERPAPPRELLVPQAEVTARSLRLQWVPGSDGASPIRYFTMQVRELPRGEWQTYSSSISHEATACVVDRLRPFTSYKLRLKATNDIGDSDFSSETEAVTTLQDVPGEPPGSVSATPHTTSSVLIQWQPPRDESLNGLLQGYRIYYRELEYEAGSGTEAKTLKNPIALHAELTAQSSFKTVNSSSTSTMCELTHLKKYRRYEVIMTAYNIIGESPASAPVEVFVGEAAPAMAPQNVQVTPLTASQLEVTWDPPPPESQNGNIQGYKIYYWEADSQNETEKMKVLFLPEPVVRLKNLTSHTKYLVSISAFNAAGDGPKSDPQQGRTHQAAPGAPSFLAFSEITSTTLNVSWGEPAAANGILQGYRVVYEPLAPVQGVSKVVTVEVRGNWQRWLKVRDLTKGVTYFFRVQARTITYGPELQANITAGPAEGSPGSPRDVLVTKSASELTLQWTEGHSGDTPTTGYVIEARPSDEGLWDMFVKDIPRSATSYTLSLDKLRQGVTYEFRVVAVNEAGYGEPSNPSTAVSAQVEAPFYEEWWFLLVMALSSLIVILLVVFALVLHGQNKKYKNCSTGKGISTMEESVTLDNGGFAALELSSRHLNVKSTFSKKNGTRSPPRPSPGGLHYSDEDICNKYNGAVLTESVSLKEKSADASESEATDSDYEDALPKHSFVNHYMSDPTYYNSWKRRAQGRAPAPHRYEAVAGSEAGAQLHPVITTQSAGGVYTPAGPGARTPLTGFSSFV
Protein: Iron-sulfur cluster assembly protein SufC (PfSufC) (EC 3.6.1.-) (Q8ILW0)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Plastid, apicoplast {ECO:0000269|PubMed:21722645, ECO:0000269|PubMed:24086138}.
Interaction partners:
- Iron-sulfur cluster assembly protein SufB
Sequence:
MKRRKWLNITWAVTIYIFFGMINVSSYNEGRKRKNKMYSFVINGYNEYKNKYSFLRKPKNVVHMENNNFDMDRLSLLKNLEEESKIITEGEGWDKTHPLLEIKDLHAIEIEGEKEILKGINLEIYLGEKHTIMGRNGSGKSTLAKVIAGHPYYKITKGIIKYKGLDLINLPVNVRSLCGIFLAFQYPVELPMVKNNEFLRAALNSHRRHRNEEEISVSEFNLMMIEEIKKVGLSSEFLDRPVNYGFSGGEKKRNEILQMLILKPTFCILDETDSGLDVDSFKLTSNVITNFSNDNNSFLIVTHYKKLLELLKPNFIHIMHQGKIIESGDFSLVDKIENKGYSQFLKE
Protein: Kelch-like protein 36 (Q8N4N3)
Organism: Homo sapiens (Human)
Function: Probable substrate-specific adapter of an E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.
Interaction partners:
- Uncharacterized protein KIAA0513
Sequence:
MMEGSRQTRVSRPYKISESSKVYRWADHSSTVLQRLNEQRLRGLFCDVVLVADEQRVPAHRNLLAVCSDYFNSMFTIGMREAFQKEVELIGASYIGLKAVVDFLYGGELVLDGGNIDYVLETAHLLQIWTVVDFCCEYLEQEVSEDNYLYLQELASIYSLKRLDAFIDGFILNHFGTLSFTPDFLQNVSMQKLCVYLSSSEVQRECEHDLLQAALQWLTQQPEREAHARQVLENIHFPLIPKNDLLHRVKPAVCSLLPKEANCEGFIEEAVRYHNNLAAQPVMQTKRTALRTNQERLLFVGGEVSERCLELSDDTCYLDAKSEQWVKETPLPARRSHHCVAVLGGFIFIAGGSFSRDNGGDAASNLLYRYDPRCKQWIKVASMNQRRVDFYLASIEDMLVAIGGRNENGALSSVETYSPKTDSWSYVAGLPRFTYGHAGTIYKDFVYISGGHDYQIGPYRKNLLCYDHRTDVWEERRPMTTARGWHSMCSLGDSIYSIGGSDDNIESMERFDVLGVEAYSPQCNQWTRVAPLLHANSESGVAVWEGRIYILGGYSWENTAFSKTVQVYDREADKWSRGVDLPKAIAGGSACVCALEPRPEDKKKKGKGKRHQDRGQ
Protein: Ammonium transporter Rh type C (Rhesus blood group family type C glycoprotein) (Rh family type C glycoprotein) (Rh type C glycoprotein) (Q3BCQ4)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: Functions as an electroneutral and bidirectional ammonium transporter. May regulate transepithelial ammonia secretion (By similarity).
Subcellular location: Apical cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Also detected at the basolateral membrane and in subapical vesicles. {ECO:0000250}.
Interaction partners:
Sequence:
MVWNTNLRWRLPVTCLLLQVALVVLFGVFVRYDMDADPHWIDKKEAENSTSDMENEFYYRYPSFQDVHVMIFVGFGFLMTFLQRYGYSSVGFNFLLAAFGIQWALLLQGWFHSYYRGYIRVGVENLINADFCVGSVCVAFGAVLGKVSPVQLLIMTLFQVTLFSVNEFILLNLLEVKDAGGSMTIHTFGAYFGLTVTWILYRPGLHQSKERQSSVYHSDLFAMIGTLFLWMYWPSFNSAVSNHGDAQHRAAINTYCSLAACVLTSVALSSALHKKGKLDMVHIQNATLAGGVAVGTAAEMMLMPYGSLIVGFICGIVSTLGFVYLTPFLESRLRVQDTCGIHNLHGIPGIIGAIVGAVTASCANTDVYGVNGLTQAFGFDGFKTNRTPSMQGKFQAAGLFVSLAMALVGGIIVGIILKLPFWGQPADENCFEDAIYWEMPEEPKSTVLHPEDSTLKPSEP
Protein: Lymphocyte antigen 6E (Ly-6E) (Stem cell antigen 2) (SCA-2) (Q90986)
Organism: Gallus gallus (Chicken)
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q64253}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q64253}.
Interaction partners:
- Mucolipin 2.
- Terminal nucleotidyltransferase 5C
- Interferon-induced transmembrane protein 3
Sequence:
MKAFLFAVLAAVLCVERAHTLICFSCSDASSNWACLTPVKCAENEEHCVTTYVGVGIGGKSGQSISKGCSPVCPSAGINLGIAAASVYCCDSFLCNISGSSSVKASYAVLALGILVSFVYVLRARE
Protein: Crossover junction endonuclease MUS81 (EC 3.1.22.-) (Q96NY9)
Organism: Homo sapiens (Human)
Function: Interacts with EME1 and EME2 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, replication forks and nicked Holliday junctions. Plays an essential role in mitosis for the processing of stalled or collapsed replication forks.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:11741546, ECO:0000269|PubMed:14617801, ECO:0000269|PubMed:14638871, ECO:0000269|PubMed:15805243}. Note=Recruited to foci of DNA damage in S-phase cells.
Interaction partners:
- Structure-specific endonuclease subunit EME2
- Structure-specific endonuclease subunit SLX4
- Structure-specific endonuclease subunit EME1
- Structure-specific endonuclease subunit SLX1
- DNA excision repair protein ERCC-1
- Fanconi anemia group M protein
- DNA repair endonuclease XPF
- DNA repair protein RAD51 homolog 1
- DNA repair protein RAD52 homolog
- Bifunctional 3'-5' exonuclease/ATP-dependent helicase WRN
Sequence:
MAAPVRLGRKRPLPACPNPLFVRWLTEWRDEATRSRRRTRFVFQKALRSLRRYPLPLRSGKEAKILQHFGDGLCRMLDERLQRHRTSGGDHAPDSPSGENSPAPQGRLAEVQDSSMPVPAQPKAGGSGSYWPARHSGARVILLVLYREHLNPNGHHFLTKEELLQRCAQKSPRVAPGSARPWPALRSLLHRNLVLRTHQPARYSLTPEGLELAQKLAESEGLSLLNVGIGPKEPPGEETAVPGAASAELASEAGVQQQPLELRPGEYRVLLCVDIGETRGGGHRPELLRELQRLHVTHTVRKLHVGDFVWVAQETNPRDPANPGELVLDHIVERKRLDDLCSSIIDGRFREQKFRLKRCGLERRVYLVEEHGSVHNLSLPESTLLQAVTNTQVIDGFFVKRTADIKESAAYLALLTRGLQRLYQGHTLRSRPWGTPGNPESGAMTSPNPLCSLLTFSDFNAGAIKNKAQSVREVFARQLMQVRGVSGEKAAALVDRYSTPASLLAAYDACATPKEQETLLSTIKCGRLQRNLGPALSRTLSQLYCSYGPLT
Protein: Sulfotransferase ssu-1 (EC 2.8.2.1) (Suppressor of stomatin uncoordination protein 1) (Q9U2Z2)
Organism: Caenorhabditis elegans
Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfonation of xenobiotics that contain phenol functional groups. Acts in ASJ sensory neurons to modulate developmental arrest, perhaps by modifying endocrine signaling via the orphan nuclear receptor nhr-1.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:16567400}. Membrane {ECO:0000269|PubMed:16567400}; Peripheral membrane protein {ECO:0000269|PubMed:16567400}.
Interaction partners:
- Suppressor of Stomatin mutant Uncoordination
- Nuclear hormone receptor family member nhr-1
- Carboxylic ester hydrolase
- Putative inositol monophosphatase 3
- Sulfatase N-terminal domain-containing protein
- Neuferricin homolog
- Nuclear hormone receptor family member nhr-40
- 3'
- Specificity protein transcription factor 1
Sequence:
MTPKTPKTPKPPQTPRPMLTVGSPPCTPCSPFVLNATSFCFRKGPARSVVYQPNGHPKQVVIDGEIWPPIFKPKNVRTAKSMQFGETDVVIATYPKCGTTWLQHITSQLIKGHDYKAGKGNELCVQSPMIERMGAAFADNIKGPRVLKTHFHHYNIPKYPDTKYIYCVRNPKDCLTSYFHHNRNFKIYNWANGTWDVFLDLFASGQLAFGDYFEHLLSWLPCLKDDNVLFLKYEDMFQDLENAVYKIGQFLGGEAAHRVENPEILREIVDNSTIDAMKKDQKRWFPESQLHKVEFIRKGGSRDWKNYFTREQSDRIDSIFAAKFAGTPAEHWWKYEMAWEEKPLSIENLSMEEEEEEQSQKLFALPPLPPQRRFSRTSLLSAGYGSVWSLSSQNANMSASSSVNKDLSTFAE
Protein: Dynein light chain 1, cytoplasmic (Dynein light chain LC8-type 1) (P61285)
Organism: Bos taurus (Bovine)
Function: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in changing or maintaining the spatial distribution of cytoskeletal structures (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P63167}. Chromosome {ECO:0000250|UniProtKB:P63167}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P63167}. Nucleus {ECO:0000250|UniProtKB:P63167}. Mitochondrion {ECO:0000250|UniProtKB:P63167}. Note=Upon induction of apoptosis translocates together with BCL2L11 to mitochondria. Recruited to DNA double-strand breaks (DSBs) by TP53BP1 when phosphorylated at Ser-88. {ECO:0000250|UniProtKB:P63167}.
Interaction partners:
- Cytoplasmic dynein 1 intermediate chain 1
- Dynein light intermediate chain
- Cytoplasmic dynein 1 intermediate chain 2
- Dynein light intermediate chain
- Dynein light chain Tctex-type 1
- Cytoplasmic dynein 1 heavy chain 1
- Bcl-2-like protein 11
- Cytoplasmic dynein 2 light intermediate chain 1
- Cytoplasmic dynein 2 heavy chain 1
- Dynein light chain roadblock-type 1
Sequence:
MCDRKAVIKNADMSEEMQQDSVECATQALEKYNIEKDIAAHIKKEFDKKYNPTWHCIVGRNFGSYVTHETKHFIYFYLGQVAILLFKSG
Protein: UPF3 regulator of nonsense transcripts homolog B (yeast) (Q3ULL6)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Regulator of nonsense transcripts 2
- Regulator of nonsense transcripts 1
- Protein mago nashi homolog 2
- Protein mago nashi homolog
- Eukaryotic initiation factor 4A-III
- Telomerase-binding protein EST1A
- RNA-binding protein with serine-rich domain 1
- RNA-binding protein 8A
- Protein CASC3
- Nonsense-mediated mRNA decay factor SMG5
Sequence:
MKEEKDHRPKEKRVTLFTPQGATGGCIGATAEGAKGDDRQDRNRDKKEALSKVVIRRLPPTLTKEQLQEHLQPMPEHDYFEFFSNDTSLYPHMYARAYINFKNQEDILLFRDRFDGYVFLDNKGQEYHAIVEFAPFQKAAKKKIKKRDTKVGTIEDDPEYRKFLESYATDNEKMTSTPETLLEEIEAKNRELIAKRTTPLLSFLKNKQRMREEKREERRRREIERKRQREEERRKWKEEEKRKRKDIEKLKKIERIPEREKIRDEPKIKLLRKPEKGDEKELDKRDKTKRLDKENLNEERASGHSYTLPRRSDVELKDEKPKRLDDEGVRDYRDRDRDYERDQERMIRERERLKRQEEERRRQQQKERYEKEKAFKRKEEEMKREKEALRDKGKKSENTESICSLEKIEKKEEVVKRDRIRNKDRPAMQLYQPGARSRSRLCPADDSIKPGDSPVDKKQESGISHRKEGGEE
Protein: Malate synthase, glyoxysomal (EC 2.3.3.9) (P28344)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Glyoxysome.
Interaction partners:
- Isocitrate lyase
- Methylisocitrate lyase, mitochondrial
- Acetyl-coenzyme A synthetase
- Malic enzyme
- Malic enzyme
- Citrate synthase, mitochondrial
- fumarate hydratase
- Phosphoenolpyruvate carboxykinase
- Malate dehydrogenase
- malate dehydrogenase
Sequence:
MSQVDAQLKDVAILGSVSNEARKILTKEACAFLAILHRTFNPTRKALLQRRVDRQAEIDKGHLPDFLPETKHIRDDPSWKGAPPAPGLVDRRVEITGPTDRKMVVNALNSDVWTYMADFEDSSAPTWDNMINGQINLYDAIRRQVDFKQGQKEYKLRTDRTLPTLIARARGWHLDEKHFTVDGEPISGSLFDFGLYFFHNAKELVARGFGPYFYLPKMESHLEARLWNDVFNLAQDYIGMPRGTIRGTVLIETITAAFEMEEIIYELRDHSSGLNCGRWDYIFSFIKKFRQHPNFVLPDRSDVTMTVPFMDAYVKLLIKTCHKRGVHAMGGMAAQIPIKDNAEANDKAMEGVRADKLREVRAGHDGTWVAHPALASIASEVFNKYMPTPNQMHVRREDVNITANDLLNTNVPGKITEDGIRKNLNIGLSYMEGWLRGVGCIPINYLMEDAATAEVSRSQLWQWARHGVTTSEGKKVDKAYALRLLKEQADALAAKGPKGNKFQLAGRYFAGQVTGEDYADFLTSLLYNEISSPGTASKL