wanglab/gogpt-training-data huggingface dataset:
Protein: AXO (Q9XYX0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MAFPYIWALLPLICSASGLSLPNMTSTDAVVAGGGILPILVAGNPGNLGSSNMSLSGGGGFPAAVPADNRYRIREEVTLPRRPGGSSGTGGGCCNSGINNNNSAMIQGQKSNQYEKCAGPGDPGPCKQYIYKWRYEPTTNECTNFIWGGCEGNPQNRFGTEAECLFHCVGGPHTLPPFLQSTTREPSTTESSMLLGLPYTQSPAQSPDGMGGAEGGDGTTPVPIEQRGPELTFAETGQGKTFIFAKNNTFIQMDGDIIQTFQLRLCREISFQFRTRLLHGLLVYHNVKNPDRINLDPYALYVIVEKGQLKVVHVFGSIQRVSLFGESLNRDEWHSVMVRIDVHGARLIARVDNSQEEVYLKGLNHEYNYGVSTNLPSVVLVGGLSSEEKLHGVKYITESFVGCIRNVVLSSGKAASDLLPIAPLVATKHENVNEGCSDMCESRHNLCFVGSRCINRYGGTSCVCFGTHYEGEALRHYTHIITLRGASYVSYRIYDWKDRVHSSTRRISLMFRTNFDDSALFYSSGESLKHQYIAASIKNQSVHVEMDFGDNVMSTVLTDDLTRGYWHNLTILHEQRTVSIILDQQRKVLELPATASGNMLFDPEIYFGGGWELHKKKGLASHNYFVGSLKYVYYNTISILYELQRGNPKVHYHGVLEAEFVENEVNVIQSHYPFATSHIWWPIITPRNLILNSISAAVGRARCWPTVTLTTSAGNGFWEIRLTSDKLSFDLVPDVNNNVTHSTTIKINRATSWHSVELDYKLGEIRFTVDYRHTLSQMYGLTFNIGDKLIIGSSLKSAAMGLVGCIRDIEINGHLIEPRHVVKTERVVGKVALDNCHYIYPCKRPITCEHGGKCFVKDDRVTCDCKHTGYIGKNCHFTKYRKTCEELALLGFTKSDVYLIDIDGNGVFPPAHVKCDFQSLENATKTIVEHNLPSQVDVRSARESDFSFNIRYREFSPHMLQELISHSLYCTQYIKYDCYRAQLELHSATWFTSSAKNLTVDFLGNVKRGACPCSVNKTCVDPNQSCNCDVKENKWNSDEGYYQDPQSLGITNMYFLQQKDMDDEPRSITLGPLECVETNTQKYVVTFTTSQSYIEVPGWRKGDIAFSFRTTGEKAILLFQPPIRPHYPSFMVALTGDDQLTFTFTLSTGTTRELVINSHRRLNGGEWHKIWIDYNQYHVRFMINTDYQMLDLLPEEEFGPFEGSMYIGGATFDLLKKLSVKAGLIGCFRGLVVNGEILDIYSYMSVHLSEIIKDCKPSCVPSPCRNGAQCKEFWSSFKCVLQQSLGTYRRILRDKHHEKVLTFINRESFLMRNYLSVGATPVILMHGINGERDVLKGILNQDILINLRTYDTNALVLYANDHYNNFVHLYISLNREIVFLYNYGDEIVNLTLLDDTLMASLKSIQVAIVRGEQETRMHVNEHSVSIDRGTLLLDEYANKPWSNRKKRSCRPNVDAPALEGYIGCVRGLKIGAQLIDLADINERNIAPTQEGVLPNCQIKCDADPCKNGGTCQEHFAEQLSTCDCEHTSFLGEFCSEEKGADFSGESTLQRKFELPGTGRVDYVRLQTGFSSFDLRRANRIMLLMQTELTHHYLLLAITSDGYLQLEEDRDNGQTVGARIDRNFLNSARHTVYYVRNGTQSQLFIDREQVPLSEVRRTCPYHRWRCWLESRPDRWHQQHGLAVCRL
Protein: LIM zinc-binding domain-containing protein (Q17522)
Organism: Caenorhabditis elegans
Interaction partners:
- Uncharacterized protein T25D10.1
- F-box domain-containing protein
- F-box domain-containing protein
- Tyrosine-protein phosphatase domain-containing protein
- ShKT domain-containing protein
- CUB_2 domain-containing protein
- CUB-like domain-containing protein
- Cytochrome b561 domain-containing protein
- CUB_2 domain-containing protein
Sequence:
MPNCPNCQKPVYFAERVSSLGKDWHRPCLKCANKACGKTLSAGSHSEHEGKPYCNRCYGALFGPKGYGHGGTESHTFLQGTTGN
Protein: Hepatic leukemia factor (Q16534)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Transducin-like enhancer protein 6
- Nuclear factor interleukin-3-regulated protein
- Transducin-like enhancer protein 2
- Sushi repeat-containing protein SRPX2
- Transcription factor E2-alpha
- Annexin
Sequence:
MEKMSRPLPLNPTFIPPPYGVLRSLLENPLKLPLHHEDAFSKDKDKEKKLDDESNSPTVPQSAFLGPTLWDKTLPYDGDTFQLEYMDLEEFLSENGIPPSPSQHDHSPHPPGLQPASSAAPSVMDLSSRASAPLHPGIPSPNCMQSPIRPGQLLPANRNTPSPIDPDTIQVPVGYEPDPADLALSSIPGQEMFDPRKRKFSEEELKPQPMIKKARKVFIPDDLKDDKYWARRRKNNMAAKRSRDARRLKENQIAIRASFLEKENSALRQEVADLRKELGKCKNILAKYEARHGPL
Protein: Cadherin-8 (O54800)
Organism: Rattus norvegicus (Rat)
Function: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types.
Subcellular location: Cell membrane; Single-pass type I membrane protein.
Interaction partners:
- Catenin beta-1
- Junction plakoglobin
- Catenin alpha-2
- Catenin alpha-2
- Cadherin-4
- Cadherin-7
- Cadherin-12
- Cadherin-13
- Catenin delta 1
- Cadherin-20
Sequence:
MPERLAETLLDLWTPLIILWITLPSFVYMAPMNQAHVLTTGSPLELSRQSEEMRILNRSKRGWVWNQMFVLEEFSGPEPILVGRLHTDLDPGSKKIKYILSGDGAGTIFQINDITGDIHAIKRLDREEKAEYTLTAQAVDWETNKPLEPPSEFIIKVQDINDNAPEFLNGPYHATVPEMSILGTSVTNVTATDADDPVYGNSAKLVYSILEGQPYFSIEPETAIIKTALPNMDREAKEEYLVVIQAKDMGGHSGGLSGTTTLTVTLTDVNDNPPKFAQSLYHFSVPEDVVLGTAIGRVKANDQDIGENAQSSYDIIDGDGTALFEITSDAQAQDGVIRLRKPLDFETKKSYTLKVEAANIHIDPRFSGRGPFKDTATVKIVVEDADEPPVFSSPTYLLEVHENAALNSVIGQVTARDPDITSSPIRFSIDRHTDLERQFNINADDGKITLATPLDRELSVWHNISIIATEIRNHSQISRVPVAIKVLDVNDNAPEFASEYEAFLCENGKPGQVIQTVSAMDKDDPKNGHFFLYSLLPEMVNNPNFTIKKNEDNSLSILAKHNGFNRQKQEVYLLPIVISDSGNPPLSSTSTLTIRVCGCSNDGVVQSCNVEPYVLPIGLSMGALIAILACIILLLVIVVLFVTLRRHKNEPLIIKDDEDVRENIIRYDDEGGGEEDTEAFDIATLQNPDGINGFLPRKDIKPDLQFMPRQGLAPVPNGVDVDEFINVRLHEADNDPTAPPYDSIQIYGYEGRGSVAGSLSSLESTTSDSDQNFDYLSDWGPRFKRLGELYSVGESDKET
Protein: Mitochondrial RNA binding complex 1 subunit (Q389W4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLNVLSSTASAALATVVVARPSALHLIFERCKLNLVEFTAQDVYQICTTAYNMDTLGMLQDPDFMRGLHDAFRRSDQTVISPFQANLIADTFRKVGINSMPKEVSVPEEDAISPESLILVLRNMNITKQRDERKINEVLKLMFPILDEFSPTQLSLTVTELARLKSTNADFVGKLAKRIMEYNDDLSALDISSAAVSLAYCPGISHNILYRMMQIVEERMGEFQPEDYINVLHALNTLGPKFVNTFRKIVECGLQHVENMDAVTLTNYMVCFSTMDYKQREHIDIYADALVEVATDLSEKDLVMAFIALQRLRLLSDTMFGTMASCVIRYAAKMDPRNIAPIMDICSTVPHASDHLMKVLMDRAVECTRILTANQLGDILDILGLYPPAREHPLVQLFGKQARLRLDLMGPDALANATRGLANLGYADPEYYAQAAETGFRYGFKDWTLLEPMLMGLSITGQCPPTMVRVLGSHIAPMARSMSLMEIERANRYLRRLGCEDDFVYKAMASRVLQFVKEVTPEMPEDLQVLLQRGAVEPGAAPGVM
Protein: Esr2b protein (Estrogen receptor 2b) (Q5PR29)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|PIRNR:PIRNR002527}.
Interaction partners:
Sequence:
MSSSPGPAPVLDSSKADRGASPALLPRLYASPLGMDNQTVCIPSPYVEACQDYSPPHGGEFNHGALTLYSPVSSAVLGFHRPPVSESLVPLSPTILWPPHSLHYPPPLAYSETRSHSAWEEAKTHTLSQSSSVLSHTKLLGQQLEGDNGLNPSASIVGKGDTHFCAVCHDYASGYHYGVWSCEGCKAFFKRSIQGHNDYICPATNQCTIDKSRRKSCQACRLRKCYEVGMMKCGVRRERCSYRGARHRRNPQIRDSSGGVVGLRGQSQQHLEFPLSPSQHLFPSGGRAEGRGLNYSPEQLVSCILEAEPPQIYLREPVKKPYTEASMMMSLTSLADKELVLMISWAKKIPGFVELTLSDQVHLLECCWLDILMLGLMWRSVDHPGKLIFTPDLKLNREEGNCVEGIMEIFDMLLATTSRFRELKLQREEYVCLKAMILLNSNNCSSLPQTPEDVESRGKVLNLLDSVTDALVWIISRTGLSSQQQSIRLAHLLMLLSHIRHLSNKGIEHLSNMKRKNVVLLYDLLLEMLDANTSQSSRMLEDRQQSPENLHTSRPQPDLKDSDQETPHSPRAEETVNKTLHSSLLREDMDTN
Protein: Phospholipase A2, group III (D3ZGN6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Group 10 secretory phospholipase A2
- Group XIIA secretory phospholipase A2
- Phospholipase A2 group V
- Phospholipase A2
- Phospholipase A2, membrane associated
- Group IIC secretory phospholipase A2
- Group XIIB secretory phospholipase A2-like protein
- Phospholipase A and acyltransferase 3
- Phospholipase A2
- Phospholipase A2
Sequence:
MPKAWHYSRPSGMRTTGCRFVSGRMNPSSSQPSGLSVLMSPCGTPSSTPLDQSCREHWPLCRASGRPAEGLRLVPREPGRSEKQSTAEHLPESTNEGEEAGPFLARCGAVLGTLLRMPQNWVSRRGLGMFHGPDFCCREHDQCPQTISPLQYNYGIRNFRFHTISHCDCDARFQQCLRSQGDSIADIMGVAFFNVLEIPCFVLKEQETCVAWHWWGGCRTYGSLPLAHLQPRTYYNASWKAEATPLTPSPQSPAPSWKRGPQQTPARHHSTTTVTPLQTPAISSRPDMMIPRGQPGVSHPGLQDGPKRQGAHRVCRSLRHLDQCEHQIKPQETKFHLLNSAQTPLFHCNCTRRLARFLRHHSLPANTNKVWELLGTTCFKLAPQLNCPEGKGCSRDHRAIKVSARHLQRLHQNGLHFWDKGTGEVLAQPLEPPGTLMSFYSQCLQLTQAIWRPGGQKKFWSS
Protein: Phosphotransferase RcsD (EC 2.7.2.-) (Phosphotransfer intermediate RcsD) (P39838)
Organism: Escherichia coli (strain K12)
Function: Component of the Rcs signaling system, which controls transcription of numerous genes. RcsD is a phosphotransfer intermediate between the sensor kinase RcsC and the response regulator RcsB. It acquires a phosphoryl group from RcsC and transfers it to RcsB. The system controls expression of genes involved in colanic acid capsule synthesis, biofilm formation and cell division.
Subcellular location: Cell inner membrane {ECO:0000305|PubMed:11309126}; Multi-pass membrane protein {ECO:0000305|PubMed:11309126}.
Interaction partners:
- Transcriptional regulatory protein RcsB
- Outer membrane lipoprotein RcsF
- Sensor histidine kinase RcsC
- Transcriptional regulatory protein RcsA
- Sensor protein EvgS
- Aerobic respiration control sensor protein ArcB
- Signal transduction histidine-protein kinase BarA
- Putative membrane protein IgaA homolog
- Transcriptional activator protein BglJ
- Sensor protein TorS
Sequence:
MRQKETTATTRFSLLPGSITRFFLLLIIVLLVTMGVMVQSAVNAWLKDKSYQIVDITHAIQKRVDNWRYVTWQIYDNIAATTSPSSGEGLQETRLKQDVYYLEKPRRKTEALIFGSHDNSTLEMTQRMSTYLDTLWGAENVPWSMYYLNGQDNSLVLISTLPLKDLTSGFKESTVSDIVDSRRAEMLQQANALDERESFSNMRRLAWQNGHYFTLRTTFNQPGHLATVVAFDLPINDLIPPGMPLDSFRLEPDATATGNNDNEKEGTDSVSIHFNSTKIEISSALNSTDMRLVWQVPYGTLLLDTLQNILLPLLLNIGLLALALFGYTTFRHFSSRSTENVPSTAVNNELRILRAINEEIVSLLPLGLLVHDQESNRTVISNKIADHLLPHLNLQNITTMAEQHQGIIQATINNELYEIRMFRSQVAPRTQIFIIRDQDREVLVNKKLKQAQRLYEKNQQGRMIFMKNIGDALKEPAQSLAESAAKLNAPESKQLANQADVLVRLVDEIQLANMLADDSWKSETVLFSVQDLIDEVVPSVLPAIKRKGLQLLINNHLKAHDMRRGDRDALRRILLLLMQYAVTSTQLGKITLEVDQDESSEDRLTFRILDTGEGVSIHEMDNLHFPFINQTQNDRYGKADPLAFWLSDQLARKLGGHLNIKTRDGLGTRYSVHIKMLAADPEVEEEEERLLDDVCVMVDVTSAEIRNIVTRQLENWGATCITPDERLISQDYDIFLTDNPSNLTASGLLLSDDESGVREIGPGQLCVNFNMSNAMQEAVLQLIEVQLAQEEVTESPLGGDENAQLHASGYYALFVDTVPDDVKRLYTEAATSDFAALAQTAHRLKGVFAMLNLVPGKQLCETLEHLIREKDVPGIEKYISDIDSYVKSLL
Protein: Thioredoxin-1 (DmTrx-1) (Protein deadhead) (P47938)
Organism: Drosophila melanogaster (Fruit fly)
Function: Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. As a reducing substrate of peroxiredoxin 1, thioredoxin 2 is preferred over thioredoxin 1. Required for female meiosis and early embryonic development.
Subcellular location: Nucleus {ECO:0000269|PubMed:14579129}.
Interaction partners:
- Maternal effect protein oskar
- Protein matrimony
- CG5272 protein
- Chorion peroxidase
- Deubiquitinase otu
- Tubulin alpha-4 chain
- LD24340p
- G2/mitotic-specific cyclin-B
- Vitellogenin receptor Yl
- Thioredoxin reductase 1, mitochondrial
Sequence:
MASVRTMNDYHKRIEAADDKLIVLDFYATWCGPCKEMESTVKSLARKYSSKAVVLKIDVDKFEELTERYKVRSMPTFVFLRQNRRLASFAGADEHKLTNMMAKLVKA
Protein: UDP-galactose transporter, putative (Q388K9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MPSVKWLSAASISLVVLMLQNSLLVVLTRYSRINIPPEKRYHTSTLVLNQEILKMVVCLFLLSQEGGKCSTALPNAACMNTPSGGGFLTVLWGVCFCKEARELLVPAFLFVSQNYLIFLSLANLEASAFQVLSQTKLPFTALLSKYMLGRHLSSMQWLSLLLLSIGVLLTQAQGSNPRHTATTATQRPVVGTLACLISALSSSYASVYFEKLAKTTKPSLATRNIQLSRFGILFAALAMLIFDVLPSYGSNAGQGREPFRFWKGYDQWLTIALVCLNALGGLLVSAAMKYADNILKTFATGGAVILSGIASYFIWETPMTLLFIVGATLITLSAVLYNKYDSHAHHTAAGQTSKGEEHH
Protein: Parathymosin (Zinc-binding 11.5 kDa protein) (P04550)
Organism: Rattus norvegicus (Rat)
Function: Parathymosin may mediate immune function by blocking the effect of prothymosin alpha which confers resistance to certain opportunistic infections.
Interaction partners:
- Prothymosin alpha
- Uncharacterized protein.
Sequence:
MSEKSVEAAAELSAKDLKEKKDKVEEKAGRKERKKEVVEEEENGAEEEEEETAEDGEDDDEGDEEDEEEEEEEDEGPVRKRTAEEEDEADPKRQKTENGASA
Protein: T-cell surface glycoprotein CD8 beta chain (CD antigen CD8b) (P10966)
Organism: Homo sapiens (Human)
Function: Integral membrane glycoprotein that plays an essential role in the immune response and serves multiple functions in responses against both external and internal offenses. In T-cells, functions primarily as a coreceptor for MHC class I molecule:peptide complex. The antigens presented by class I peptides are derived from cytosolic proteins while class II derived from extracellular proteins. Interacts simultaneously with the T-cell receptor (TCR) and the MHC class I proteins presented by antigen presenting cells (APCs). In turn, recruits the Src kinase LCK to the vicinity of the TCR-CD3 complex. A palmitoylation site in the cytoplasmic tail of CD8B chain contributes to partitioning of CD8 into the plasma membrane lipid rafts where signaling proteins are enriched. Once LCK recruited, it initiates different intracellular signaling pathways by phosphorylating various substrates ultimately leading to lymphokine production, motility, adhesion and activation of cytotoxic T-lymphocytes (CTLs). Additionally, plays a critical role in thymic selection of CD8+ T-cells.
Subcellular location: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:11714755, ECO:0000269|PubMed:3145196}; Single-pass type I membrane protein {ECO:0000305}. Note=Requires the partner CD8A for efficient cell surface expression (PubMed:3145196). The heterodimer CD8A/CD8B localizes to lipid rafts due to CD8B cytoplasmic tail palmitoylation. {ECO:0000269|PubMed:10925291, ECO:0000269|PubMed:11714755, ECO:0000269|PubMed:3145196}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 3]: Secreted {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 4]: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 5]: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 6]: Secreted {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 7]: Secreted {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 8]: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MRPRLWLLLAAQLTVLHGNSVLQQTPAYIKVQTNKMVMLSCEAKISLSNMRIYWLRQRQAPSSDSHHEFLALWDSAKGTIHGEEVEQEKIAVFRDASRFILNLTSVKPEDSGIYFCMIVGSPELTFGKGTQLSVVDFLPTTAQPTKKSTLKKRVCRLPRPETQKGPLCSPITLGLLVAGVLVLLVSLGVAIHLCCRRRRARLRFMKQFYK
Protein: Protein SCD6 (Suppressor of clathrin deficiency protein 6) (P45978)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in regulation of translation and mRNA degradation. Represses translation by binding the eIF4G subunit (TIF4631 or TIF4632) of the eIF4F complex dependent on its RGG domain, forming an mRNP repressed for translation initiation.
Subcellular location: Cytoplasm, P-body {ECO:0000269|PubMed:22284680}. Cytoplasm, Stress granule {ECO:0000269|PubMed:22284680}.
Interaction partners:
- Enhancer of mRNA-decapping protein 3
- m7GpppN-mRNA hydrolase
- ATP-dependent RNA helicase DHH1
- mRNA-decapping enzyme subunit 1
- 5'-3' exoribonuclease 1
- LSM1-LSM7 complex subunit LSM1
- Chromo domain-containing protein 1
- Polyadenylate-binding protein, cytoplasmic and nuclear
- Eukaryotic initiation factor 4F subunit p150
- Eukaryotic translation initiation factor 4E
Sequence:
MSQYIGKTISLISVTDNRYVGLLEDIDSEKGTVTLKEVRCFGTEGRKNWGPEEIYPNPTVYNSVKFNGSEVKDLSILDANINDIQPVVPQMMPPASQFPPQQAQSPPQAQAQAHVQTNPQVPKPESNVPAAVAGYGVYTPTSTETATASMNDKSTPQDTNVNSQSRERGKNGENEPKYQRNKNRSSNRPPQSNRNFKVDIPNEDFDFQSNNAKFTKGDSTDVEKEKELESAVHKQDESDEQFYNKKSSFFDTISTSTETNTNMRWQEEKMLNVDTFGQASARPRFHSRGLGRGRGNYRGNRGNRGRGGQRGNYQNRNNYQNDSGAYQNQNDSYSRPANQFSQPPSNVEF
Protein: SHC-transforming protein 4 (Rai-like protein) (RaLP) (SHC-transforming protein D) (mShcD) (Src homology 2 domain-containing-transforming protein C4) (SH2 domain protein C4) (Q6S5L9)
Organism: Mus musculus (Mouse)
Function: Activates both Ras-dependent and Ras-independent migratory pathways in melanomas. Contributes to the early phases of agrin-induced tyrosine phosphorylation of CHRNB1.
Subcellular location: Postsynaptic cell membrane {ECO:0000269|PubMed:17452444}. Note=Colocalized with MUSK at the neuromuscular junction.
Interaction partners:
- Epidermal growth factor receptor
- Insulin-like growth factor 1 receptor
- Receptor tyrosine-protein kinase erbB-3
- Receptor tyrosine-protein kinase erbB-2
- Receptor tyrosine-protein kinase erbB-4
- Mast/stem cell growth factor receptor Kit
- Growth factor receptor-bound protein 2
- Proto-oncogene tyrosine-protein kinase Src
- Fibroblast growth factor receptor 3
- Son of sevenless homolog 1
Sequence:
MRERSQDSQAGLTLYVGLFGHLGMLHRTKYSRFRNESITSLDEGSPGGSVGNKGSSPPPYPALAPHLPTEDATVSSQESPTALCTLIPRMASMKLANPITFLGLKTFCLGTKQVSRLKLQENQDQTPSRPASPESNLNRTGPAPAPDPDQVGRRPTSLRPDTCPLPGPGEPSPRSKQDGPPLQHLLGNGLNYCVRYMGCIEVLQSMRSLDFGMRTQVTREAISRLCEAVPGAHGAIKKRKAPVKFLTTVLGKSNLQFSGMNIKLTVSTSSLTLMNLDNQQIIANHQMQSISFASGGDPDTTDYVAYVAKDPVNQRACHILECRSGMAQDVISTIGQAFELRFKQYLKNPSLNTWEREEVLVDGAPEDRDHDYYNSIPGKQPPEGGISDVRIQAQATDQMAYCPIRCEKLCYLPGNSTCSGVYKNCMGRSRPIGIPHERAGQGDTPSLRHFWRVDLFDDPCYVNTQALQSMHSYAGNQSSALPQGSPWHLGKAPETVQPGATAKPGSALALPHIRQQLWDEECFHGKLSRGAAEKLLVKDGDFLVRESVTSPGQFVLSGLQGGQAKHLLLVDPEGKVRTKDHVFDNVGHLIKYHMDNNLPIISSGSEVRLKQPIRKYDNTGLLPPKK
Protein: T. brucei spp.-specific protein (Q383Z1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLLVGFKPCEIVFLVDTLLGSGVSRLPQLFSFFFGGGVHSCARQRKSRKGFAPPNWHPLPRPRRLTAFPYHSQVVAHKRVVRRLLTINNLVFNCCGNLFLPICTLHPKFPFTNDLSQYVVTCEFPPLQLHFSTQAPKNCFRKQLDLVLCSINVAVDVFHPALLRTFRWIC
Protein: Dynein axonemal intermediate chain 2 (Axonemal dynein intermediate chain 2) (Q4QR00)
Organism: Xenopus laevis (African clawed frog)
Function: Part of the dynein complex of multiciliated cell cilia.
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:30561330, ECO:0000269|PubMed:33263282}. Dynein axonemal particle {ECO:0000269|PubMed:30561330, ECO:0000269|PubMed:33263282}. Note=Located in the proximal region of respiratory cilia. {ECO:0000250|UniProtKB:Q9GZS0}.
Interaction partners:
Sequence:
MEIVYVYTRKRSEFGRQCNFSDRPAELHVDILPDPSQALNFIERNPCDVAIQCSHDMSEHEVNTERYDMEAHGINHVEGGWPKDINPQEMEQTIRFRKKVEKDDHYVTTISQLGSVMEHCIKQNNAINIYEEYFEETEELEGIDETPSANTVNVFRDPNEIKRTATHLSWHPDGNRKLAVAYSCLEFQRAPKDMNFESYIWDIEIPNKPELTLRPASPLVCLEYNPKDSHVLIGGCYNGQIAYWDTRKGGNPVESTVIEYSHRDPVYKVIWLQSKTGTECFSASTDGQILWWDIRKLSEPTEKLILDISKKENIDNALGAVSMEFEPTLPTKFMVGTEQGMIVSCNRKAKTPPEKIVCTYGGHHGPIYSIQRNPFFPKNFLTVGDWTARIWSEDCRESSIMWTKYHTSYLTDACWSPTRPTVFLTTKIDGTLDVWDYMYKQNNPSLSLKVSDEPLYNICMQDNGRFVACGSKMGVTTLMELSKGLYTLQRNERNLASAMFERETKREKILEARHREMRLKERSKAEPGEEVKDEKPAEDMKEIIANAEKDFFENIEAELKRKEQQEIKQSEDEHQEKEVSEEKIVHE
Protein: Oligoribonuclease (EC 3.1.15.-) (P0A784)
Organism: Escherichia coli (strain K12)
Function: 3'-to-5' exoribonuclease specific for small oligoribonucleotides 2 to 5 nucleotides in length, as well as small (2 to 5 nucleotides) ssDNA oligomers. Probably responsible for the final step in mRNA degradation.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Ribonuclease T
- Ribonuclease R
- Sulfoquinovose isomerase
- 3'
- Polyribonucleotide nucleotidyltransferase
- Ribonuclease E
- Ribonuclease D
- Exoribonuclease 2
- Small ribosomal subunit biogenesis GTPase RsgA
- RNA pyrophosphohydrolase
Sequence:
MSANENNLIWIDLEMTGLDPERDRIIEIATLVTDANLNILAEGPTIAVHQSDEQLALMDDWNVRTHTASGLVERVKASTMGDREAELATLEFLKQWVPAGKSPICGNSIGQDRRFLFKYMPELEAYFHYRYLDVSTLKELARRWKPEILDGFTKQGTHQAMDDIRESVAELAYYREHFIKL
Protein: Rho GDP-dissociation inhibitor 3 (Rho GDI 3) (Rho-GDI gamma) (Q99819)
Organism: Homo sapiens (Human)
Function: Inhibits GDP/GTP exchange reaction of RhoB. Interacts specifically with the GDP- and GTP-bound forms of post-translationally processed Rhob and Rhog proteins, both of which show a growth-regulated expression in mammalian cells. Stimulates the release of the GDP-bound but not the GTP-bound RhoB protein. Also inhibits the GDP/GTP exchange of RhoB but shows less ability to inhibit the dissociation of prebound GTP.
Subcellular location: Cytoplasm.
Interaction partners:
- Transforming protein RhoA
- Cell division control protein 42 homolog
- Tumor necrosis factor receptor superfamily member 16
- Rho-related GTP-binding protein RhoB
- Rho-related GTP-binding protein RhoG
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit gamma
- cAMP-dependent protein kinase catalytic subunit beta
- Rho GDP-dissociation inhibitor 1
- Rho GDP-dissociation inhibitor 2
Sequence:
MLGLDACELGAQLLELLRLALCARVLLADKEGGPPAVDEVLDEAVPEYRAPGRKSLLEIRQLDPDDRSLAKYKRVLLGPLPPAVDPSLPNVQVTRLTLLSEQAPGPVVMDLTGDLAVLKDQVFVLKEGVDYRVKISFKVHREIVSGLKCLHHTYRRGLRVDKTVYMVGSYGPSAQEYEFVTPVEEAPRGALVRGPYLVVSLFTDDDRTHHLSWEWGLCICQDWKD
Protein: Dual specificity mitogen-activated protein kinase kinase 5 (MAP kinase kinase 5) (MAPKK 5) (EC 2.7.12.2) (MAPK/ERK kinase 5) (MEK 5) (Q9WVS7)
Organism: Mus musculus (Mouse)
Function: Acts as a scaffold for the formation of a ternary MAP3K2/MAP3K3-MAP3K5-MAPK7 signaling complex. Activation of this pathway appears to play a critical role in protecting cells from stress-induced apoptosis, neuronal survival and cardiac development and angiogenesis.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Mitogen-activated protein kinase kinase kinase 3
- Mitogen-activated protein kinase 7
- Mitogen-activated protein kinase kinase kinase 2
- SKI family transcriptional corepressor 1
- BTB/POZ domain-containing protein 9
- Mitogen-activated protein kinase kinase kinase 4
Sequence:
MLWLALGPFCAMENQVLVIRIKIPNSGAVDWTVHSGPQLLFRDVLDVIGQVLPEATTTAFEYEDEDGDRITVRSDEEMKAMLSYYYSTVMEQQVNGQLIEPLQIFPRACKPPGERNIHGLKVNTRAGPSQHTSPVVSDSLPSNSLKKSSAELRKILANGQMNEQDIRYRDTLGHGNGGTVYKAHHVPSGKILAVKVILLDITLELQKQIMSELEILYKCDSSYIIGFYGAFFVENRISICTEFMDGGSLDVYRKIPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTGGQVKLCDFGVSTQLVNSIAKTYVGTNAYMAPERISGEQYGIHSDVWSLGISFMELALGRFPYPQIQKNQGSLMPLQLLQCIVDEDSPVLPLGEFSEPFVHFITQCMRKQPKERPAPEELMGHPFIVQFNDGNSTVVSMWVCRALEERRSQQGPP
Protein: Probable transcriptional regulator (Q9HWJ7)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- MmsAB operon regulatory protein
- Proline utilization regulator
- Probable transcriptional regulator
- Ornithine utilization regulator
- Probable transcriptional regulator
- HTH-type transcriptional regulator ExsA
- VOC family protein
Sequence:
MERRRFSAALQGQNLRFTGAGEGGSARARVGFLLLEHFSLPAFTQALDTLVTANLIRSESFAVSNFSLSGEPVTSDLGLLICPDLALASAALQGLDLLVVCGGLRTPLRSSAALREALQDVASRGVALAGLWNGAWFLGDAGLLDGYRCCIHPEHRAALAEIARNSQVTSDSYMVDRDRLTAASPTGAFNLALEWIARRHGRDLVEAVVDILAFEESRYRRVRPALHEKMSEPLREVINLMSANIEEPLSQEQLAHYVGRSRRQIERLFQQQLGTTPVRYYLELRITECRRLLQHSDLTMLEVLVACGFVSPSHFSKCYTAFYGYPPSKEVRYGNVRSTK
Protein: Probable E3 ubiquitin-protein ligase MID2 (EC 2.3.2.27) (Midin-2) (Midline defect 2) (Midline-2) (RING finger protein 60) (RING-type E3 ubiquitin transferase MID2) (Tripartite motif-containing protein 1) (Q9UJV3)
Organism: Homo sapiens (Human)
Function: May play a role in microtubule stabilization.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:35266954}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:35266954}. Note=Microtubule-associated. {ECO:0000269|PubMed:35266954}.
Interaction partners:
- E3 ubiquitin-protein ligase Midline-1
- Immunoglobulin-binding protein 1
- Ribose-phosphate pyrophosphokinase 3
- Gamma-butyrobetaine dioxygenase
- Collagen alpha-6
- Ribose-phosphate pyrophosphokinase 1
- Ribose-phosphate pyrophosphokinase 2
Sequence:
MGESPASVVLNASGGLFSLKMETLESELTCPICLELFEDPLLLPCAHSLCFSCAHRILVSSCSSGESIEPITAFQCPTCRYVISLNHRGLDGLKRNVTLQNIIDRFQKASVSGPNSPSESRRERTYRPTTAMSSERIACQFCEQDPPRDAVKTCITCEVSYCDRCLRATHPNKKPFTSHRLVEPVPDTHLRGITCLDHENEKVNMYCVSDDQLICALCKLVGRHRDHQVASLNDRFEKLKQTLEMNLTNLVKRNSELENQMAKLIQICQQVEVNTAMHEAKLMEECDELVEIIQQRKQMIAVKIKETKVMKLRKLAQQVANCRQCLERSTVLINQAEHILKENDQARFLQSAKNIAERVAMATASSQVLIPDINFNDAFENFALDFSREKKLLEGLDYLTAPNPPSIREELCTASHDTITVHWISDDEFSISSYELQYTIFTGQANFISKSWCSWGLWPEIRKCKEAVSCSRLAGAPRGLYNSVDSWMIVPNIKQNHYTVHGLQSGTRYIFIVKAINQAGSRNSEPTRLKTNSQPFKLDPKMTHKKLKISNDGLQMEKDESSLKKSHTPERFSGTGCYGAAGNIFIDSGCHYWEVVMGSSTWYAIGIAYKSAPKNEWIGKNASSWVFSRCNSNFVVRHNNKEMLVDVPPHLKRLGVLLDYDNNMLSFYDPANSLHLHTFDVTFILPVCPTFTIWNKSLMILSGLPAPDFIDYPERQECNCRPQESPYVSGMKTCH
Protein: UDP-glycosyltransferase 79B3 (EC 2.4.1.-) (Q9T081)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MGGLKFHVLMYPWFATGHMTPFLFLANKLAEKGHTVTFLLPKKSLKQLEHFNLFPHNIVFRSVTVPHVDGLPVGTETASEIPVTSTDLLMSAMDLTRDQVEAVVRAVEPDLIFFDFAHWIPEVARDFGLKTVKYVVVSASTIASMLVPGGELGVPPPGYPSSKVLLRKQDAYTMKKLEPTNTIDVGPNLLERVTTSLMNSDVIAIRTAREIEGNFCDYIEKHCRKKVLLTGPVFPEPDKTRELEERWVKWLSGYEPDSVVFCALGSQVILEKDQFQELCLGMELTGSPFLVAVKPPRGSSTIQEALPEGFEERVKGRGLVWGGWVQQPLILSHPSVGCFVSHCGFGSMWESLLSDCQIVLVPQLGDQVLNTRLLSDELKVSVEVAREETGWFSKESLCDAVNSVMKRDSELGNLVRKNHTKWRETVASPGLMTGYVDAFVESLQDLVSGTTHD