wanglab/gogpt-training-data huggingface dataset:
Protein: DnaJ homolog subfamily A member 2 (Cell cycle progression restoration gene 3 protein) (Dnj3) (Dj3) (HIRA-interacting protein 4) (Renal carcinoma antigen NY-REN-14) (O60884)
Organism: Homo sapiens (Human)
Function: Co-chaperone of Hsc70. Stimulates ATP hydrolysis and the folding of unfolded proteins mediated by HSPA1A/B (in vitro).
Subcellular location: Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
Interaction partners:
- Heat shock cognate 71 kDa protein
- Heat shock 70 kDa protein 1A
- Heat shock 70 kDa protein 1-like
- DnaJ homolog subfamily A member 1
- Heat shock-related 70 kDa protein 2
- DnaJ homolog subfamily B member 1
- Heat shock 70 kDa protein 4
- Heat shock protein HSP 90-alpha
- DnaJ homolog subfamily A member 4
- Stress-induced-phosphoprotein 1
Sequence:
MANVADTKLYDILGVPPGASENELKKAYRKLAKEYHPDKNPNAGDKFKEISFAYEVLSNPEKRELYDRYGEQGLREGSGGGGGMDDIFSHIFGGGLFGFMGNQSRSRNGRRRGEDMMHPLKVSLEDLYNGKTTKLQLSKNVLCSACSGQGGKSGAVQKCSACRGRGVRIMIRQLAPGMVQQMQSVCSDCNGEGEVINEKDRCKKCEGKKVIKEVKILEVHVDKGMKHGQRITFTGEADQAPGVEPGDIVLLLQEKEHEVFQRDGNDLHMTYKIGLVEALCGFQFTFKHLDGRQIVVKYPPGKVIEPGCVRVVRGEGMPQYRNPFEKGDLYIKFDVQFPENNWINPDKLSELEDLLPSRPEVPNIIGETEEVELQEFDSTRGSGGGQRREAYNDSSDEESSSHHGPGVQCAHQ
Protein: Acyl-coa dehydrogenase, putative (EC 1.3.99.3) (Q383A3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Electron transfer flavoprotein subunit alpha
- Electron transfer flavoprotein subunit beta
- propanoyl-CoA C-acyltransferase
- Nonspecific lipid-transfer protein, putative
- Probable enoyl-CoA hydratase, mitochondrial
- Chaperone protein DNAJ, putative
- Acetyl-coenzyme A synthetase
- Methylglutaconyl-CoA hydratase, mitochondrial, putative
Sequence:
MFRRSLSRRSLQYQPCFKDLSFLVEDVFNMYAHYEKLGYTNVKREFLTNLLAEAGTLATTSLLPLYSSSDVEGCQWLQNSQVGTPKGFEAAYKTLCSKGWIGISQPLEFGGKALPYSVGSITREVMETANPPLLTYATQSIGAAEALMTCVSAKKHEMFLRRLVSGEWSGSLSLTEGQSGAAEGVVTAERAQDGTYNLTGTRNFILAGDHNLTANVLYVVLARLPSSQATGTDLSLFLVPRHVPKSDGSLETERNVKCLGLEATMGMKGSSICRMGFDNSTGYFVGEFNSGVKRTVTTTNTAAVAAAVQGVCHAELAFQNALSRTRGCNSQCTSESSTCAEGTSTVLIPDANMRLSILFAKAVAEGGRALSLDVSRLLDIYHNTTDATAREGMGNKINFYSTIANTCLTTWNFQAISRCLWMWSPQGVVKGNDMEQILRDARAAAQHSGVMTSNSVEFLNRHILPLHTEEVATFGSNVRALVRPYLFSRGTIGQCARRLWLLQKQWRLGIAKVKMLAMQEPDSVGAVSEDVIMYAGYMVLAYNWLRMATVAQKLIDSGKDVDGFYRCKVDVCQYVFQYLVPYADAHFQIMQNGASVMKSCESTWDLR
Protein: Triadin (E9Q9K5)
Organism: Mus musculus (Mouse)
Function: Contributes to the regulation of lumenal Ca2+ release via the sarcoplasmic reticulum calcium release channels RYR1 and RYR2, a key step in triggering skeletal and heart muscle contraction. Required for normal organization of the triad junction, where T-tubules and the sarcoplasmic reticulum terminal cisternae are in close contact. Required for normal skeletal muscle strength. Plays a role in excitation-contraction coupling in the heart and in regulating the rate of heart beats.
Subcellular location: Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:11707337}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q28820}.
Interaction partners:
- Calsequestrin-1
- Aspartyl/asparaginyl beta-hydroxylase
- Ryanodine receptor 2
- Calsequestrin-2
- Ryanodine receptor 1
- Histidine rich calcium binding protein
- Junctophilin-2
- Junctophilin-1
- Peptidyl-prolyl cis-trans isomerase FKBP1B
- Peptidyl-prolyl cis-trans isomerase FKBP1A
Sequence:
MTEITAEGNASTTTTVIDNKNGCIPKSPGKVLKRSVTEDIVTTFSSPAAWLLVIALIITWSAVAIVMFDLVDYKNFSASSIAKIGSDPLKLVNDAVEETTDWIYGFFSLLSDIISSEGDEDDEDADEDIDKGEIEEPPLKRKEIHQEKAEKEEKPEKKIQTKASHREREKGKEKLKGEKPEKTATHKEKLEKKERPETKMMAKEDKKIKTKEKTEEKAKKEMKVGKQEKVKPTAAKAKETPKTPPKARKKDDKEMPAVHEQKDQYAFCRYMIDMFVHGDLKPGQSPVMPPPSLTPSKPALSTTALEEKEKEEKKKMEKKDTSDTKKKEKEVKKKSEETTIDGKGKEPGKPPETKQMTAKLTTQAAARKDEKKEESKKMRKPTEEQPKGKKQEKKEKHIEPAKTPKKEHPGPSEKLKKAKAEQAKEEIAAASTKKALHGKKEEKAKTVEQEVKKEKSGKSSSDLKDKEVKKEKSGKSSSDLKDKEPQLKNEEKSKPQVKKEAKLASSDKGQTRKQNITRPEQVIPHVKPEKAEHQEKGHPSIKKDKPKPSSKGAPEVPDSGKKKIEKSEKESKVPTREENLQVYNVTKAEKPGKIPKDSKEAPASKKDKEDSKEAPTSKKDKEDSKDVPHSKKDKEVTDDVSSPKKQTRPISFFQCVYLNGYNGYGFQFPVTPVQQPGENPGKTNSPGQKQQEQ
Protein: Uroporphyrinogen decarboxylase (EC 4.1.1.37) (A0A494C0Q8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRQAGRYLPEFRETRAAQDFFSTCRSPEACCELTLQPLRRFPLDAAIIFSDILVVPQALGMEVTMVPGKGPSFPEPLREEQDLERLRDPEVVASELGYVFQAITLTRQRLAGRVPLIGFAGAPWTLMTYMVEGGGSSTMAQAKRWLYQRPQASHQLLRILTDALVPYLVGQVVAGAQALQLFESHAGHLGPQLFNKFALPYIRDVAKQVKARLREAGLAPVPMIIFAKDGHFALEELAQAGYEVVGLDWTVAPKKARECVGKTVTLQGNLDPCALYASEEEIGQLVKQMLDDFGPHRYIANLGHGLYPDMDPEHVGAFVDAVHKHSRLLRQN
Protein: Paxillin (F5GZ78)
Organism: Homo sapiens (Human)
Subcellular location: Cell junction, focal adhesion {ECO:0000256|ARBA:ARBA00004246}. Cytoplasm, cell cortex {ECO:0000256|ARBA:ARBA00004544}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MADALLADLESTTSHISKRPVFLSEETPYSYPTGNHTYQEIAVPPPVPPPPSSEALNGTILDPLDQWQPSSSRFIHQQPQSSSPVYGSSAKTSSVSNPQDSVGSPCSRVGEEEHVYSFPNKQKSAEPSPTVMSTSLGSNLSELDRLLLELNAVQHNPPGFPADEANSSPPLPGALSPLYGVPETNSPLGGKAGPLTKEKPKRNGGRGLEDVRPSVESLLDELESSVPSPVPAITVNQGEMSSPQRVTSTQQQTRISASSATRELDELMASLSDFKIQGLEQRADGERCWAAGWPRDGGRSSPGGQDEGGFMAQGKTGSSSPPGGPPKPGSQLDSMLGSLQSDLNKLGVATVAKGVCGACKKPIAGQVVTAMGKTWHPEHFVCTHCQEEIGSRNFFERDGQPYCEKDYHNLFSPRCYYCNGPILDKVVTALDRTWHPEHFFCAQCGAFFGPEGFHEKDGKAYCRKDYFDMFAPKCGGCARAILENYISALNTLWHPECFVCRECFTPFVNGSFFEHDGQPYCEVHYHERRGSLCSGCQKPITGRCITAMAKKFHPEHFVCAFCLKQLNKGTFKEQNDKPYCQNCFLKLFC
Protein: Uncharacterized sulfatase PB10D8.02c (EC 3.1.6.-) (Q9C0V7)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 31
- Mediator of RNA polymerase II transcription subunit 6
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 7
- Mediator of RNA polymerase II transcription subunit 21
- Putative glutathione S-transferase C1183.02
- Mediator of RNA polymerase II transcription subunit 19
- Mediator of RNA polymerase II transcription subunit 4
- Mediator of RNA polymerase II transcription subunit 10
Sequence:
MAFNKQAESKKPNFLVIVADDLGWSDVSPFGSEIHTPNIERLAKEGVRLTNFHTASACSPTRSMLLSGTDNHIAGLGQMAETVRRFSKVWGGKPGYEGYLNDRVAALPEILQEAGYYTTMSGKWHLGLTPDRYPSKRGFKESFALLPGGGNHFAYEPGTRENPAVPFLPPLYTHNHDPVDHKSLKNFYSSNYFAEKLIDQLKNREKSQSFFAYLPFTAPHWPLQSPKEYINKYRGRYSEGPDVLRKNRLQAQKDLGLIPENVIPAPVDGMGTKSWDELTTEEKEFSARTMEVYAAMVELLDLNIGRVIDYLKTIGELDNTFVIFMSDNGAEGSVLEAIPVLSTKPPVKYFDNSLENLGNYNSFIWYGPRWAQAATAPSRLSKGFITEGGIRCPAIIRYPPLIKPDIISDEFVTVMDILPTILELAEVPHPGHKFQGRDVVIPRGKPWIDHFVHGKPVHKDTDFSGWELFGQRAIRKGNYKAIYVPKEGIKTEWELYDLSQDKGELENLAKVHPDILNELIEYWLVYEAETGVVTAPDDFVAENVGLFKPAKHNL
Protein: Cytoplasmic envelopment protein 3 (28 kDa structural phosphoprotein) (pp28) (F5HI87)
Organism: Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5)
Function: Plays an important role in the cytoplasmic envelopment of tegument proteins and capsids during the assembly and egress processes. Participates also in viral entry at the fusion step probably by regulating the core fusion machinery.
Subcellular location: Virion tegument {ECO:0000255|HAMAP-Rule:MF_04041}. Virion membrane {ECO:0000255|HAMAP-Rule:MF_04041}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04041}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04041}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04041}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04041}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_04041}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04041}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04041}. Note=Virion membrane-associated tegument protein. Associates with host membrane lipids rafts. During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN). {ECO:0000255|HAMAP-Rule:MF_04041}.
Interaction partners:
Sequence:
MGAELCKRICCEFGTTSGEPLKDALGRQVSLRSYDNIPPTSSSDEGEDDDDGEDDDNEERQQKLRLCGSGCGGNDSSSGSHREATHDGPKKNAVRSTFREDKAPKPSKQSKKKKKPSKHHHHQQSSIMQETDDLDEEDTSIYLSPPPVPPVQVVAKRLPRPDTPRTPRQKKISQRPPTPGTKKPAASLPF
Protein: Growth hormone 1 (B2Z9Z3)
Organism: Oncorhynchus tshawytscha (Chinook salmon) (Salmo tshawytscha)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU003618}.
Interaction partners:
Sequence:
MGQVFLLMPVLLVSCFLSQGAAIENQRLFNIAVSRVQHLHLLAQKMFNDFDGTLLPDERRQLNKIFLLDFCNSDSIVSPVDKHETQKSSVLKLLHISFRLIESWEYPSQTLIISNSLMVRNANQISEKLSDLKVGINLLIQGSQDGLLSLDDNDSQQLPPYGNYYQNLGGDGNVRRNYELLACFKKDMHKVETYLTVAKCRKSLEANCTL
Protein: Frequency clock protein (P19970)
Organism: Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Function: Circadian clock component involved in the generation of biological rhythms, in particular in rhythm stability, period length, and temperature compensation. Oscillates in abundance with a daily peak early in the morning. Behaves as a negative element in circadian transcriptional loop. May bind to wc-2 protein. The complex frq-wc-2 may turn off the expression of frq.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- FRQ-interacting RNA helicase
- White collar 2 protein
- Small ribosomal subunit protein mS38
- White collar 1 protein
- Serine/threonine-protein kinase chk2
- Vivid PAS protein VVD
- non-specific serine/threonine protein kinase
- Protein ras-1
- F-box/WD-40 domain-containing protein 1
- Phosphatidylethanolamine N-methyltransferase
Sequence:
MADSGDKSQGMRPPPFDSRGHPLPRRASPDKSITLENHRLARDTSSRVTSSSALGVTESQPQLKSSPTRRNSSGESEPTNWFNQSNRNPAAAFHDESHIMEVDPPFYQKETDSSNEESRYPPGRNPVHPPGGVQLPGFRPVAAHSSAADDYRSVIDDLTVENKRLKEELKRYKQFGSDVMRKEKLFEIKVHGLPRRKKRELEATLRDFAASLGDSSESTSQRRKTGRHGTAVHSSGVSLSKHDSSSSSRSRPVDSAYNSMSTGRSSHAPHSSGPSLGRPSLTRAKSVGTQKVENYLRDTPDGLLPHHIVMTDKEKKKLVVRRLEQLFTGKISGRNMQRNQSMPSMDAPLAPEGTNMAPPRPPPEGLREACIQLQDGDNPRKNRSSKDNGSASNSGGDQTELGGTGTGSGDGSGSGGRTGNNTSPPGAIAPDQRPTRPRDLDPDRVQIPSENMDYIRHLGLVSPEFLQGSRTSYQDVAPDAEGWVYLNLLCNLAQLHMVNVTPSFIRQAVSEKSTKFQLSADGRKIRWRGGTDGTKFSSDSSEDKSQQSPMTEDTEDGSDKNGRRKKRKTQQASSEIGRFGPSRSPSDTFHYKPMFVHRNSSSIETSLEESMSQGSEDAVDESNMGNSKWDFSGSGTTQQRRKRRYDGAIVYYTGAPFCTDLSGDPGDMSPTAQMTAGREVEGSGSGDEVEHVLQRTLSGSSLPIRPLSDDRARVAEVLDFDPGNPPELVADDGSSPNDEDFVFPWCEDPAKVRIQPIAKEVMEPSGLGGVLPDDHFVMLVTTRRVVRPILQRQLSRSTTSEDTAEFIAERLAAIRTSSPLPPRSHRLTVAPLQVEYVSGQFRRLNPAPLPPPAIFYPPFSTDSSWDDGDDLASDDEEVEEVEEDSYSEGQISRRANPHFSDNNTYMRKDDLAFDTETDVRMDSDDNRLSDSGHNMRAMMPRAEAVDGDDSPLAAVTGKEVDMLHTGSSVATAGGAESGYSSSMEDVSSS
Protein: ERAD-associated E3 ubiquitin-protein ligase component HRD3 (HMG-CoA reductase degradation protein 3) (Q05787)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the endoplasmic reticulum quality control (ERQC) system involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. Component of the HRD1 ubiquitin ligase complex, which is part of the ERAD-L and ERAD-M pathways responsible for the rapid degradation of soluble lumenal and membrane proteins with misfolded lumenal domains (ERAD-L), or ER-membrane proteins with misfolded transmembrane domains (ERAD-M). ERAD-L substrates are ubiquitinated through HRD1 in conjunction with the E2 ubiquitin-conjugating enzymes UBC1 and UBC7-CUE1. Ubiquitinated substrates are then removed to the cytosol via the action of the CDC48-NPL4-UFD1 ATPase complex and targeted to the proteasome. ERAD-M substrates are processed by the same HRD1-HRD3 core complex, but only a subset of the other components is required for ERAD-M. Stabilizes the HRD1 ubiquitin-protein ligase. Also functions in recruiting misfolded protein substrates in conjunction with YOS9.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- DER1-like family member protein 1
- Degradation in the endoplasmic reticulum protein 1
- U1 SNP1-associating protein 1
- UBX domain-containing protein 2
- Cell division control protein 48
- Protein OS-9 homolog
- ERAD-associated E3 ubiquitin-protein ligase HRD1
- Ubiquitin-conjugating enzyme E2 7
- ERAD-associated E3 ubiquitin-protein ligase DOA10
- Endoplasmic reticulum chaperone BiP
Sequence:
MITLLLYLCVICNAIVLIRADSIADPWPEARHLLNTIAKSRDPMKEAAMEPNADEFVGFYVPMDYSPRNEEKNYQSIWQNEITDSQRHIYELLVQSSEQFNNSEATYTLSQIHLWSQYNFPHNMTLAHKYLEKFNDLTHFTNHSAIFDLAVMYATGGCASGNDQTVIPQDSAKALLYYQRAAQLGNLKAKQVLAYKYYSGFNVPRNFHKSLVLYRDIAEQLRKSYSRDEWDIVFPYWESYNVRISDFESGLLGKGLNSVPSSTVRKRTTRPDIGSPFIAQVNGVQMTLQIEPMGRFAFNGNDGNINGDEDDEDASERRIIRIYYAALNDYKGTYSQSRNCERAKNLLELTYKEFQPHVDNLDPLQVFYYVRCLQLLGHMYFTGEGSSKPNIHMAEEILTTSLEISRRAQGPIGRACIDLGLINQYITNNISQAISYYMKAMKTQANNGIVEFQLSKLATSFPEEKIGDPFNLMETAYLNGFIPAIYEFAVMIESGMNSKSSVENTAYLFKTFVDKNEAIMAPKLRTAFAALINDRSEVALWAYSQLAEQGYETAQVSAAYLMYQLPYEFEDPPRTTDQRKTLAISYYTRAFKQGNIDAGVVAGDIYFQMQNYSKAMALYQGAALKYSIQAIWNLGYMHEHGLGVNRDFHLAKRYYDQVSEHDHRFYLASKLSVLKLHLKSWLTWITREKVNYWKPSSPLNPNEDTQHSKTSWYKQLTKILQRMRHKEDSDKAAEDSHKHRTVVQNGANHRGDDQEEASEILGFQMEDLVTMGCILGIFLLSILMSTLAARRGWNVRFNGAQLNANGNRQQEQQQQQQAQGPPGWDFNVQIFAI
Protein: Sec-independent protein translocase protein TATA, chloroplastic (Protein THYLAKOID ASSEMBLY 4) (Protein TWIN-ARGININE TRANSLOCATION A) (Q9LKU2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across the thylakoid membrane. Involved in delta pH-dependent protein transport required for chloroplast development, especially thylakoid membrane formation. TATC and TATB mediate precursor recognition, whereas TATA facilitates translocation (By similarity).
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=The C-terminus is located in the stroma. {ECO:0000250}.
Interaction partners:
- Sec-independent protein translocase protein TATC, chloroplastic
- Sec-independent protein translocase protein TATB, chloroplastic
- Preprotein translocase subunit SCY1, chloroplastic
- Inner membrane protein ALBINO3
- Signal recognition particle subunit SRP54, chloroplastic
- RHOMBOID-like protein 10, chloroplastic
- Cell division protein FtsY homolog, chloroplastic
- Mitochondrial inner membrane protein OXA1
- Trigger factor-like protein TIG, Chloroplastic
- GMP synthase
Sequence:
MATSVATLSSPPPVSLPLLSSSRSSFFSNCFTVTTRPNTRSLVAIGRRIRQEPTRKPLTCNALFGLGVPELAVIAGVAALLFGPKKLPEIGKSIGKTVKSFQQAAKEFESELKTEPEESVAESSQVATSNKEEEKKTEVSSSSKENV
Protein: Uncharacterized protein YMR244W (Q04018)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized protein YER085C
- Uncharacterized protein YPR078C
Sequence:
MVLCKLLTPYFLLSILSVGVFTATAAPSPSIQMTENTNQDHHEHAKRGGTCAFPNYDGMVAVQKGGSNGGWAMSPDQECSYGSWCPYACKPGQLMGQWDPSATTYSYPKCQNGGLYCDSNGNLQKPNSDKDYCYDGKGTVIAKNNANSGDVAFCQTVLPGNEAMLIPTLVGSGSKQTLAVPGTDYWASSASHYYVNAPGVSVEDACQWGSSANPQGNWAPFVAGSNMDDNQNTFVKIGWNPVYLESSCPFKNVKPSFGIRITCDDESQCEGLPCSIDPSSNGVNEVTSSGGGSSGAGGGNFCVVTARNGAKANIEVFDVGSGSSSKGKRELNPLDVITTTVTETKYKTVTVTAKT
Protein: Large ribosomal subunit protein uL16m (39S ribosomal protein L16, mitochondrial) (L16mt) (MRP-L16) (Q3T0J3)
Organism: Bos taurus (Bovine)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:11279069, ECO:0000305|PubMed:16510155}.
Interaction partners:
- Small ribosomal subunit protein uS15m
- Large ribosomal subunit protein bL27m
- Ribosomal protein
- Large ribosomal subunit protein uL22m
- Large ribosomal subunit protein mL46
- Small ribosomal subunit protein bS6m
- Large ribosomal subunit protein bL21m
- Small ribosomal subunit protein uS9m
- Small ribosomal subunit protein uS11m
- Large ribosomal subunit protein bL20m
Sequence:
MWRLLSGARAPVLRATLSDSWAAPPARAGLKTLLPVPTFEDVSIPEKPKLRFVERAPLVPKVRREPKNLRDIRGPSTEATEFTEGNFAILALGGGYLHWGHFEMMRLTINRFMDPKNMFALWRVPAPFKAITRKGMGQRMGGGKGAIDHYVTPVKAGRLIVEVGGRCEFQEVQGILNQVAHKLPFPAKAVSRETLEKIQKDQEERERNNQNPWTFERIATANMLGIRKVLSPYDLTHRGRYWGKFYMPERV
Protein: TIR domain-containing protein (A0A060WMZ6)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
- Interleukin 1 receptor accessory protein
- Interleukin-1
- Interleukin-1
- Death domain-containing protein
- Interleukin-1
- Interleukin-1
- Interleukin-18
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
Sequence:
MGLCVVLLLFFLLAAVAVKVFDIDLALLFRGVFKCCGRSEDGKVYDAYVVYQMDGLDQEREEKVYHFVSIVLPTVLEKKCGFRLFIHGRDDLPGEDNMELVEDCMRLSRRLIVILTPSSSTWSGSGGQGSCGQWGYSSSLTTAGDYDCQVGLLQALVHSEMNVILIQLGDMGEGGYTHLPPGLQHLVRKSAPLMWHEGRRGSTLPNSSFWKRVRYMMPWPRSTSFDNQLI
Protein: DNA helicase MCM8 (EC 3.6.4.12) (Minichromosome maintenance 8) (I0IUP3)
Organism: Gallus gallus (Chicken)
Function: Component of the MCM8-MCM9 complex, a complex involved in homologous recombination repair following DNA interstrand cross-links and plays a key role during gametogenesis. The MCM8-MCM9 complex probably acts as a hexameric helicase required to process aberrant forks into homologous recombination substrates and to orchestrate homologous recombination with resection, fork stabilization and fork restart.
Subcellular location: Nucleus {ECO:0000269|PubMed:22771115}. Note=Localizes to nuclear foci and colocalizes with RAD51.
Interaction partners:
- Cell division control protein
- DNA helicase MCM9
- DNA replication licensing factor MCM3
- DNA replication licensing factor MCM4
- DNA replication licensing factor MCM5
- Chromatin licensing and DNA replication factor 1.
- Uncharacterized protein.
- Cell division cycle 45.
- Mini-chromosome maintenance complex-binding protein
- DNA helicase
Sequence:
MSRDLRGRGCPRGRGFQGWRGGWRGGWRGGWRGGWRGRTQKVEWKRAPEPASSRLVQSTLDQFIPYKGWKLYFSEAYADKSPFVQKTQAFEKFFMQRIELYDKDEIERKGSILVDYKELIEDRELTKSIPNISTELRDMPQKILQCMGLAIHQVLTKDLERHAAELQVQEGLPLDGEPIINVPLIHARLYNYEPLTQLKNVRANCYGKYIALRGTVVRVSNIKPLCTKLAFVCGTCGDVQSVPLPDGKYTLPTKCLVPECRGRSFTPDRSSPLTATVDWQSVKVQELMSDDQREAGRIPRTIECELVQDLVDSCVPGDVVTITGVVKVSSTEEGASKNKNDKCVFLLYIEANSVSNSKGQKTKNFEEETFQRSFMEFSLKDLYAVQEIQAEENLFRIIVNSLCPAIYGHEIVKAGLALALFGGCQKFVDDKNRIPVRGDPHVLIVGDPGLGKSQMLQAVCNVAPRGVYVCGNTSTSSGLTVTLSRDGASGDFALEAGALVLGDQGICGIDEFDKMGSQHQALLEAMEQQSISLAKAGIVCSLPARTSIVAAANPVGGHYNKAKTVSENLKMGSALLSRFDLVFILLDTPNEDHDHLLSEHVMAIRAGKQAVCSSAVVSRTNVQDRSVLEVVSDRPLLERLKISPGENFDAIPHQLLRKYVGYARQYVHPHLSPEAAQVLQEFYLELRKQNQGASSTPITTRQLESLIRLTEARSRLELREKCTKEDAEDVIEIMKYSMLGTYSDEFGKLDFERSQHGSGMSNRSQAKRFVSALSSIAERTYSNLFDLQQLRQVAKELQIRVFDFESFIESLNDQGYLLKKGSRLYQLQTM
Protein: RE54577p (Q9W128)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- CRAL-TRIO domain-containing protein
- Tetraspanin
- AT03047p
- Organic anion transporting polypeptide 33Eb
Sequence:
MARLEVIRGLTFALLLTQLLAAHVARAEVIDAEETDRFCYPESSKNSRRSCECSNVSASPWGNRALRIDCSYKDYKVADLSLLLPLYIDSLDLSWNALDSVPIFTSDSLHQLNLRHNNISQLVSGNFKQLTSLRELYLGWNSIGKLESGSFDGLPHLQVLDLAHNNLHLLPGHLFAPLLVLGTLDISWNRRFNESGGDLYTGLGVNWKLSTLRLDACSLNDLHLPVNAPLKELSLRRNQLKRIPTQLPETLLRLDISDNLLEELLPEDTANLTQVRQLFIEDMPVLQRVVANSLTHVDVLETLSFQNSRQLSHLDAEAFGPIMTTPTKKRALRSLSFRGTMLRTFNSTLAPIFTQLAELDLNGLPLQCDCELVWLKQLPVQTNGRCYKPARIRGMLVTSARGDAFSCDTWPRWAYGLVVLSLIALSAAGIYLIVMGLRPHRGVTMRRKVGAGSPYARVTIEPNRQENPH
Protein: MIOREX complex component 7 (Mitochondrial organization of gene expression protein 7) (P53869)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of MIOREX complexes, large expressome-like assemblies of ribosomes with factors involved in all the steps of post-transcriptional gene expression.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095}.
Interaction partners:
Sequence:
MPPRSIEEWFYYKLLSSPGFHRFVRKVYRKVNGIKEDPFTDQSTAFQYLYKPTPRQKFKALRLLFWDEMRSTFGFRRRLGDRFKKD
Protein: Cortactin, isoform A (Cortactin, isoform B) (Cortactin, isoform C) (Cortactin, isoform D) (LD29964p) (Q9VDF4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Dynamin
- Polychaetoid, isoform O
- Calmodulin-related protein 97A
- IP04855p
- Cofilin/actin-depolymerizing factor homolog
- Tropomyosin-1, isoforms 9A/A/B
- AT09290p
- Protein deacetylase HDAC6
- Paxillin, isoform F
- PFTAIRE-interacting factor 1A, isoform H
Sequence:
MWKASAGHQIQATSAASAEDDDWETDPDFVNDVSEQEQRWGSKTIDGSGRTAGTIDMDKLREETEQADLDKKKQLLKDQNAGYGYGGKFGVEKDRMDKSAVGHDYQGKVGKHASQKDYSDGFGGKFGVQEDRKDKSAVGWDHVEKVEKHASQKDYATGFGGKFGVQSDRVDKSAVGWDHIEKVEKHESQKDYSKGFGGKFGVQEDRKDKSAVGWDHKEAPQKHASQVDHKVKPVIEGAKPSNLRAKFENLAKNSEEESRKRAEEQKRLREAKDKRDREEAAKKTVAENTPRTSTEAPPPKGSRAAIQTGRTGGIGNAISAFNQMQSPVSETPPARKEPIIIPKAQPVKIELEAKEEPTASTTSAAVAPTPTVVPAREPETAPVAKAAAPPPDVVPQIEVETVDTPPRSEPQSPVYVPTPQPEVHAQVQVQPEPQPQADPEPVVEEEPLYQNQAEIKAASPLPPTNGTVSEAVAPSGTATVPEEAIYANSDNLADYLEDTGIHAIALYDYQAADDDEISFDPDDVITHIEKIDDGWWRGLCKNRYGLFPANYVQVVGQNS
Protein: Tumor necrosis factor (Cachectin) (TNF-alpha) (Tumor necrosis factor ligand superfamily member 2) (TNF-a) [Cleaved into: Tumor necrosis factor, membrane form (N-terminal fragment) (NTF); Intracellular domain 1 (ICD1); Intracellular domain 2 (ICD2); C-domain 1; C-domain 2; Tumor necrosis factor, soluble form] (P06804)
Organism: Mus musculus (Mouse)
Function: Cytokine that binds to TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR. It is mainly secreted by macrophages and can induce cell death of certain tumor cell lines. It is potent pyrogen causing fever by direct action or by stimulation of interleukin-1 secretion and is implicated in the induction of cachexia, Under certain conditions it can stimulate cell proliferation and induce cell differentiation (By similarity). Induces insulin resistance in adipocytes via inhibition of insulin-induced IRS1 tyrosine phosphorylation and insulin-induced glucose uptake. Induces GKAP42 protein degradation in adipocytes which is partially responsible for TNF-induced insulin resistance. Plays a role in angiogenesis by inducing VEGF production synergistically with IL1B and IL6 (By similarity).
Subcellular location: Cell membrane; Single-pass type II membrane protein.; SUBCELLULAR LOCATION: [Tumor necrosis factor, membrane form]: Membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Tumor necrosis factor, soluble form]: Secreted.; SUBCELLULAR LOCATION: [C-domain 1]: Secreted {ECO:0000250}.; SUBCELLULAR LOCATION: [C-domain 2]: Secreted {ECO:0000250}.
Interaction partners:
- TNF receptor-associated factor 2
- Tumor necrosis factor receptor superfamily member 1A
- Tumor necrosis factor receptor superfamily member 1B
- Tumor necrosis factor receptor type 1-associated DEATH domain protein
- Receptor-interacting serine/threonine-protein kinase 1
- Inhibitor of nuclear factor kappa-B kinase subunit beta
- Tumor necrosis factor alpha-induced protein 3
- Tumor necrosis factor receptor superfamily member 6
- Tumor necrosis factor receptor superfamily member 10B
- NF-kappa-B essential modulator
Sequence:
MSTESMIRDVELAEEALPQKMGGFQNSRRCLCLSLFSFLLVAGATTLFCLLNFGVIGPQRDEKFPNGLPLISSMAQTLTLRSSSQNSSDKPVAHVVANHQVEEQLEWLSQRANALLANGMDLKDNQLVVPADGLYLVYSQVLFKGQGCPDYVLLTHTVSRFAISYQEKVNLLSAVKSPCPKDTPEGAELKPWYEPIYLGGVFQLEKGDQLSAEVNLPKYLDFAESGQVYFGVIAL
Protein: LD41958p (WD repeat and FYVE domain containing 2, isoform A) (WD repeat and FYVE domain containing 2, isoform B) (Q9VKW1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Early endosome {ECO:0000256|ARBA:ARBA00004412}.
Interaction partners:
- AP complex subunit sigma
Sequence:
MAAEIKPAQRTNNDRFNTSKKPELLSKLEGSSDDVNAAILIPGENGVISVSDDKTVRVWLKRDSGQYWPSICQYMPSGCTAIEYVSESRHLYVGQENGTVTQYALSEDCNRLSFLRDYLSHQARVMAVVFSKTHKWILSAGKDKQFAYHCTESGKRVGGYNFETPCTALQFDALAKYAFVGDHAGQITMLRCDVQGVQLITTFNGHSAEIRCLKWVEGPQLLFSGACDQSVLVWDVGGKRGTIYELQGHSNKVSALSYANHTQQLISCGEDSVVVFWEMNAMRKEVPGWVDTNNCQLCSRPFFWNFRSMMDQKQLGIRQHHCRHCGKAVCDNCSTNRINIPIMGFEFDVRTCDPCYKQLQTVERPSLASFNDAKHSIVYMDLDEDRKRLLTVGQDRLIKIWDLSNIWA