wanglab/gogpt-training-data huggingface dataset:
Protein: Gephyrin [Includes: Molybdopterin adenylyltransferase (MPT adenylyltransferase) (EC 2.7.7.75) (Domain G); Molybdopterin molybdenumtransferase (MPT Mo-transferase) (EC 2.10.1.1) (Domain E)] (Q8BUV3)
Organism: Mus musculus (Mouse)
Function: Microtubule-associated protein involved in membrane protein-cytoskeleton interactions. It is thought to anchor the inhibitory glycine receptor (GLYR) to subsynaptic microtubules (By similarity). Acts as a major instructive molecule at inhibitory synapses, where it also clusters GABA type A receptors.
Subcellular location: Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q03555}; Lipid-anchor {ECO:0000250|UniProtKB:Q03555}; Cytoplasmic side {ECO:0000250|UniProtKB:Q03555}. Cell membrane {ECO:0000250|UniProtKB:Q03555}; Lipid-anchor {ECO:0000250|UniProtKB:Q03555}; Cytoplasmic side {ECO:0000250|UniProtKB:Q03555}. Cytoplasm, cytosol {ECO:0000269|PubMed:25025157}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q03555}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9NQX3}. Postsynaptic density {ECO:0000269|PubMed:27609886}. Note=Cytoplasmic face of glycinergic postsynaptic membranes (By similarity). Forms clusters at synapses (PubMed:25025157). {ECO:0000250|UniProtKB:Q03555, ECO:0000269|PubMed:25025157}.
Interaction partners:
- Rho guanine nucleotide exchange factor 9
- Glycine receptor subunit beta
- Neuroligin-2
- Neuronal acetylcholine receptor subunit alpha-3
- Vesicular inhibitory amino acid transporter
- Molybdopterin synthase catalytic subunit
- Glycine--tRNA ligase
- Gamma-aminobutyric acid receptor subunit gamma-2
- Gamma-aminobutyric acid receptor-associated protein
- Molybdenum cofactor biosynthesis protein 1
Sequence:
MATEGMILTNHDHQIRVGVLTVSDSCFRNLAEDRSGINLKDLVQDPSLLGGTISAYKIVPDEIEEIKETLIDWCDEKELNLILTTGGTGFAPRDVTPEATKEVIEREAPGMALAMLMGSLNVTPLGMLSRPVCGIRGKTLIINLPGSKKGSQECFQFILPALPHAIDLLRDAIVKVKEVHDELEDLPSPPPPLSPPPTTSPHKQTEDKGVQCEEEEEEKKDSGVASTEDSSSSHITAAALAAKIPDSIISRGVQVLPRDTASLSTTPSESPRAQATSRLSTASCPTPKQIRRPDESKGVASRVGSLKARLPSCSSTYSVSEVQSRCSSKENILRASHSAVDITKVARRHRMSPFPLTSMDKAFITVLEMTPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRFIIGESQAGEQPTQTVMPGQVMRVTTGAPIPCGADAVVQVEDTELIRESDDGTEELEVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSEIGLLATVGVTEVEVNKFPVVAVMSTGNELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGGVSMGEKDYLKQVLDIDLHAQIHFGRVFMKPGLPTTFATLDIDGVRKIIFALPGNPVSAVVTCNLFVVPALRKMQGILDPRPTIIKARLSCDVKLDPRPEYHRCILTWHHQEPLPWAQSTGNQMSSRLMSMRSANGLLMLPPKTEQYVELHKGEVVDVMVIGRL
Protein: Sortilin (Q8IKV8)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- Vacuolar protein sorting-associated protein 35
- Calponin homology domain-containing protein, putative
- Proteasome subunit beta
- Proteasome subunit alpha type
- Proteasome subunit alpha type-1, putative
- Proteasome subunit alpha type
- Proteasome subunit beta
- Vacuolar protein sorting-associated protein 26
- Phosphoinositide phosphatase SAC1
- SDE2-like domain-containing protein
Sequence:
MKKKLEKQKKLLEYEKGYYSNKVKMRNMLFFKSIGNKNHLFLVFLLFLFFSFSCINFTQCQITKKKVSVSEINFDSAVDDVQWCGNNHMTVLVKTVKGRLYRSSDGGKIWTNITGNLSDKENNKSDPSSNHMNEMTTVDLIMVNSVNKNIVLIIGNQKNHYISEDSGETFRLLNYQNKINFWQFHSTKTHWALVSSWTEACYSNDDNSGECMQTLSLTKDLGRTFQLIDIYVVQFNWGDKESHLEDTIYYTRHKNRNGHQQRFSGWSKDVDFVATHNFGKSVDVLVKQGNKFLISNGYIFVAKLNDVIKQTVNMMVSTDGGKTFNKANLPENIHEKSYTVLDTSEGSIMLHVNHGTSSEKINTGNVYISDASGLNYTLSLPNNIRTSSGECEFDRVLSLDGVYIANFLDVNNEIKDEDLRFQNFKSAIEEDIAPFETNTEKRKKQYNKGKNEDAVRTVISFNKGGEWSYLKAPKVDSRGNKYECGDNCYLHLHGITNYHQYAPFYSIENAVGIIMGTGNVGSHLRYESDEVNTFLSRDGGVTWIEAHKGPYIYEYGDYGGLIVMADDLRKTNQIVFSWNEGQSWFDFELGQFSIDVDNIVAEPNSASVEFLVYGTRNDVGVLYHLDFNALGQPLCKGLWAADSVSSDYETWSPTSGNFNDKCILGRKITYTRRKQTSECFNGKDLKRTVDKKPCECTPEDYECETGFTRKIGSYECKPNDPTLTIEGCTSSSYFYANAYRKVPGDICVNGWVPEKVPVPCPSYAPFNKTAKSILFIIFIMGIVMLIITYICRNPKFKNLFYNYGFDTFENVKYSVIKTKRGNVNNNVFEPEMEFIDAEQDDNEEDVPTLLPYSSDRNRSTNKDFTLARNRTNQNNNITSRNISPSKNYADNIELL
Protein: Activating transcription factor-2 (Q56H90)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDTAGDMDHLASVSFGDFETKSPEGDVSCYQNFRAQAEHVSLDISLGQKSDTLFAADQTPTPTRLIKNCDEVGLFEDLQHVNPFDIGFQQAAERNVSGTPSRPEARPNDGESLHTPQVYPVEAPTVVSVPSENQVPQSVSCGDMDVDQLLATTVTSPSKASQDGPPPLQLIQPQVLTWVLPAQSVPISIATVDCNRNRVKPTGAIHPFILPKPTAKELNKTSKRPEPILVSCNPPNNEPSSASLTPTSQLPIKERLKAIIHSNNNRRSFSTPPKAAKAKDRSRDEDCMERRRAAASRYRNKMRNEHKDLIKQNAQLQQENQELHERISRLEKELQQHRSHSSLAGVVADQLRIPPSSIHLLINVPNVLVPSSASNASAAKK
Protein: CAP-Gly domain-containing linker protein 1 (Cytoplasmic linker protein 170) (CLIP-170) (Restin) (Q922J3)
Organism: Mus musculus (Mouse)
Function: Binds to the plus end of microtubules and regulates the dynamics of the microtubule cytoskeleton. Promotes microtubule growth and microtubule bundling. Links cytoplasmic vesicles to microtubules and thereby plays an important role in intracellular vesicle trafficking. Plays a role macropinocytosis and endosome trafficking.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P30622}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16954346}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P30622}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell projection, ruffle {ECO:0000250|UniProtKB:P30622}. Note=Localizes to microtubule plus ends. Localizes preferentially to the ends of tyrosinated microtubules (PubMed:16954346). Accumulates in plasma membrane regions with ruffling and protrusions. Associates with the membranes of intermediate macropinocytic vesicles (By similarity). {ECO:0000250|UniProtKB:P30622, ECO:0000269|PubMed:16954346}.
Interaction partners:
- Ras GTPase-activating-like protein IQGAP1
- Dynactin subunit 1
- Microtubule-associated protein RP/EB family member 1
- CLIP-associating protein 2
- Cell division control protein 42 homolog
- Microtubule-associated protein RP/EB family member 3
- Serine/threonine-protein kinase mTOR
- Nuclear migration protein nudC
- CLK4-associating serine/arginine rich protein
- CLIP-associating protein 1
Sequence:
MSMLKPSGLKAPTKILKPGSTALKTPAAAAAPVEKTIPSEKASGPPSSETQEEFVDDFRVGERVWVNGNKPGFIQFLGETQFAPGQWAGIVLDEPIGKNDGSVAGVRYFQCEPLKGIFTRPSKLTRKVQAEDEANGLQAAPGRTASPLSTAAATMVSSSPATPSNIPHKPSQSTAKEPSATPQISNLTKTASESISNLSEAGSVKKGERELKVGDRVLVGGTKAGVVRFLGETDFAKGEWCGVELDEPLGKNDGAVAGTRYFQCQPKYGLFAPVHKVTKIGFPSTTPAKAKAAAVRRVMAATPASLKRSPSASSLSSMSSVASSVSSKPSRTGLLTETSSRYARKISGTTALQEALKEKQQHIEQLLAERDLERAEVAKATSHVGEIEQELALARDGHDQHVLELEAKMDQLRTMVEAADREKVELLNQLEEEKRKVEDLQFRVEEESITKGDLEVATVSEKSRIMELEKDLALRAQEVAELRRRLESSKPPGDVDMSLSLLQEISALQEKLEAIHTDHQGEMTSLKEHFGAREEAFQKEIKALHTATEKLSKENESLRSKLDHANKENSDVIALWKSKLETAIASHQQAMEELKVSFSKGIGTDSAEFAELKTQIERLRLDYQHEIESLQSKQDSERSAHAKEMETMQAKLMKIIKEKEDSLEAVKARLDSAEDQHLVEMEDTLNKLQEAEIKVKELEVLQAKYTEQSEVIGNFTSQLSAVKEKLLDLDALRKANSEGKLELETLRQQLEGAEKQIKNLETERNAESSKANSITKELQEKELVLTGLQDSLNQVNQVKETLEKELQTLKEKFASTSEEAVSAQTRMQDTVNKLHQKEEQFNVLSSELEKLRENLTDMEAKFKEKDDREDQLVKAKEKLENDIAEIMKMSGDNSSQLTKMNDELRLKERSVEELQLKLTKANENASFLQKSIGEVTLKAEQSQQQAARKHEEEKKELEEKLLELEKKMETSYNQCQDLKAKYEKASSETKTKHEEILQNLQKMLADTEDKLKAAQEANRDLMQDMEELKTQADKAKAAQTAEDAMQIMEQMTKEKTETLASLEDTKQTNARLQNELDTLKENNLKTVEELNKSKELLSVENQKMEEFKKEIETLKQAAAQKSQQLSALQEENVKLAEELGRTRDEVTSHQKLEEERSVLNNQLLEMKKRESEFRKDADEEKASLQKSISLTSALLTEKDAELEKLRNEVTVLRGENATAKSLHSVVQTLESDKVKLELKVKNLELQLKENKRQLSSSSGNTDAQAEEDERAQESQIDFLNSVIVDLQRKNQDLKMKVEMMSEAALNGNGEDLNSYDSDDQEKQSKKKPRLFCDICDCFDLHDTEDCPTQAQMSEDPPHSTHHGSRSEERPYCEICEMFGHWATNCNDDETF
Protein: Joining chain of multimeric IgA and IgM (E1BY93)
Organism: Gallus gallus (Chicken)
Interaction partners:
- Ig-like domain-containing protein.
- Uncharacterized protein
- Ig-like domain-containing protein.
- B-cell antigen receptor complex-associated protein beta chain
- Ig-like domain-containing protein.
- Uncharacterized protein.
- KRAB domain containing zinc finger protein
- CD300 molecule like family member g
- Ig-like domain-containing protein.
- Ig-like domain-containing protein.
Sequence:
MKSSLPWVALAVSLGFVLVAGYQWDDGEERVLVNNKCKCVTVTSKFVPSKDNPEEEVLERNIRIIVPLKSRENISDPTSPLRTTFVYRMTELCKKCDPVEIELGGETYQAQQSNSCNEPETCYTYNRDKCYTTTFPFVYHGETKHIQAALTPTSCYAE
Protein: ARM repeat superfamily protein (F4IPA6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004308}.
Interaction partners:
Sequence:
MSDALSAIPAAVHRNLSDKLYEKRKNAALELENIVKNLTSSGDHDKISKVIEMLIKEFAKSPQANHRKGGLIGLAAVTVGLSTEAAQYLEQIVPPVINSFSDQDSRVRYYACEALYNIAKVVRGDFIIFFNKIFDALCKLSADSDANVQSAAHLLDRLVKQDIVTESDQFSIEEFIPLLKERMNVLNPYVRQFLVGWITVLDSVPDIDMLGFLPDFLDGLFNMLSDSSHEIRQQADSALSEFLQEIKNSPSVDYGRMAEILVQRAASPDEFTRLTAITWINEFVKLGGDQLVRYYADILGAILPCISDKEEKIRVVARETNEELRSIHVEPSDGFDVGAILSVARRQLSSEFEATRIEALNWISTLLNKHRTEVLCFLNDIFDTLLKALSDSSDDVVLLVLEVHAGVAKDPQHFRQLIVFLVHNFRADNSLLERRGALIVRRMCVLLDAERVYRELSTILEGEDNLDFASTMVQALNLILLTSPELSKLRELLKGSLVNREGKELFVALYTSWCHSPMAIISLCLLAQAYQHASVVIQSLVEEDINVKFLVQLDKLIRLLETPIFTYLRLQLLEPGRYTWLLKTLYGLLMLLPQQSAAFKILRTRLKTVPTYSFSTGNQIGRATSGVPFSQYKHQNEDGDLEDDNINSSHQGINFAVRLQQFENVQNLHRGQARTRVNYSYHSSSSSTSKEVRRSEEQQQQQQQQQQQQQQQQRPPPSSTSSSVADNNRPPSRTSRKGPGQLQL
Protein: Probable plastid-lipid-associated protein 3, chloroplastic (AtPap3) (Fibrillin-2) (Plastoglobulin 40) (AtPGL40) (O82291)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probably involved in light/cold stress-related jasmonate (JA) biosynthesis.
Subcellular location: Plastid, chloroplast, plastoglobule {ECO:0000269|PubMed:16461379, ECO:0000269|PubMed:22274653}.
Interaction partners:
- Probable plastid-lipid-associated protein 13, chloroplastic
- Probable plastid-lipid-associated protein 8, chloroplastic
- Plastid-lipid-associated protein 6, chloroplastic
- Alternative NAD
- Probable lipid phosphate phosphatase 4
- Probable plastid-lipid-associated protein 4, chloroplastic
- Pentatricopeptide repeat-containing protein At1g01970
- At2g27680/F15K20.22
- Probable membrane metalloprotease ARASP2, chloroplastic
- Putative chloroplast RNA binding protein family protein)
Sequence:
MATLFTVARPSSLLYVSSINPSKTFSPSISLKLNSLSFSFGYRPKPLRFSKIRSSLPSESESESDLDASAVTDEWGEKPGDANEPDSQPDNVTVNVITDEWGEKSGPELEESGTRFMESDPPRNEDEWGGEIGGETEADAGNGSAVSDPTWELKRCLADSVYGTELGFKAGSEVRAEVLELVNQLEALNPTPAPLENPELLDGNWVLLYTAFSELIPLLAAGSTPLLKVKSISQSIDTNNLIIDNSTTLSSPFADFSFSATASFEVRSPSRIEVSFKEGTLKPPVIKSSVDLPESVGVFGQQISLSLLKQSLNPLQDVAANISRALSGQPPLKLPFPGNRGSSWLLTTYLDKDLRISRGDGGLFVLAREGSSLLEL
Protein: Protein phosphatase methylesterase 1 (PME-1) (EC 3.1.1.-) (Q94F26)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Serine/threonine-protein phosphatase PP2A-4 catalytic subunit
- Serine/threonine-protein phosphatase PP2A-5 catalytic subunit
- Serine/threonine-protein phosphatase PP2A-2 catalytic subunit
- Serine/threonine-protein phosphatase PP2A-1 catalytic subunit
- Serine/threonine-protein phosphatase PP2A-3 catalytic subunit
- Serine/threonine-protein phosphatase 2A activator
- WW domain-containing protein
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A gamma isoform
Sequence:
MDSSSNLNPLREDTSEEHLEPIEAPASVFAARPLRPPSTNSSEKYSPVEWKSYFDKEDDISITGSDDVFHVYMAGNEGPVVFCLHGGGYSGLSFSIVASKIKEKARVVAMDLRGHGKSVSENELELSLETMSNDVLAVIKELYGDSPPAIVLVGHSMGGSVAVQVAANKTLPSLAGLVVVDVVEGTAISSLIHMQKILSNRMQHFPSIEKAIEYSVRGGSLRNIDSARVSIPTTLKYDDSKHCYVYRTRLEETEQYWKGWYDGLSEKFLSSPVPKLLLLAGTDRLDRTLTIGQMQGKFQMIVVKHTGHAIQEDVPEEFANLVLNFISRNRIGPHGVEIPGMWKPSQQTKT
Protein: Antisense-enhancing sequence 1 (EC 5.1.-.-) (AES factor 1) (Q8NIL3)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: May have isomerase activity (By similarity). Enhances target gene silencing when coexpressed with antisense RNA.
Interaction partners:
- UPF0654 protein C11D3.01c
- Uncharacterized methyltransferase C70.08c
- UPF0654 protein C869.09
Sequence:
MTEHSFKQIDVFSNKGFRGNPVAVFFDADNLSQKEMQQIAKWTNLSETTFVQKPTIDKADYRLRIFTPECELSFAGHPTIGSCFAVVESGYCTPKNCKIIQECLAGLVELTIDGEKDEDTWISFKLPYYKILQTSETAISEVENALGIPLNYSSQVSPPVLIDDGPKWLVIQLPNATDVLNLVPKFQSLSQVCKNNDWIGVTVFGELGKDSFESRSFAPLIHVNEDPACGSGAGAVGVYIGSSQKTPTSLSFTISQGTKLSRQAISKVSVDVSSNKSIAVFVGGQAKTCISGKSFI
Protein: ATP-dependent RNA helicase DDX19B (EC 3.6.4.13) (DEAD box RNA helicase DEAD5) (DEAD box protein 19B) (Q9UMR2)
Organism: Homo sapiens (Human)
Function: ATP-dependent RNA helicase involved in mRNA export from the nucleus. Rather than unwinding RNA duplexes, DDX19B functions as a remodeler of ribonucleoprotein particles, whereby proteins bound to nuclear mRNA are dissociated and replaced by cytoplasmic mRNA binding proteins.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10428971}. Nucleus, nucleoplasm {ECO:0000269|PubMed:10428971}. Note=Associates with the nuclear pore complex cytoplasmic fibrils. {ECO:0000269|PubMed:10428971}.
Interaction partners:
- Nuclear pore complex protein Nup214
- ATP-dependent RNA helicase DDX19A
- MIF4G domain-containing protein
- mRNA export factor GLE1
- CBP80/20-dependent translation initiation factor
Sequence:
MATDSWALAVDEQEAAAESLSNLHLKEEKIKPDTNGAVVKTNANAEKTDEEEKEDRAAQSLLNKLIRSNLVDNTNQVEVLQRDPNSPLYSVKSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEPPQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKISEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIATQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIKLKREEETLDTIKQYYVLCSSRDEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKDGNPDNETYLHRIGRTGRFGKRGLAVNMVDSKHSMNILNRIQEHFNKKIERLDTDDLDEIEKIAN
Protein: Heparan sulfate 2-O-sulfotransferase 1 (EC 2.8.2.-) (A1L1P8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004323}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004323}.
Interaction partners:
- Heparan sulfate 2-O-sulfotransferase 1
- Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 1
- Exostosin glycosyltransferase 2
- Heparan-sulfate 6-O-sulfotransferase 1-A
- Sulfotransferase
- Adenosine 3'-phospho 5'-phosphosulfate transporter 1
- Exostosin-like 3
- Xylosyltransferase II.
Sequence:
MGLLRLMMPPKFQLLALLAFAIAMIFLENQIQKLEESRGKLEQAIARHEVREIERRHSQVGVKEVQLEEDDTVVIYNRVPKTASTSFTNIAYDLCNKNHYHVLHINTSKNNPVMSLQDQVRFVKNVTLWKEMKPAFYHGHVSFLDFTKFGVKKKPIYINVIRDPIERLVSYYYFLRFGDDYRPGLRRRKQGDKKTFDECVSAGGSDCAPEKLWLQIPFFCGHYSECWNIGSRWALEQAKYNLVNEYMLVGVTEELEDFVMMLEAALPRFFKGATELYKTGKRSHLRKTSEKKPPTKESIARLQQSNIWKMENEFYEFALEQFQYVRAHAVREKDGELYLLTQNFFYEKIYPKSN
Protein: Centrosomal protein of 128 kDa (Zgc:162199 protein) (A4QNW2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MDSSSESGTYNRPRGHRWRARERSDSGFPRDTHVSDISVKIDTLANTLQDTSRNLNKVDRMLEQYKEHADDQVEAMATLRESLEESVQHLQGQRLRKSTSGWRTSNSILQTSDLEDGSATERWCSPPTSTLRNYGSAATGNRRRSGSVVVHFRDATQAEDEIHSLHQSLRDLRSDQLRLGDDIDREISKRNRTDIETKKILEDLAGHVRASKSEELVSLRVEKRLQEIEDEMHSREQVASERHHIEKPDGMSQLQKMDDMRSQLLRIEKDHVQLQREMSLLLSQQRSARRQQQGGVTGVDSELERGLYVSSEVEELKKSIEQREKEKAQLAFQVEVLSADLEQHQLQKLSQLKEVQSLVKNNSLECSHLKAQLIESETRREELRSKAQEAIRQWKTKCKKLGREVQELKNESRNGTDKNKWNQERAGILSQQTERTRRQLADALGSLAQREEDVHRCEVDLAEARSRLVTSELKLQEAQENMRRLEEETQKQISLQLHLREENIRLQERVDLLEQRREVDQRSMLDLQSLHKNLTAAKADLVTRLAEVESSKKDLEIQLAAAQEESSSFGRQLELERLVHQKELSHLQEGKAEQDRDVHNKLISYQREREELEALVKDLKSEALADGELRRTLQLKLDKMKTECDKLTEELSTREESLTQLLRKYHILRKELNVKVKLAKKEEERRHTAEHSMAELRERLASLQTEQESILHATGAQIDSACQFLSDAKLEAITLTPGLQKDSHRWLAEVKTKLQWLCEEVREREAREKRLRRILQHHKEQMKTLKESKDLELQRLLDQIAMQERLLNDIQSEKRGLLEKGRKKEDELRNLQDRIIDLETSTKLALDHLESVPEKLSLLENFKDLEESQRQREMVELRYARYTEIVGDLQRQLEESKRRIQEYRDEKLDATCRSLQLSGLTSSLLSQSNILTNSSLSFHTSQKPVANPDLEPSLTQEHFNGTTSEQTSM
Protein: Large ribosomal subunit protein eL27B (60S ribosomal protein L27-B) (O74538)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- mRNA export factor elf1
- Large ribosomal subunit protein eL28
- Large ribosomal subunit protein uL24
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein eL6
- Large ribosomal subunit protein eL39
- Large ribosomal subunit protein eL14
- Large ribosomal subunit protein eL31
- Large ribosomal subunit protein eL29
- Large ribosomal subunit protein eL13
Sequence:
MVKILKPGKVALVTRGRFAGKKVVILQNVDQGSKSHPFGHAVVAGVERYPLKVTKSMGAKRIAKRSRVKPFIKVINYNHLMPTRYALELDNLKGLVTPTTFSEPSQRSAAKKTVKNTFEEKYQTGKSAWFFTPLRF
Protein: Non-selective voltage-gated ion channel VDAC1 (Outer mitochondrial membrane protein porin 1) (Plasmalemmal porin) (Porin 31HL) (Porin 31HM) (Voltage-dependent anion-selective channel protein 1) (VDAC-1) (hVDAC1) (P21796)
Organism: Homo sapiens (Human)
Function: Forms a channel through the mitochondrial outer membrane and also the plasma membrane. The channel at the outer mitochondrial membrane allows diffusion of small hydrophilic molecules; in the plasma membrane it is involved in cell volume regulation and apoptosis. It adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The open state has a weak anion selectivity whereas the closed state is cation-selective. Binds various signaling molecules, including the sphingolipid ceramide, the phospholipid phosphatidylcholine, and the sterol cholesterol. In depolarized mitochondria, acts downstream of PRKN and PINK1 to promote mitophagy or prevent apoptosis; polyubiquitination by PRKN promotes mitophagy, while monoubiquitination by PRKN decreases mitochondrial calcium influx which ultimately inhibits apoptosis. May participate in the formation of the permeability transition pore complex (PTPC) responsible for the release of mitochondrial products that triggers apoptosis. May mediate ATP export from cells.
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:10661876, ECO:0000269|PubMed:31015432, ECO:0000269|PubMed:31206022, ECO:0000269|PubMed:7539795}; Multi-pass membrane protein {ECO:0000269|PubMed:18755977, ECO:0000269|PubMed:18832158, ECO:0000269|PubMed:27641616}. Cell membrane {ECO:0000269|PubMed:25168729, ECO:0000269|PubMed:25296756}; Multi-pass membrane protein {ECO:0000269|PubMed:18755977, ECO:0000269|PubMed:18832158}. Membrane raft {ECO:0000269|PubMed:25168729}; Multi-pass membrane protein {ECO:0000269|PubMed:18755977, ECO:0000269|PubMed:18832158}. Note=Found in a complex with HSPA9 and VDAC1 at the endoplasmic reticulum-mitochondria contact sites. {ECO:0000250|UniProtKB:Q9Z2L0}.
Interaction partners:
- Peptidyl-prolyl cis-trans isomerase F, mitochondrial
- Translocator protein
- Bcl-2-like protein 1
- Non-selective voltage-gated ion channel VDAC2
- Apoptosis regulator Bcl-2
- Stress-70 protein, mitochondrial
- Hexokinase-1
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR3
- Hexokinase-2
- ADP/ATP translocase 3
Sequence:
MAVPPTYADLGKSARDVFTKGYGFGLIKLDLKTKSENGLEFTSSGSANTETTKVTGSLETKYRWTEYGLTFTEKWNTDNTLGTEITVEDQLARGLKLTFDSSFSPNTGKKNAKIKTGYKREHINLGCDMDFDIAGPSIRGALVLGYEGWLAGYQMNFETAKSRVTQSNFAVGYKTDEFQLHTNVNDGTEFGGSIYQKVNKKLETAVNLAWTAGNSNTRFGIAAKYQIDPDACFSAKVNNSSLIGLGYTQTLKPGIKLTLSALLDGKNVNAGGHKLGLGLEFQA
Protein: Developmental protein SEPALLATA 1 (Agamous-like MADS-box protein AGL2) (P29382)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor. Functions with SEPALLATA2/AGL4 and SEPALLATA3/AGL9 to ensure proper development of petals, stamens and carpels, and to prevent the indeterminate growth of the flower meristem. Forms a heterodimer via the K-box domain with AGAMOUS, that could be involved in genes regulation during floral meristem development.
Subcellular location: Nucleus.
Interaction partners:
- Floral homeotic protein AGAMOUS
- MADS-box protein
- Agamous-like MADS-box protein AGL8
- Floral homeotic protein APETALA 3
- Floral homeotic protein APETALA 1
Sequence:
MGRGRVELKRIENKINRQVTFAKRRNGLLKKAYELSVLCDAEVALIIFSNRGKLYEFCSSSNMLKTLDRYQKCSYGSIEVNNKPAKELENSYREYLKLKGRYENLQRQQRNLLGEDLGPLNSKELEQLERQLDGSLKQVRSIKTQYMLDQLSDLQNKEQMLLETNRALAMKLDDMIGVRSHHMGGGGGWEGGEQNVTYAHHQAQSQGLYQPLECNPTLQMGYDNPVCSEQITATTQAQAQQGNGYIPGWML
Protein: Cathepsin S (EC 3.4.22.27) (O70370)
Organism: Mus musculus (Mouse)
Function: Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules and MHC class II antigen presentation. The bond-specificity of this proteinase is in part similar to the specificities of cathepsin L.
Subcellular location: Lysosome {ECO:0000250|UniProtKB:P25774}. Secreted {ECO:0000250|UniProtKB:P25774}. Cytoplasmic vesicle, phagosome {ECO:0000250|UniProtKB:P25774}.
Interaction partners:
- H-2 class II histocompatibility antigen gamma chain
- Interleukin-10 receptor subunit alpha
- BH3-interacting domain death agonist
- Myeloperoxidase
- Cathepsin B
- Apoptosis regulator Bcl-2
- Bcl-2-like protein 1
- Cyclic AMP-responsive element-binding protein 1
- Interleukin-10 receptor subunit beta
- Procathepsin L
Sequence:
MRAPGHAAIRWLFWMPLVCSVAMEQLQRDPTLDYHWDLWKKTHEKEYKDKNEEEVRRLIWEKNLKFIMIHNLEYSMGMHTYQVGMNDMGDMTNEEILCRMGALRIPRQSPKTVTFRSYSNRTLPDTVDWREKGCVTEVKYQGSCGACWAFSAVGALEGQLKLKTGKLISLSAQNLVDCSNEEKYGNKGCGGGYMTEAFQYIIDNGGIEADASYPYKATDEKCHYNSKNRAATCSRYIQLPFGDEDALKEAVATKGPVSVGIDASHSSFFFYKSGVYDDPSCTGNVNHGVLVVGYGTLDGKDYWLVKNSWGLNFGDQGYIRMARNNKNHCGIASYCSYPEI
Protein: Cysteine protease ATG4A (EC 3.4.22.-) (AUT-like 2 cysteine endopeptidase) (Autophagy-related cysteine endopeptidase 2) (Autophagin-2) (Autophagy-related protein 4 homolog A) (HsAPG4A) (hAPG4A) (Q8WYN0)
Organism: Homo sapiens (Human)
Function: Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins. The protease activity is required for proteolytic activation of ATG8 family proteins: cleaves the C-terminal amino acid of ATG8 proteins to reveal a C-terminal glycine. Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy. Preferred substrate is GABARAPL2 followed by MAP1LC3A and GABARAP. Protease activity is also required to counteract formation of high-molecular weight conjugates of ATG8 proteins (ATG8ylation): acts as a deubiquitinating-like enzyme that removes ATG8 conjugated to other proteins, such as ATG3. In addition to the protease activity, also mediates delipidation of ATG8 family proteins. Catalyzes delipidation of PE-conjugated forms of ATG8 proteins during macroautophagy. Compared to ATG4B, the major protein for proteolytic activation of ATG8 proteins, shows weaker ability to cleave the C-terminal amino acid of ATG8 proteins, while it displays stronger delipidation activity. Involved in phagophore growth during mitophagy independently of its protease activity and of ATG8 proteins: acts by regulating ATG9A trafficking to mitochondria and promoting phagophore-endoplasmic reticulum contacts during the lipid transfer phase of mitophagy.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q8BGE6}.
Interaction partners:
- Gamma-aminobutyric acid receptor-associated protein
- GABA type A receptor associated protein like 1
- Gamma-aminobutyric acid receptor-associated protein-like 2
- Serine/threonine-protein kinase ULK1
- Serine/threonine-protein kinase ULK2
- Microtubule-associated protein 1 light chain 3 beta
- Ubiquitin-like-conjugating enzyme ATG3
- Ubiquitin-like modifier-activating enzyme ATG7
- Ubiquitin-like protein ATG12
- Microtubule-associated protein 1 light chain 3 alpha
Sequence:
MESVLSKYEDQITIFTDYLEEYPDTDELVWILGKQHLLKTEKSKLLSDISARLWFTYRRKFSPIGGTGPSSDAGWGCMLRCGQMMLAQALICRHLGRDWSWEKQKEQPKEYQRILQCFLDRKDCCYSIHQMAQMGVGEGKSIGEWFGPNTVAQVLKKLALFDEWNSLAVYVSMDNTVVIEDIKKMCRVLPLSADTAGDRPPDSLTASNQSKGTSAYCSAWKPLLLIVPLRLGINQINPVYVDAFKECFKMPQSLGALGGKPNNAYYFIGFLGDELIFLDPHTTQTFVDTEENGTVNDQTFHCLQSPQRMNILNLDPSVALGFFCKEEKDFDNWCSLVQKEILKENLRMFELVQKHPSHWPPFVPPAKPEVTTTGAEFIDSTEQLEEFDLEEDFEILSV