wanglab/gogpt-training-data huggingface dataset:
Protein: Glycylpeptide N-tetradecanoyltransferase 1 (EC 2.3.1.97) (Myristoyl-CoA:protein N-myristoyltransferase 1) (NMT 1) (Type I N-myristoyltransferase 1) (Peptide N-myristoyltransferase 1) (Q9LTR9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins. Can also use decanoyl-CoA and lauroyl-CoA as substrates.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10734119}. Note=Mostly associated to ribosomes. Present to a lower extent in mitochondria.
Interaction partners:
- SWIB complex BAF60b domain-containing protein
- Protein PLASTID MOVEMENT IMPAIRED 2
- Coiled-coil protein
- Putative leucine-rich repeat receptor-like protein kinase At2g19210
- Uncharacterized protein At1g66480
- Mitochondrial fission protein ELM1
- Expressed protein
- Phosphoethanolamine N-methyltransferase 1
Sequence:
MADNNSPPGSVEQKADQIVEANPLVKDDTSLETIVRRFQDSMSEAKTHKFWETQPVGQFKDIGDTSLPEGPIEPATPLSEVKQEPYNLPSVYEWTTCDMNSDDMCSEVYNLLKNNYVEDDENMFRFNYSKEFLRWALRPPGYYQSWHIGVRAKTSKKLVAFISGVPARIRVRDEVVKMAEINFLCVHKKLRSKRLAPVMIKEVTRRVHLENIWQAAYTAGVILPTPITTCQYWHRSLNPKKLIDVGFSRLGARMTMSRTIKLYKLPDAPITPGFRKMEPRDVPAVTRLLRNYLSQFGVATDFDENDVEHWLLPREDVVDSYLVESPETHDVTDFCSFYTLPSTILGNPNYTTLKAAYSYYNVATQTSFLQLMNDALIVSKQKGFDVFNALDVMHNESFLKELKFGPGDGQLHYYLYNYRLKSALKPAELGLVLL
Protein: snRNA-activating protein complex subunit 3 (Small nuclear RNA-activating complex polypeptide 3) (A0A0C4DHH3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDTTYITTNPALSLRDFLADYQKKISGTADEVPFFLQKNPVLVDVSESCSLDLIESPDDSSIAVFQPAADKCRPTFSPPQENQHVPSTFTALSQHKDKSHSPNLHIDACGELELTVRLYRPPRAYHRGFKVEIPVFAEEFVCLGSNYLTELRDKISCVCNGKRFVDISDDPDAPLPSIDTNPGYFFINDTFYNDQRNPDNPDYSKTVLQWAARANGVNGETLKVESMEGKRFIDLTVSPGSPLHYLHHGNCEHLFVISQVEVLTPLSKRPDRSLYPYPHAFSTFNRRTCYMCGIRSYSFIVNQSRRQLHDPSYLCRRCFLSFFYVDGVKLGQFKAYRMYDHVELEGEEEDIKQQNLPS
Protein: Non-structural protein (I6W9F2)
Organism: Phlebovirus JS2010-014
Interaction partners:
Sequence:
MSLSKCSNVDLKSVAMNANTVRLEPSLGEYPTLRRDLVECSCSVLTLSMVKRMGKMTNTVWLFGNPKNPLHQLEPGLEQLLDMYYKDMRCYSQRELSALRWPSGKPSVWFLQAAHMFFSIKNSWAMETGRENWRGLFHRITKGRRYLFEGDMILDSLEAIEKRRLRLGLPDILITGLSPILDVALLQIESLARLRGMSLNHHLFTSSSLRKPLLDCWDFFIPIRKKKTDGSYSVLDEDDEPGVLQGYPYLMAHYLNRCPFHNLIRFDEELRTAALNTIWGRDWPAIGDPPKEV
Protein: Probable diguanylate cyclase DgcC (DGC) (EC 2.7.7.65) (P0AAP1)
Organism: Escherichia coli (strain K12)
Function: A probable diguanylate cyclase. The last member of a cascade of expressed proteins, its expression requires DgcM. DgcC production induces biosynthesis of cellulose in some E.coli isolates, but not in K12 strains. Cyclic-di-GMP is a second messenger which controls cell surface-associated traits in bacteria.
Subcellular location: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cyclic di-GMP phosphodiesterase PdeL
- Probable cyclic di-GMP phosphodiesterase PdeD
- Cellulose synthase catalytic subunit
- Probable cyclic di-GMP phosphodiesterase PdeN
- Probable cyclic di-GMP phosphodiesterase PdeC
- Probable cyclic di-GMP phosphodiesterase PdeG
- Probable cyclic di-GMP phosphodiesterase PdeB
- Cyclic di-GMP phosphodiesterase PdeH
- Probable cyclic di-GMP phosphodiesterase PdeK
- Oxygen sensor protein DosP
Sequence:
MFPKIMNDENFFKKAAAHGEEPPLTPQNEHQRSGLRFARRVRLPRAVGLAGMFLPIASTLVSHPPPGWWWLVLVGWAFVWPHLAWQIASRAVDPLSREIYNLKTDAVLAGMWVGVMGVNVLPSTAMLMIMCLNLMGAGGPRLFVAGLVLMVVSCLVTLELTGITVSFNSAPLEWWLSLPIIVIYPLLFGWVSYQTATKLAEHKRRLQVMSTRDGMTGVYNRRHWETMLRNEFDNCRRHNRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIGRFGGDEFAVIMSGTPAESAITAMLRVHEGLNTLRLPNTPQVTLRISVGVAPLNPQMSHYREWLKSADLALYKAKKAGRNRTEVAA
Protein: Meiotic driver cw27 (A0A1X9Q9H1)
Organism: Schizosaccharomyces pombe (Fission yeast)
Function: Promotes unequal transmission of alleles from the parental zygote to progeny spores by acting as poison/antidote system where the poison and antidote proteins are produced from the same locus; the poison component is trans-acting and targets all spores within an ascus whereas the antidote component is spore-specific, leading to poisoning of all progeny that do not inherit the allele.
Subcellular location: [Isoform 1]: Spore membrane {ECO:0000250|UniProtKB:A0A218N034}; Multi-pass membrane protein {ECO:0000255}. Vacuole {ECO:0000250|UniProtKB:A0A218N034}. Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Note=Contained within spores expressing the isoform and localizes isoform 2 to the vacuole. {ECO:0000250|UniProtKB:A0A218N034}.; SUBCELLULAR LOCATION: [Isoform 2]: Ascus epiplasm {ECO:0000250|UniProtKB:A0A218N034}. Cytoplasm {ECO:0000250|UniProtKB:A0A218N034}. Spore membrane {ECO:0000250|UniProtKB:A0A218N034}; Multi-pass membrane protein {ECO:0000255}. Vacuole {ECO:0000250|UniProtKB:A0A218N034}. Endoplasmic reticulum {ECO:0000250|UniProtKB:A0A218N034}. Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes in trans to all spores within an ascus. Localization to the spore vacuole is dependent on isoform 1. {ECO:0000250|UniProtKB:A0A218N034}.
Interaction partners:
Sequence:
MKNKYYPLRSSMDELSTKNDNEIDLEKGPLPEYNSEDGSTLPPYSENLNLKDPKQMGQSITKLFNWNKSTTPPDYDENRLLITDEGNNPPNTHRENHSSGTTDNSSPFLIKLLISFTSIILFNAPAVCYLKYKDAFFKNYGAAEWTLIGFWCASSLIIFTFSWCFYETWTKAVKVTVIFLAQCIKVTAISLAKCVKVISIGLFNIRREMMIIIWILWLIICCILFGCVKDGRLNLNKALICSTCTISAVLFLIVSSVCIPIWTLWRALSGMLQVLGIHGIIALLVNGLMSLFGKHFGWRGYEIEGFVLFFTGNALFLYEMERPGVLKRMRNTTRNVIGFILGGIANAIGGIANAIGGANDNNDIPLGELEVESEV
Protein: N-acetylglucosamine-6-sulfatase (EC 3.1.6.14) (Glucosamine-6-sulfatase) (A0A8J8YF65)
Organism: Rattus norvegicus (Rat)
Subcellular location: Lysosome {ECO:0000256|PIRNR:PIRNR036666}.
Interaction partners:
Sequence:
MHRHTRTPLKKTKALIGEKGMTFSSAYVPSALCCPSRASILTGKYPHNHHVVNNTLEGNCSSKSWQKIQEPYTFPAILKLVCGYQTFFAGKYLNEYGAPDAGGLEHVPLGWSYWYALEKNSKYYNYTLSINGKARRHGENYSVDYLTDVLANLSLDFLDYKSNSEPFFMMISTPAPHSPWTAAPQYQKAFPNVIAPRNKNFNIHGTNKHWLIRQAKTPMTNSSIKFLDDAFRRRWQTLLSVDDLVEKLVKRLDSTGELDNTYIFYTSDNGYHTGQFSLPIDKRQLYEFDIKVPLLVRGPGIKPNQTSKMLVSNIDLGPTILDLAGYDLNKTQMDGTSLLPILKGDGNLTWRSDVLVEYQGEGRNVTDPTCPSLSPGVSQCFPDCVCEDAYNNTYACVRTLSSMWNLQYCEFDDQEVFVEVYNITADPDQITNIAKSIDPELLGKMNYRLMMLQSCSGPTCRTPGVFDPGYRFDLRLMFSNHGSIRMRRFSKHPL
Protein: Methyl-CpG binding domain protein 2 (X6RBL6)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MRAHPGGGRCCPEQEEGESAAGGSGAGGDSAIEQGGQGSALAPSPVSGVRREGARGGGRGRGRWKQAGRGGGVCGRGRGRGRGRGRGRGRGRGRGRPPSGGSGLGGDGGGCGGGGSGGGGAPRREPVPFPSGSAGPGPRGPRATESGKRMDCPALPPGWKKEEVIRKSGLSAGKSDVYYFSPSGKKFRSKPQLARYLGNTVDLSSFDFRTGKMMPSKLQKNKQRLRNDPLNQNKFVCTFLL
Protein: Uncharacterized protein YFR016C (P43597)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Protein SPA2
- Protein BNI1
- Bud site selection protein 6
Sequence:
MVESLTVENQEHNVQPPSVTSAGDSYSTLATDLPLPSTNDIIESRDQLTESDLDEAINATENFAQELSSQRKSSKLKGHKKKNQGQIKANRDRDTIVKLSSSVGETEEASTRDAISHDLERKDDVIEIATDTINDATESPTQIPIDVNVVIKETSTNNVAEGTENVPPIKESTGIEVGNSPITRRKKNKKKKTTNRRGRNSSNPADTTDLSKQSTLDSILVGIEEYLQEDGSKNEDIKVNIVQDEPVNVEKMDIRTRNESSDKTFDIDVPNKDNVDETSSKSENNINEEKAEHTLPREENEILNVNEGNAASFKHQLEPHGLEAGDENGQASTKDVESESLTKNGFNFKENESKHLKAGEKQQTESDRDGISPSVLAKNQKETEIGKEDHVFEQKDKEDEKCRKELSVNHENNMSHNFNAAGSDSIIPPETERETYDDETMGPTKRISDNEKNLQHGTNDISVEVEKEEEEEEEEEENSTFSKVKKENVTGEQEAVRNNEVSGTEEESTSKGEEIMGGDEKQSEAGEKSSIIEIEGSANSAKISKDNLVLEDEAEAPTQENKPTEVVGEIDIPDAPRDDVEIVEAVEKNIIPEDLEVAKEDQEGEQVKLDEPVKAMKDDKIAMRGAESISEDMKKKQEGTAELSNEKAKKEVDETARESAEGVEVEKSKTPESPKVVKRCTSGRPEDLQINERDPEVLKEDVRVPDEDVKPEIATTIENSEEEDPKSQRVQISTEQAETTQKDMGDVGSTTSFKEEEKPKRFEITQEGDKITGKDTNHEHGEATEAASENSKASDVGTAEKYIEPSSESVKKDTEEDAEVENSEKTEFIKVKAELENLDAPKEAEVTAELNKENEDVEVDTEEDAEVENSEKTEFIKVKAELGNLDAPKEAEVTAELNKENEDVEVAATSKEDIETKCSEPAETPIEDGTCTEAEVSKKDAEAVTKEDENMENSKIAEALKDVTGDQEIDDINISDEFQRTVELPELEKQDIKDNKGEDKELEVEETEKETSLPDLVVEENITEEKNEIKQEEEEVSQLDFNETESISKEAPNNDENGFEDQSTRENPKKASADDIFKDILDETNEFLEQLKIVDDSELNALLQSLDAKDSTTQTTEQSKKNNDKPQDVITTSEIRKLNEKEPVYIYTSLAGGGFHMIPRTNRLSTILTANRIPFTYRDLGTDDEARKVWKTFSKGRSLPGVVRGHNDLIGNWEEIEEANEDYKLRELIYDTI
Protein: peptidylprolyl isomerase (EC 5.2.1.8) (Q387V4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MYGVECFRPLGLAAFMLAVLSVVRVATSEDDPNKLTPQERIDRYRKRVARSFLLKMAEEPGAMTLPSGVVVHVLNRGGGGRSAAVDDECTVHYTGTLKDGTVFDSSRDRGQPFKLKLGQVIVGWQEVLQLMRPGDRWKVFIPPEHGYGARGAGPKIPPHSALVFDMELISIEGGGNGRTEKEVEEVLKGYAGKGDL
Protein: DEAD-box ATP-dependent RNA helicase 3, chloroplastic (EC 3.6.4.13) (Protein EMBRYO DEFECTIVE 1138) (Q8L7S8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Nuclear genome-encoded factor involved in ribosome biogenesis in chloroplasts. Binds specific group II introns in chloroplasts and facilitates their splicing. Is required for rRNA maturation in plastids and may contribute to the assembly of the large (50S) ribosomal subunit. Required for normal development of chloroplasts. Required for the expression of transcripts encoding plastid-localized enzymes involved in abscisic acid (ABA) biosynthesis. Required for maintenance of ABA levels and response to salt stress. Possesses RNA chaperone activity for proper splicing of introns in chloroplasts. Essential for chloroplast function and abiotic stress responses.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:18431481}. Plastid, chloroplast stroma {ECO:0000269|PubMed:23227895}.
Interaction partners:
- Probable pre-mRNA-splicing factor ATP-dependent RNA helicase DEAH2
- DExH-box ATP-dependent RNA helicase DExH15 chloroplastic
- Pescadillo homolog
- RNA helicase
- Regulator of nonsense transcripts 1 homolog
- At4g39040
- U11/U12 small nuclear ribonucleoprotein 31 kDa protein
- Small RNA-binding protein 11
- Pentatricopeptide repeat-containing protein At2g41720
- Pentatricopeptide repeat-containing protein At5g04810, chloroplastic
Sequence:
MASTVGVPSLYQVPHLEISKPNSKKRSNCLSLSLDKPFFTPLSLVRRTRRIHSSSLLVPSAVATPNSVLSEEAFKSLGLSDHDEYDLDGDNNNVEADDGEELAISKLSLPQRLEESLEKRGITHLFPIQRAVLVPALQGRDIIARAKTGTGKTLAFGIPIIKRLTEEAGDYTAFRRSGRLPKFLVLAPTRELAKQVEKEIKESAPYLSTVCVYGGVSYTIQQSALTRGVDVVVGTPGRIIDLIEGRSLKLGEVEYLVLDEADQMLAVGFEEAVESILENLPTKRQSMLFSATMPTWVKKLARKYLDNPLNIDLVGDQDEKLAEGIKLYAIATTSTSKRTILSDLITVYAKGGKTIVFTQTKRDADEVSLALSNSIATEALHGDISQHQRERTLNAFRQGKFTVLVATDVASRGLDIPNVDLVIHYELPNDPETFVHRSGRTGRAGKEGSAILMHTSSQKRTVRSLERDVGCHFEFISPPTVGDLLESSADQVVATLNGVHPDSIKFFSATAQKLYEEKGTDALAAALAHLSGFSQPPSSRSLLSHEKGWVTLQLIRDPTNARGFLSARSVTGFLSDLYRTAADEVGKIFLIADDRIQGAVFDLPEEIAKELLEKDVPEGNSLSMITKLPPLQDDGPSSDNYGRFSSRDRMPRGGGGSRGSRGGRGGSSRGRDSWGGDDDRGSRRSSGGGSSWSRGGSSSRGSSDDWLIGGRSSSSSRAPSRERSFGGSCFICGKSGHRATDCPDKRGF
Protein: Apyrase 1 (AtAPY1) (EC 3.6.1.5) (ATP-diphosphatase) (ATP-diphosphohydrolase) (Adenosine diphosphatase) (ADPase) (NTPDase) (Nucleoside triphosphate diphosphohydrolase 1) (Q9SQG2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the hydrolysis of phosphoanhydride bonds of nucleoside tri- and di-phosphates. Substrate preference is ATP > ADP. Functions with APY2 to reduce extracellular ATP level which is essential for pollen germination and normal plant development. Plays a role in the regulation of stomatal function by modulating extracellular ATP levels in guard cells.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:22430844}; Single-pass type II membrane protein {ECO:0000269|PubMed:22430844}. Membrane {ECO:0000305|PubMed:22430844}; Single-pass type II membrane protein {ECO:0000305|PubMed:22430844}. Note=As cell membrane protein, the functional domain could be at the extracellular side.
Interaction partners:
- Probable apyrase 6
- At5g66005
- Probable apyrase 3
- Probable apyrase 5
- Probable apyrase 4
- Adenylosuccinate synthetase, chloroplastic
- At1g72880
- GMP synthase
- Apyrase 2
- Inosine triphosphate pyrophosphatase
Sequence:
MTAKRAIGRHESLADKVHRHRGLLLVISIPIVLIALVLLLMPGTSTSVSVIEYTMKNHEGGSNSRGPKNYAVIFDAGSSGSRVHVYCFDQNLDLVPLENELELFLQLKPGLSAYPNDPRQSANSLVTLLDKAEASVPRELRPKTPVRVGATAGLRALGHQASENILQAVRELLKGRSRLKTEANAVTVLDGTQEGSYQWVTINYLLRTLGKPYSDTVGVVDLGGGSVQMAYAIPEEDAATAPKPVEGEDSYVREMYLKGRKYFLYVHSYLHYGLLAARAEILKVSEDSNNPCIATGYAGTYKYGGKAFKAAASPSGASLDECRRVAINALKVNNSLCTHMKCTFGGVWNGGGGGGQKKMFVASFFFDRAAEAGFVDPNQPVAEVRPLDFEKAANKACNMRMEEGKSKFPRVEEDNLPYLCLDLVYQYTLLVDGFGLKPSQTITLVKKVKYGDYAVEAAWPLGSAIEAVSSP
Protein: SSD domain-containing protein (G5ECF2)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MSSSYFGASGPDPISRQSPAAVRFQRKVSTGSAPTVPPPAVPPPESSADEEEPRASSNNNYSSTSTVAAPTREPTRVSTLKREEKEKKQKERMERERRELEEKRVQEDEMKKEEHNHTVHPSLGERTSYVEEPPSTTTTLDRRDRKAEKALVRRITNEMQMATYVQQIDLSTVKQPVGAYTQGVFRIRMLRFAEAILRRTFWALGKFIANHKIVSILVALLCFATAFILPTLHKEHLYIDLPFSHILGSDSDVISNGIGISPKMQEFNSSNPAFSCMKWRDSNRFAVLLRTMASRDTILRKDAVLAYTALKKKLDHFPVEKREFMTQCSLECETDKDMVDRIIKKSPQVALTYPETFVSMSKDSTNLTRVYLGAAIGGVETDTDGAISKATSLLMNFELKDDLTGKEHNSWHRHFEDQTRLTAASNISLMSWSPETFKDTVVASLKDQYWCLQFCVIILFVFCFLGSFGINAYQSKPCLGIMIFITLVVGSITGLSMQFYRDLPVDPLVYPICFVTIGIGLLWLFQLQFSWSRYSSAAVHPTEKIAFILAHDAPGIAASAVVIVLTFLAMGAAIQNGHMVSSFLGIASSVAILLVFTVFFISVFVFIGGSREARGVKWYQIFKTGDTHFTAPQLASFDSASLFSLHDRLLDARPCASRAVGAFVISPKIRYPIIMLCTAYVFFAIYGFYNTGIDIKEEYFLPAGSSEKSFIEQYRDQFGKTTQFVELTIESSIEYHDHEVQNNIFDIMDFAIAEGYATRAVNWLAEFAKFEKASIYDVNPDTFVPVVNLVFLPSETYRKYTSDIVMDRFQTQIIKSRMYLELTAKGFAERTSFVDTILKKAAAKGIPLSVDIPSSMSLRHDISVFTSGMLAFGVAIVMLFFVSLLLLGQPALTVMLLITSIAVLGETVGYAYFWSVPMNIVTLTMALAGNALTCVIVIAFCYSYSMSGKSQIRAGVRIQYTFQATLVPVLFACIVPVLTFLPLLYVDVPVVNHLFKIVVLNATASLIHYLFFLPNMMLAFSERFGFSCTSFQCAELCCDMDDESSIYYIPTGGRAIHPEGLYHHPSYTYTVPKPLMNAPPPHYLAIAAPPVNSIYGQTEYTSRGEMKRVSRRNRRHSESSIGETENDGTPGRDRESRRRRQRRAVSRDSEIYEDLPSPRAVNSSRSTSPRRQQPGSMRRPNNHHSGSQNPRPQAFHYDEGAQWRPYVQPSPYMFYPGPVYGQQQRR
Protein: Tetraspanin (Q1L9G6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane {ECO:0000256|RuleBase:RU361218}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU361218}. Secreted, extracellular exosome {ECO:0000256|ARBA:ARBA00004550}.
Interaction partners:
- SLAIN motif-containing protein-like
- Sidekick cell adhesion molecule 2a.
- Immunoglobulin superfamily, member 8.
- Shroom family member 2a.
- Meiotic nuclear division protein 1 homolog
- Clavesin-2
- Band 4.1-like protein 3a isoform 1
Sequence:
MMSKSGLSSGEQCIKYIIFFFNFMLWLAGTGVLAVGLWLRFDAKTKEFFTAENGQTVFLTGVYILIVAGAVMMVVGFLGCCGAIKESACMLGLFFMFLLVIFAAEVAAGIWGLSNKDKIVSDIQQFYTQTVKNYKESPDGPLKETLTAIHFSLQCCGPTGLVTDGVSVTCPKQEGLANVITTGCSSVIQDMFNSRLHVIGGVGIGIGVIMVFGMIFSMLLCCAIRRTRDIV
Protein: Protein pelota homolog (hPelota) (Protein Dom34 homolog) (Q9BRX2)
Organism: Homo sapiens (Human)
Function: Cotranslational quality control factor involved in the No-Go Decay (NGD) pathway. In the presence of ABCE1 and HBS1L, is required for 48S complex formation from 80S ribosomes and dissociation of vacant 80S ribosomes. Together with HBS1L and in presence of ABCE1, recognizes stalled ribosomes and promotes dissociation of elongation complexes assembled on non-stop mRNAs; this triggers endonucleolytic cleavage of the mRNA, a mechanism to release non-functional ribosomes and to degrade damaged mRNAs as part of the No-Go Decay (NGD) pathway. As part of the PINK1-regulated signaling, upon mitochondrial damage is recruited to the ribosome/mRNA-ribonucleoprotein complex associated to mitochondrial outer membrane thereby enabling the recruitment of autophagy receptors and induction of mitophagy.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:21448132}.
Interaction partners:
- HBS1-like protein
- Ubiquitin-like protein FUBI
- Small ribosomal subunit protein RACK1
- ATP-binding cassette sub-family E member 1
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein eS6
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein uS12
- Ubiquitin-ribosomal protein eS31 fusion protein
- Large ribosomal subunit protein uL3
Sequence:
MKLVRKNIEKDNAGQVTLVPEEPEDMWHTYNLVQVGDSLRASTIRKVQTESSTGSVGSNRVRTTLTLCVEAIDFDSQACQLRVKGTNIQENEYVKMGAYHTIELEPNRQFTLAKKQWDSVVLERIEQACDPAWSADVAAVVMQEGLAHICLVTPSMTLTRAKVEVNIPRKRKGNCSQHDRALERFYEQVVQAIQRHIHFDVVKCILVASPGFVREQFCDYLFQQAVKTDNKLLLENRSKFLQVHASSGHKYSLKEALCDPTVASRLSDTKAAGEVKALDDFYKMLQHEPDRAFYGLKQVEKANEAMAIDTLLISDELFRHQDVATRSRYVRLVDSVKENAGTVRIFSSLHVSGEQLSQLTGVAAILRFPVPELSDQEGDSSSEED
Protein: GPI mannosyltransferase 3 (EC 2.4.1.-) (GPI mannosyltransferase III) (GPI-MT-III) (Glycosylphosphatidylinositol-anchor biosynthesis protein 10) (P30777)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the third mannose to Man2-GlcN-acyl-PI during GPI precursor assembly.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- GPI mannosyltransferase 2
- GPI mannosyltransferase 1
- Glycosylphosphatidylinositol anchor biosynthesis protein 11
- GPI ethanolamine phosphate transferase 3
- GPI ethanolamine phosphate transferase 1
- Protein PBN1
- N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
- GPI transamidase component GPI16
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit GPI15
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit GPI19
Sequence:
MAHEVHRIKPKLGRTQIFWVFLAFRVLNAVLTRTFFQADEFWQALEPAHWKAFKYGELTWEWKFGVRSYLFPMIFELTYRLVSLSSILLHYALLLLSTIGSDLLILLLPKYELSWQVAEDLKRLPFDVTRSFEYYGVIYAPKIVMAVLASIGEYYIVRFVQKLYLLTLDKRNEKEEEERRSGLSEITKFALLLSLTNFFNCFFITRTFINSFEMILTSIALYYWDWTGGQMIKESSFTKSLIFAFLACLQRPSSGLIWVIPSISLILNLVGKKQYHLLFITFSKVLRSFFLVFTANAIIDMYFYEKVTFPFFRFLKFNFTTPLSKFYGVAPWHFHFFQSLPIVLGASIPAFAFGLFFPLSKRSFPKKYLNPFFQVKLTILLNLLVYSTLPHKEFRFIFPLQPLFILISSFGLLRLDRDYWKRLSGLKSLLWLVPFVSVFIALLLDTFHESGSIEVMKFLHEEPEIDSLGFIMPCHSTPGQSYLHRSDIQDLWSITCNPPLHLLGDPEAYSKLETYMDESDHLYDDISAFIYKNFPPPFRKDLRSPGKTYSHEWPTYLVVFEHMENAFLKDFLKDSSYIEYNRFFNSLAHWDSRRSGDIIIYYKLPFDYSDIPAADI
Protein: At1g32160/F3C3_6 (Beta-casein (DUF760)) (Q9FVR1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- At4g33110
- At1g63610
- At5g52960
- Electron transporter, putative
- AT3g29240/MXO21_9)
- Pentatricopeptide repeat
- Thioredoxin domain-containing protein
- ARM repeat superfamily protein
- ATP-dependent Clp protease adapter protein CLPS1
- Uncharacterized protein At3g49140
Sequence:
MQAIGSSHGRRLCFNHYLSDSFSKFLSPSSSPSLLPQRCHSFCIPKLGSSSTNENGRGRSVTVRASGDEDSNENFAPLAPVELESPVGQLLEQILRTHPHLLPVTVDEQLEKFAAESESRKADSSSTQDILQKRISEVRDKERRKTLAEIIYCLVVHRFVEKGISMIPRIKPTSDPAGRIDLWPNQEEKLEVIHSADAFEMIQSHLSSVLGDGPAVGPLSSIVQIGKIKLGKLYAASAMYGYFLRRVDQRYQLERTMNTLPKRPEKTRERFEEPSPPYPLWDPDSLIRIQPEEYDPDEYAIQRNEDESSSYGLRSYVTYLDSDTLQRYATIRSKEAMTLIEKQTQALFGRPDIRILEDGKLDTSNDEVLSLSVSGLAMLVLEAVAFGSFLWDSESYVESKYHFLKA
Protein: DEAD-box ATP-dependent RNA helicase 17 (EC 3.6.4.13) (Q7XJN0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- rRNA biogenesis protein RRP5
- Ribosome biogenesis protein BOP1 homolog
- DEAD-box ATP-dependent RNA helicase 16
- DEAD-box ATP-dependent RNA helicase 32
- DEAD-box ATP-dependent RNA helicase 13
- ATP-dependent RNA helicase DEAH13
- Nucleolar complex-associated protein 2
- Protein REBELOTE
- Protein SLOW WALKER 2
- U3 small nucleolar RNA-associated protein 18 homolog
Sequence:
MKRAQQSARETKQEAKDASKAKSGLFASCSFSSLGLDTKLSDQLKERMGFEAPTLVQAQAIPVILSGRDVLVNAPTGTGKTIAYLAPLIHHLQGHSPKVDRSHGTFALVIVPTRELCLQVYETLEKLLHRFHWIVPGYVMGGEKKAKEKARLRKGISILIATPGRLLDHLKNTASFVHKNLRWVIFDEADSILELGYGKEIEQIIKLLGSGQNEQGEEDDIVPKGIQKQNLLLSATLNDKVNDLAKLSLDDPVMIGLDNTKLQQNLSIESPAAPDSDAEDMVIHVNKSANPLSEDYGIPSQLVQRYLRVPCGARLVALLSVLKNLFEREASQKVVVFFSTRDAVDFHYSLLSEFQWPPNSETEEEGTKELFLKCKTFRLHGSMEQEDRRSAFGTFKTEKQAVLLSTDVAARGLDFPKVRCIIQYDCPGEATEYVHRVGRTARIGEKGEALLFLQPIEIDYLKELKKHGASLTEYPLMKVLDKFPIPGNMPRIKKVLSLESHPWVISLQRALESLTYAEPKMKSLAKNAFVSWVRGYAAHKGELKSIFVVKKLHLGHVAKSFALREQPSLVGKSHHKETMKRKRDERQKGQQGKKRKKMSGTGNRSTQKT
Protein: Seipin-2 (AtSEIPIN2) (F4I340)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in lipid metabolism and lipid droplet (LD) morphology, number, and size. Supports the formation of small-sized LDs and modulates triacylglycerol accumulation. Induces probably a reorganization of the endoplasmic reticulum into LD-forming domains.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:26362606}; Multi-pass membrane protein {ECO:0000255}. Note=Localized to the lipid droplet-forming sites. {ECO:0000269|PubMed:26362606}.
Interaction partners:
- Voltage-dependent L-type calcium channel subunit
- Protein C2-DOMAIN ABA-RELATED 2
- REF/SRPP-like protein At3g05500
- REF/SRPP-like protein At1g67360
- Transmembrane 9 superfamily member 8
- Alpha/beta-Hydrolases superfamily protein
- Oleosin 18.5 kDa
- G-box-binding factor 1
- Glycine-rich domain-containing protein 1
Sequence:
MDSESESESNPSTTDEFDRFLDAPDEFYYDCLPIRSNSHQPSSLLRRRKSAHRRDLISSDIETEPSSSSDGFDVGEKSSYVEKNAELRGDIDTSDVIESTKDSIDLSSEKENDLDVISSSGNDMDVIDSGRNRVDPFQEESTVTTVSSDDQGDDDYAGSVPQFREPPNSTEWSLLGFLVGLVIKAIEFQVSFMTSLLTFPPWLLRNCFLFFFDPFSTIRFGRRFLMARVAGISDMIFGYMNPFRLKDTKQMLSIVCKFGWGMFWAVYVGIVLFGLLVSSLMIGGYVINRIADKPFEVKETLNFDYTKNSPEAYVPISSCAGVECEGSCKESNEMSKIRGLRVIPRDQKLDIILSMTLPESAYNKNLGMFQVRVDFLSVDGQTIASIRRPCMLRFRSEPIRLVQTFFKVVPLVTGYVSEIQTLSLKLKGFVEKDIPTACLKIIIEQRAEFRPGAGIPELYDASLSVESGLPFFRKIIWKWRKTLFVWISMSLFITELLFTLVCCRPLIIPRTQPRDRSPSNPTGVWR
Protein: Protein mono-ADP-ribosyltransferase PARP16 (EC 2.4.2.-) (ADP-ribosyltransferase diphtheria toxin-like 15) (Poly [ADP-ribose] polymerase 16) (PARP-16) (Q7TMM8)
Organism: Mus musculus (Mouse)
Function: Intracellular mono-ADP-ribosyltransferase that plays a role in different processes, such as protein translation and unfolded protein response (UPR), through the mono-ADP-ribosylation of proteins involved in those processes. Acts as an inhibitor of protein translation by catalyzing mono-ADP-ribosylation of ribosomal subunits, such as RPL14 and RPS6, thereby inhibiting polysome assembly and mRNA loading. Mono-ADP-ribosylation of ribosomal subunits is promoted by NMNAT2. Involved in the unfolded protein response (UPR) by ADP-ribosylating and activating EIF2AK3 and ERN1, two important UPR effectors. May also mediate mono-ADP-ribosylation of karyopherin KPNB1 a nuclear import factor. May not modify proteins on arginine or cysteine residues compared to other mono-ADP-ribosyltransferases.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8N5Y8}; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:Q8N5Y8}.
Interaction partners:
- Protein mono-ADP-ribosyltransferase PARP4
- Protein mono-ADP-ribosyltransferase PARP10
- Protein mono-ADP-ribosyltransferase PARP3
- Protein mono-ADP-ribosyltransferase PARP14
- Protein mono-ADP-ribosyltransferase PARP12
- Poly [ADP-ribose] polymerase 2
- Protein mono-ADP-ribosyltransferase PARP11
- Protein mono-ADP-ribosyltransferase PARP9
Sequence:
MQLSNRAAAREAASRDVLAADLRCSLFASALQSYKRDSVLRPFPASYARHDCKDFEALLADTGRLPNLKELLQSSRDTDKQAWDLVSWILSSKILTIHSAKKAEFEKIQQLTGAPHTPVPTPDFLFEIEYFDPANSRFYETKGERDLIYAFHGSRLENFHSIIHNGLHCHLNKTSLFGEGTYLTSDLSLALIYSPHGHGWQHSLLGPILSCVAVCEVIDHPDVKCQIKKKDSKEIDRSRARIKHSEGGEIPPKYFVVTNNQLLRVKYLLVYSQKQPKRASSQLSWLSSHWFVIMMSLYLLLLLIVSVTNSSVFHHFWNRVKR