wanglab/gogpt-training-data huggingface dataset:
Protein: Small ribosomal subunit protein uS19c (30S ribosomal protein S19, chloroplastic) (P0C479)
Organism: Oryza sativa subsp. indica (Rice)
Function: Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
Subcellular location: Plastid, chloroplast.
Interaction partners:
- Large ribosomal subunit protein uL16c
- Small ribosomal subunit protein uS12cz/uS12cy
- Small ribosomal subunit protein uS14c
- Uncharacterized protein
- Large ribosomal subunit protein uL5c
- Small ribosomal subunit protein uS2c
- Small ribosomal subunit protein mS33
- Large ribosomal subunit protein mL46
- Small ribosomal subunit protein uS11c
- Large ribosomal subunit protein bL34m
Sequence:
MTRKKTNPFVAHHLLAKIEKVNMKEEKETIVTWSRASSILPAMVGHTIAIHNGKEHIPIYITNPMVGRKLGEFVPTRHFTSYESARKDTKSRR
Protein: RRM domain-containing protein (D5MCQ8)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MNASSAPQQQQQQQQPQQGQAPQQQQQGPPQHQYQQQRPFHGTNLYIRGLMPNTNDDLLREMCSKYGNIASTKAIMDKATNNCKGYGFVDFESPQAAAAAVDGLNTEGVQAQMAKLQQQEQDPTNLYIANLPLDFTEQMLETELNKFGMVISTRILRTPDNQSRGVGFARMDSKEKCEVIISALNGGRFDTMSKEGPALLIKQADTGRKSKHSMNNPEMLQRMQYPQVYQSYYGYHPAAVYQQHYDVNSLASQMGGMHVGGGNPQANGGGDMYGAHMYGQNAGGQGGQGVGQGGQVFPADESTINGQDNVFTPLLLSSLNLFSLSILSNQSSLQKKTQCAAARAAINTHVHIVSPLPDPQNLLLFLNPKTIVPF
Protein: Threonylcarbamoyl-AMP synthase (TC-AMP synthase) (EC 2.7.7.87) (L-threonylcarbamoyladenylate synthase) (Ribosome maturation factor TsaC) (t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaC) (tRNA threonylcarbamoyladenosine biosynthesis protein TsaC) (P45748)
Organism: Escherichia coli (strain K12)
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosphate. Is also able to catalyze the reverse reaction in vitro, i.e. the formation of ATP from TC-AMP and PPi. Shows higher affinity for the full-length tRNA(Thr) lacking only the t(6)A37 modification than for its fully modified counterpart. Could also be required for the maturation of 16S rRNA. Binds to double-stranded RNA but does not interact tightly with either of the ribosomal subunits, or the 70S particles.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01852}.
Interaction partners:
- tRNA threonylcarbamoyladenosine biosynthesis protein TsaB
- tRNA N6-adenosine threonylcarbamoyltransferase
- Uncharacterized protein YrdD
- Shikimate dehydrogenase
- tRNA threonylcarbamoyladenosine biosynthesis protein TsaE
- Uncharacterized protein YrdB
- Protein Smf
- Protein Smg
- Single-stranded DNA-binding protein
Sequence:
MNNNLQRDAIAAAIDVLNEERVIAYPTEAVFGVGCDPDSETAVMRLLELKQRPVDKGLILIAANYEQLKPYIDDTMLTDVQRETIFSRWPGPVTFVFPAPATTPRWLTGRFDSLAVRVTDHPLVVALCQAYGKPLVSTSANLSGLPPCRTVDEVRAQFGAAFPVVPGETGGRLNPSEIRDALTGELFRQG
Protein: Eukaryotic translation initiation factor eIF-1 (Protein translation factor SUI1) (P32911)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Additional factor that functions in concert with eIF-2 and the initiator tRNA in directing the ribosome to the proper start site of translation.
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 1A
- Eukaryotic translation initiation factor 2 subunit alpha
- Eukaryotic translation initiation factor 3 subunit G
- Eukaryotic translation initiation factor 2 subunit beta
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 3 subunit A
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 5
- Eukaryotic translation initiation factor 2 subunit gamma
Sequence:
MSIENLKSFDPFADTGDDETATSNYIHIRIQQRNGRKTLTTVQGVPEEYDLKRILKVLKKDFACNGNIVKDPEMGEIIQLQGDQRAKVCEFMISQLGLQKKNIKIHGF
Protein: Probable inactive nicotinamidase At3g16190 (Q93Z51)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Does not possess nicotinamidase activity in vitro.
Interaction partners:
- Nicotinate phosphoribosyltransferase 1
- Nicotinate phosphoribosyltransferase 2
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase
- Glutamine-dependent NAD
- Nicotinate-nucleotide pyrophosphorylase [carboxylating], chloroplastic
- COBRA-like protein 11
- Protein PHYLLO
- NAD
- NAD kinase 2, chloroplastic
- Nicotinamide adenine dinucleotide transporter 1, chloroplastic
Sequence:
MAERWRNTALLVIDMQNDFIEEGAVTQVKGGKSIVPNVIRVVELARQRGILVIWVVREHDRQGRDVELFRRHNYSSEKVGPVIKGTVGAELVDGLMINEEDDYKIVKTRFSAFFSTNLHSFLQTSGVTKLVIAGVQTPNCIRQTVFDAVALDYPNVTVITDATAAATPEIHTANILDMKNIGVKTPTLHEWSEELA
Protein: L-serine ammonia-lyase (EC 4.3.1.17) (A0A1D8PGA8)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Tryptophan synthase
- Acetolactate synthase regulatory subunit
- Threonine synthase
- Acetolactate synthase
- Threonine dehydratase
- Serine hydroxymethyltransferase
- low-specificity L-threonine aldolase
- phosphoserine phosphatase
- low-specificity L-threonine aldolase
- Serine hydroxymethyltransferase, cytosolic
Sequence:
MSTSMDLQPYTKLSQPYIQTSLTEVTNILPTKPPCRIFFKNELEQPSGSFKLRGIGHLVHKSIENALKNHSNKTIHVFASSGGNAGLAAAYSAQFYKVKCTVVLPIISKPVVQEKLKSYGARIVLFGNTINEADQHLKNLMSSIDLDSIYPVYCHPFNNPLIWNGHSSLVDEVSQQLDSKDRKLLKGMVCSFGGGGLYNGIYQGMVKNQIRGDILLIETLQAPTLTQSLEADEVITLKSVNSLATSLACSYTTEQSLKYYKDQSLVKSQVELIDDIDSLRACVAFEKCFGKVVEPACGAAMAVVYNKIDLLYKNFKHLQPEDIVVIVVCGGSCTTGSDLKGFEKMIQKSEIKL
Protein: Phospholipid/glycerol acyltransferase domain-containing protein (Q382T1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- 1-acyl-sn-glycerol-3-phosphate acyltransferase protein, putative
- Bifunctional dihydrofolate reductase-thymidylate synthase
- Cleft lip and palate transmembrane protein 1
- VASt domain-containing protein
Sequence:
MEKYRKFGDAATGINPFISMKTPTAFSTLFAAVLFPVRCVIAVVIMSLLFLVDTFNYLFYLLPGLSSLSHLLFGGLQRGLLRGLLFSLGNVSIARVPTSGSLSPSAGDVVVANLQSVWDMCVIEVAEQIPLFVAAFYGGKAGSSPEKSKKDEDGTLFVMKPSPLQRWRVWWHIYNTGTSTFLSTVADDSSNAHSGEALPIDITLLQRRCHRLGVPLVLFAEGSCTNGKGMLNISPIRVGVTPARLLVSALSYDTAALHTVVRPHSVLSYLFSMSASLYGSRDPAWYSPQFPTATARLASVGTDPPAEAVEGVVVVEGTKVRQVLCGISRPRCALNVGLREKRRFVEVFMAQ
Protein: Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 2 (EC 2.8.2.8) (Glucosaminyl N-deacetylase/N-sulfotransferase 2) (NDST-2) (N-heparan sulfate sulfotransferase 2) (N-HSST 2) [Includes: Heparan sulfate N-deacetylase 2 (EC 3.-.-.-); Heparan sulfate N-sulfotransferase 2 (EC 2.8.2.-)] (P52849)
Organism: Homo sapiens (Human)
Function: Essential bifunctional enzyme that catalyzes both the N-deacetylation and the N-sulfation of glucosamine (GlcNAc) of the glycosaminoglycan in heparan sulfate. Modifies the GlcNAc-GlcA disaccharide repeating sugar backbone to make N-sulfated heparosan, a prerequisite substrate for later modifications in heparin biosynthesis. Plays a role in determining the extent and pattern of sulfation of heparan sulfate. Required for the exosomal release of SDCBP, CD63 and syndecan.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Mast cell carboxypeptidase A
- Sulfotransferase 1C3
- Heparan sulfate 2-O-sulfotransferase 1
- Sulfotransferase 1B1
- Sulfotransferase 1C4
- Protocadherin-15
- Exostosin-1
- Exostosin-2
- Heparan-sulfate 6-O-sulfotransferase 1
- D-glucuronyl C5-epimerase
Sequence:
MLQLWKVVRPARQLELHRLILLLIAFSLGSMGFLAYYVSTSPKAKEPLPLPLGDCSSGGAAGPGPARPPVPPRPPRPPETARTEPVVLVFVESAYSQLGQEIVAILESSRFRYSTELAPGRGDMPTLTDNTHGRYVLVIYENLLKYVNLDAWSRELLDRYCVEYGVGIIGFFRAHEHSLLSAQLKGFPLFLHSNLGLRDYQVNPSAPLLHLTRPSRLEPGPLPGDDWTIFQSNHSTYEPVLLASLRPAEPAVPGPVLRRARLPTVVQDLGLHDGIQRVLFGHGLSFWLHKLIFVDAVAYLTGKRLCLDLDRYILVDIDDIFVGKEGTRMKVADVEALLTTQNKLRTLVPNFTFNLGFSGKFYHTGTEEEDAGDDMLLKHRKEFWWFPHMWSHMQPHLFHNRSVLADQMRLNKQFALEHGIPTDLGYAVAPHHSGVYPIHTQLYEAWKSVWGIQVTSTEEYPHLRPARYRRGFIHNGIMVLPRQTCGLFTHTIFYNEYPGGSRELDRSIRGGELFLTVLLNPISIFMTHLSNYGNDRLGLYTFESLVRFLQCWTRLRLQTLPPVPLAQKYFELFPQERSPLWQNPCDDKRHKDIWSKEKTCDRLPKFLIVGPQKTGTTAIHFFLSLHPAVTSSFPSPSTFEEIQFFNSPNYHKGIDWYMDFFPVPSNASTDFLFEKSATYFDSEVVPRRGAALLPRAKIITVLTNPADRAYSWYQHQRAHGDPVALNYTFYQVISASSQTPLALRSLQNRCLVPGYYSTHLQRWLTYYPSGQLLIVDGQELRTNPAASMESIQKFLGITPFLNYTRTLRFDDDKGFWCQGLEGGKTRCLGRSKGRRYPDMDTESRLFLTDFFRNHNLELSKLLSRLGQPVPSWLREELQHSSLG
Protein: V-type proton ATPase proteolipid subunit (Q7Z030)
Organism: Trypanosoma brucei
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Vacuole membrane {ECO:0000256|RuleBase:RU363060}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU363060}.
Interaction partners:
Sequence:
MLSDDTCQPEAVLFGMLGAAASLALSNIGAAYGTAKSGVAVAHLGIVEPSRVMRGIVPVVMAGILGIYGLIVSVIISNNLKLSGYAMFSGFMHLGAGLAAGFASLASGYAIGIVGDICCFAYAKTEKIFVPMILMLIFAEALGLYGLIMALLMNNRATSYTGGCS
Protein: Calcium-dependent lipid binding protein, putative (Q388M5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MEKANELMQRFGELNNPSHIFLAVVIAWLVLRCIYSIGLVLLVEVALVVGAVSYLIRKEGKRTAFNILHAHRLMRDKEFMKTVLERDLPEWLINPSANNVQWLNSLINEMWKPISEATATTVKNCLEPLLETYKPSFIYSMNLKQCTMGSQPFVITGIQYHPSREKESILDVTMTWDSDMDIVIHLDMPGPDMNVHVRRLQLSMQTRVVLFPYVSVWPCFGNMSVSIMKLWMLNFDISAGGVALDAVPAVGSFLDNFFRKTLVGMMQYPKRWTFPIVQGYEMDTSLADSAMGTLRIRFLRANEWYHRYVSDRAKTPYYIKLLMSGEDPKKRLLKSNIYSGLDTTFSDVFSFILYDTELTLHFWMYFDVPGYDVLIGECVVPVKSLVESKGREYTCMMSKTSGSRTTVRSKLLIMPEFLPYNTGGTTTTGSAPQQAPSRAVSESFANSLKSTSDAIVPPSTRSTVPNDDGVENHGGGTLFVTVQRCRNLKNKETIGVSDPYVKLQLRKQTRKSPYISSTLNPDFNFEAALEVYDIRSDVLHISILDKNDLVKDRLMGTLRIMLSQVAAAPGDIIRGDMNLDPEGQISLELKLLRH
Protein: Mrityu, isoform E (X2J8G3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MSNTPSLNSSSSNISSKAPLAQKQDTYSSDSSEEVLETAEERRRRILKERSRLNRPQHNMSGGGAVPKHDIKSPCGASPSCQATGSGMGRLPLPPERITMLVDGVRFTVEQSLLTAHPTTMLGTMFGSGFQFAHTNERGEYDVADGISHLVFRAILEYYKSGVIRCPPTVSVPELKEACDYLLIPFDATTVRCQNLSLLHELSNEGARQQFELFLEDLILPLMVASAQRGDRECHVVVLLEDDMVEWDEEFPPQMGEEYCQTVHSTAMHRFFKYIENRDVAKQVMKDRGLKKIRCGIEGYPTHKEKIRRRPGGRAEVIYSYVQRPFIHMSWEKEEAKSRHVDFQCVKSKSVTNLAEANADPPLELDASGNPIPPIAVANPHPNNAELAAGMAVAPAAIGVAGPAVVVAVDEAAGGVVMLNELDQAAIAVAVGIVDENM
Protein: AT15038p (Q8MSN7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MKRMRSSRLLVLPLILVLILTLLLQPIAVHAKSKKNKSSQSSHHGDSSSSSSSSSSSSGSSSAAASSANDESKPKGGDNGGQHFAMEPQDQTAVVGSRVTLPCRVMEKVGALQWTKDDFGLGQHRNLSGFERYSMVGSDEEGDFSLDIYPLMLDDDAKYQCQVGPGPQGEQGIRSRFAKLTVLVPPEAPKITQGDYLVTTEDREIELECVSQGGKPAAEITWIDGLGNVLTKGIEYVKEPLADSRRITARSILKLAPKKEHHNTTFTCQAQNTADRTYRSAKLLLEVKYAPKVIVSVVGGALAGGKIPEGAEVILSCQADANPHELSYRWFINDELMTGDFTTKMIIHNVSRQYHDAIVKCEVVNAVGKSEQSKKLDISFGPVFRQRPVSVEADLGATVSMRCDVAGNPEPEIEWISENSDQVVGVAAELKLKVSSETAGRYFCKAVVNGFPEIGAEATLYVKRAPIITSHKVQFGGVGGRVKIDCLAFSIPKAEHILWSFEGKIINMSSADPDIYIFEEHHLPEGVRAALIIRDSKATHFGKYNCTVLNS
Protein: Myocyte enhancer factor 2C (A0A1B0GV32)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGRKKIQITRIMDERNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNSTNKLFQYASTDMDKVLLKYTEYNEPHESRTNSDIVETLRKKGLNGCDSPDPDADDSVGHSPESEDKYRKINEDIDLMISRQRLCAVPPPNFEMPVSIPVSSHNSLVYSNPVSSLGNPNLLPLAHPSLQRNSMSPGVTHRPPSAGGLMGGDLTSGAGTSAGNGYGNPRNSPGLLVSPGNLNKNMQAKSPPPMNLGMNNRKPDLRVLIPPGSKNTMPSVNQRINNSQSAQSLATPVVSVATPTLPGQGMGGYPSAISTTYGTEYSLSSADLSSLSGFNTASALHLGSVTGWQQQHLHNMPPSALSQLGACTSTHLSQSSNLSLPSTQSLNIKSEPVSPPRDRTTTPSRYPQHTRHEAGRSPVDSLSSCSSSYDGSDREDHRNEFHSPIGLTRPSPDERESPSVKRMRLSEGWAT
Protein: MFS-type transporter SLC18B1 (Solute carrier family 18 member B1) (Vesicular polyamine transporter) (VPAT) (Q6NT16)
Organism: Homo sapiens (Human)
Function: Proton-coupled polyamine antiporter involved in the translocation of polyamines from cytosol into secretory vesicles prior to their release via exocytosis. Uses the electrochemical proton gradient generated by a V-type proton-pumping ATPase to couple the efflux of protons with the uptake of a polyamine molecule. Facilitates vesicular storage of spermine and spermidine in astrocytes with an impact on glutamatergic neuronal transmission and memory formation (By similarity). Upon antigen stimulation, regulates polyamine accumulation and release in mast cell secretory granules, which in turn potentiates mast cell degranulation and histamine secretion (By similarity).
Subcellular location: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:D3Z5L6}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:D4A9K4}; Multi-pass membrane protein {ECO:0000250|UniProtKB:D4A9K4}. Note=Colocalizes with VAMP3 and VAMP8 in mast cell secretory granules, which are distinct from histamine- and serotonin-containing granules (By similarity). Partly colocalizes with SYP in synaptic vesicles in hippocampal neurons. Colocalizes with SYP and VAMP2 in secretory vesicles of astrocytes (By similarity). {ECO:0000250|UniProtKB:D3Z5L6, ECO:0000250|UniProtKB:D4A9K4}.
Interaction partners:
- Sodium-dependent phosphate transport protein 1
- Monocarboxylate transporter 1
Sequence:
MEALGDLEGPRAPGGDDPAGSAGETPGWLSREQVFVLISAASVNLGSMMCYSILGPFFPKEAEKKGASNTIIGMIFGCFALFELLASLVFGNYLVHIGAKFMFVAGMFVSGGVTILFGVLDRVPDGPVFIAMCFLVRVMDAVSFAAAMTASSSILAKAFPNNVATVLGSLETFSGLGLILGPPVGGFLYQSFGYEVPFIVLGCVVLLMVPLNMYILPNYESDPGEHSFWKLIALPKVGLIAFVINSLSSCFGFLDPTLSLFVLEKFNLPAGYVGLVFLGMALSYAISSPLFGLLSDKRPPLRKWLLVFGNLITAGCYMLLGPVPILHIKSQLWLLVLILVVSGLSAGMSIIPTFPEILSCAHENGFEEGLSTLGLVSGLFSAMWSIGAFMGPTLGGFLYEKIGFEWAAAIQGLWALISGLAMGLFYLLEYSRRKRSKSQNILSTEEERTTLLPNET
Protein: Probable DNA-binding protein SNT1 (SANT domain-containing protein 1) (P25357)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Part of the Set3C complex, which is required to repress early/middle sporulation genes during meiosis.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- SIR4-interacting protein SIF2
- SET domain-containing protein 3
- Probable histone deacetylase HOS2
- Protein HOS4
- Peptidyl-prolyl cis-trans isomerase
- NAD-dependent protein deacetylase HST1
- Suppressor of mar1-1 protein
- Cell division control protein 15
- Transcriptional regulatory protein SIN3
- Meiosis-specific transcription factor NDT80
Sequence:
MGYPPPTRRLGDKKRYHYSNNPNRRHPSAVYSKNSFPKSSNNGFVSSPTADNSTNPSVTPSTASVPLPTAAPGSTFGIEAPRPSRYDPSSVSRPSSSSYSSTRKIGSRYNPDVERSSSTTSSTPESMNTSTITHTNTDIGNSRYSRKTMSRYNPQSTSSTNVTHFPSALSNAPPFYVANGSSRRPRSMDDYSPDVTNKLETNNVSSVNNNSPHSYYSRSNKWRSIGTPSRPPFDNHVGNMTTTSNTNSIHQREPFWKANSTTILKSTHSQSSPSLHTKKFHDANKLDKPEASVKVETPSKDETKAISYHDNNFPPRKSVSKPNAPLEPDNIKVGEEDALGKKEVHKSGREIAKEHPTPVKMKEHDELEARAKKVSKINIDGKQDEIWTTAKTVASAVEVSKESQKELTRSVERKESPEIRDYERAYDPKALKTDVTKLTVDNDNKSYEEPLEKVEGCIFPLPKAETRLWELKNQKRNKIISEQKYLLKKAIRNFSEYPFYAQNKLIHQQATGLILTKIISKIKKEEHLKKINLKHDYFDLQKKYEKECEILTKLSENLRKEEIENKRKEHELMEQKRREEGIETEKEKSLRHPSSSSSSRRRNRADFVDDAEMENVLLQIDPNYKHYQAAATIPPLILDPIRKHSYKFCDVNNLVTDKKLWASRILKDASDNFTDHEHSLFLEGYLIHPKKFGKISHYMGGLRSPEECVLHYYRTKKTVNYKQLLIDKNKKRKMSAAAKRRKRKERSNDEEVEVDESKEESTNTIEKEEKSENNAEENVQPVLVQGSEVKGDPLGTPEKVENMIEQRGEEFAGELENAERVNDLKRAHDEVGEESNKSSVIETNNGVQIMDPKGAVQNGYYPEETKELDFSLENALQRKKHKSAPEHKTSYWSVRESQLFPELLKEFGSQWSLISEKLGTKSTTMVRNYYQRNAARNGWKLLVDETDLKRDGTSSESVQQSQILIQPERPNINAYSNIPPQQRPALGYFVGQPTHGHNTSISSIDGSIRPFGPDFHRDTFSKISAPLTTLPPPRLPSIQFPRSEMAEPTVTDLRNRPLDHIDTLADAASSVTNNQNFSNERNAIDIGRKSTTISNLLNNSDRSMKSSFQSASRHEAQLEDTPSMNNIVVQEIKPNITTPRSSSISALLNPVNGNGQSNPDGRPLLPFQHAISQGTPTFPLPAPRTSPISRAPPKFNFSNDPLAALAAVASAPDAMSSFLSKKENNN
Protein: Trigger factor-like protein TIG, Chloroplastic (EC 5.2.1.8) (Immunophilin TIG) (Peptidyl-prolyl cis-trans isomerase TIG) (PPIase TIG) (Rotamase) (Q8S9L5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase (By similarity).
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Large ribosomal subunit protein bL28c
- Translation elongation factor EF1B/ribosomal protein S6 family protein
- Large ribosomal subunit protein uL23y
- Large ribosomal subunit protein uL23z
- Small ribosomal subunit protein uS9c
- Ribosomal protein L25/Gln-tRNA synthetase, anti-codon-binding domain-containing protein
- Small ribosomal subunit protein uS10c
- Small ribosomal subunit protein uS9m
- Large ribosomal subunit protein uL5c
- Large ribosomal subunit protein bL21c
Sequence:
MELCVISTTTTVKAINPFLPSITRRVSSRLFQSDSVLQFGGRLKKPISRPLDMSCVSRKIGFFGDFMSHGGNFRLFAAASPAVETSVKEDKLPADLKVTETVQANSSVKLSVEVPEIVCEDCYQRVLTEFMKLSKVPGFRPKTRVPENIIVGFVGRQYVLRATVESILKRTLPHAMESVTGRALKDSIQIVSSFPDMEKAYSKLKTLSYEVVVDVVPELKWNPEDGYKNMKVVVELGDEIDAKKACERQLRQKYKSLGALKIVTERGLQVGDLAVVDISATTIDEDGSTGQAIPDAESKGFHFDTEEGNRLLPGFLDAIIGIRAGESKSFTLVFPESWKQESLRGQRAQFTVDCKELFYRDLPTLDDSLADKLLPGCTTLKEVEETLAKRCQEMEQEAKEQATDNAILEQIRKMVEVEIPQSLFEEQGRQFYGARLLEIQGNMKLNEDQLASLSSQKAVNEFLETQRESITNIIKQNIAVGDIFKRENLEFSTDELVKEVENSISEFKKHKQEFDEERVKDQVQEILEGAKVLEWLKDRAEIQYITR
Protein: Plant UBX domain-containing protein 8 (PUX8) (Ara4-interacting protein) (Suppressor of ARA4-induced defect of ypt1) (SAY1) (F4JPR7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Plant UBX domain-containing protein 7
- Cell division control protein 48 homolog A
- Protein OS-9 homolog
- Plant UBX domain-containing protein 1
- AT3g18860/MCB22_3
- Plant UBX domain-containing protein 5
- Plant UBX domain-containing protein 3
- Probable ubiquitin conjugation factor E4
- NPL4-like protein 1
- NPL4-like protein 2
Sequence:
MATPNQEAIDTFISITGASDAVALQKLEEHRGDLNQAVNAYFSEGDRNVVREAPVNDDDEMDIDDVIPAPQSPLSMFNAARTIGRPPFSLLDSDFARRVFDSDPLMPRPPFVSHPREVRQIPIEVKDSSGPSGRSSDAPTIEDVTETAHVQGPVTTQGTVIIDEESDDDIPFAPMGRSRQDRPAGSVANNNNQDYNDIEEEMIRAAIEASKKEAEGSSNPLLEERPLHMEDDDDIAIAVTMSLKSAEEEVLRSQGYKASTSEIGASAVTAAQGPQDTQALNGRLAAPSSPFDDDSDDVDEQPLVRHRPRRAASGSLAPPNADRSRSGSPEEEHASINPAERGSGFPSEWGGISSEEHDEAVMLEAAMFGGIPETGYNHLPFLPPQPRAQPRPPSPSLTAQRLIREQQDDEYVASLQADRDKEMKSIRDAEARQLEEETARKAFLEEEKKKEEEAQRKLEEEQELERQLDAKEASLPKEPQADEENAITLLIRMPDGTRRGRRFLKSDKLQTLFNFIDIARVVKPNTYRLVRPYPRHAFGDGESESTLNDLGLTSKQEALFLELI
Protein: Actin-related protein 2 (Actin-like protein 2) (Q5M7U6)
Organism: Rattus norvegicus (Rat)
Function: ATP-binding component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility. Seems to contact the pointed end of the daughter actin filament. In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA. The Arp2/3 complex promotes homologous recombination (HR) repair in response to DNA damage by promoting nuclear actin polymerization, leading to drive motility of double-strand breaks (DSBs).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P61160}. Cell projection {ECO:0000250|UniProtKB:P61160}. Nucleus {ECO:0000250|UniProtKB:P61160}.
Interaction partners:
- Actin-related protein 3
- Actin-related protein 2/3 complex subunit 3
- Actin-related protein 2/3 complex subunit 2
- Actin nucleation-promoting factor WASL
- Actin nucleation-promoting factor WAS
- Actin related protein 3B
- Actin-related protein 2/3 complex subunit 4
- Actin-related protein 2/3 complex subunit 5
- Actin-related protein 2/3 complex subunit 1B
- Actin-related protein 2/3 complex subunit 1A
Sequence:
MDSQGRKVVVCDNGTGFVKCGYAGSNFPEHIFPALVGRPIIRSTTKVGNIEIKDLMVGDEASELRSMLEVNYPMENGIVRNWDDMKHLWDYTFGPEKLNIDTRSCKILLTEPPMNPTKNREKIVEVMFETYQFSGVYVAIQAVLTLYAQGLLTGVVVDSGDGVTHICPVYEGFSLPHLTRRLDIAGRDITRYLIKLLLLRGYAFNHSADFETVRMIKEKLCYVGYNIEQEQKLALETTVLVESYTLPDGRIIKVGGERFEAPEALFQPHLINVEGVGVAELLFNTIQAADIDTRSEFYKHIVLSGGSTMYPGLPSRLERELKQLYLERVLKGDVEKLSKFKIRIEDPPRRKHMVFLGGAVLADIMKDKDNFWMTRQEYQEKGVRVLEKLGVTVR
Protein: Eukaryotic translation initiation factor 4E-1 (eIF-4E-1) (eIF4E-1) (eIF-4F 25 kDa subunit) (eIF-4F p26 subunit) (mRNA cap-binding protein) (C7SG33)
Organism: Citrullus lanatus (Watermelon) (Citrullus vulgaris)
Function: Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (By similarity). Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures (By similarity). Key component of recessive resistance to potyviruses.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:C6ZJZ3}. Cytoplasm {ECO:0000250|UniProtKB:C6ZJZ3}.
Interaction partners:
Sequence:
MVVEETIKATSTEDLSNTIANQNPRGRGGDEDEELEEGEIVGDDDLDSSNLSAAIVHQPHPLEHSWTFWFDNPSAKSKQATWGASIRPIYTFSTVEEFWSVYNNIHHPSKLALRADLYCFKHKIEPKWEDPVCANGGKWTVNFSRGKSDNGWLYTLLAMIGEQFDCGDEICGAVVNVRSGQDKISIWTKNASNEAAQASIGKQWKEFLDYNDSIGFIFHEDAKKFDRHAKNKYSV
Protein: Extracellular superoxide dismutase [Cu-Zn] 2 (EC-SOD 2) (EC 1.15.1.1) (Q54RN1)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Protect the extracellular space from toxic effect of reactive oxygen intermediates by converting superoxyde radicals into hydrogen peroxyde and oxygen.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}; Extracellular side {ECO:0000305}.
Interaction partners:
- Catalase-A
Sequence:
MNKLIISLLIVLSAISIISADYQYGYCKFGSVGTVNQNITGYVTLTAQDGALNLVYNISSINLPTGSYATAIMTYGYNPSNNTDLGGVFQVDGKGTEQCQSGGSRAGDLYNLYVNDNRISSNFDSLTSVSIVDSPNSIIGRSIAIFQESYSCDLLKSSVGTSVGPLTTVVASCIIGIGNSANVPATNGVNTTTGNANTAGAYSSLSNTQYDAMVLLANTTKSPSAAIGGSVLFRSSSNSVSVNGIVSGVAKSVHGFHIHAFGDLTTVDGASIGGHWLSGAQVHAFPENTSRHFGDLGNLCIFDNDFKNAYYYLSTSYFSFSGLVGRGFAVHAARDDGNTYVGGDRVAQGVVALIPKAATTLNQVPSNWKYEVICSNGTYTGESTIEPSPTPSTTPTPTETSQPGTSSYLAPFFVLILSSLISVILIL