wanglab/gogpt-training-data huggingface dataset:
Protein: Phosphatidylinositol 4-kinase gamma 4 (PI-4Kgamma4) (PI4K gamma 4) (EC 2.7.1.67) (Ubiquitin-like domain kinase gamma 4) (OsUbDKgamma4) (UbDKgamma4) (Q6K881)
Organism: Oryza sativa subsp. japonica (Rice)
Function: The phosphorylation of phosphatidylinositol (PI) to PI4P is the first committed step in the generation of phosphatidylinositol 4,5-bisphosphate (PIP2), a precursor of the second messenger inositol 1,4,5-trisphosphate (InsP3) (By similarity). Involved in the control of flowering under long day conditions by promoting degradation of FTIP1. Recruits FTIP1 for degradation by the 26S proteasome in leaves, which affects RFT1 transport to the shoot apical meristem (SAM).
Subcellular location: Nucleus {ECO:0000269|PubMed:28254780}. Endoplasmic reticulum {ECO:0000269|PubMed:28254780}.
Interaction partners:
- Os04g0476800 protein.
- Os02g0593700 protein
- Os11g0209700 protein
- Os10g0411700 protein
- Os02g0621500 protein
- Os09g0512450 protein
- Small ribosomal subunit protein eS19
- 60S ribosomal protein L29
- HECT-type E3 ubiquitin transferase
- HECT-type E3 ubiquitin transferase
Sequence:
MSSAGIATLSPLLDQFCFAPHGEPRLQQLDSIVIFLAMPGVAPMPMRVLHSDSVASVKLRIQQFKGFVTTKQRLVFSGHELSLNNSHVRDYGLTDGNVLHLVVRLADLRAISIETANGKKFQFQVESCCNVGYLKDKLSAESGQQLGSLKDQRLVFDGEELEDNQLIADISKKGAAVIHLFIRRPAKVQTQQGDKETVVTVVTPKDNDNLQTDALNLAKPAKGKPAPVEPIIANGKVKLSPAVMEMIYSTISGIENGYLPVMSTEGSGGVYFMKDSSGESNVAVFKPIDEEPMAKNNPRGLPLSTDGEGLKRGTRVGEGALREVAAYILDHPVYGCKSCDVPGFSGVPPTALVRCFHMGKGSNKVGSLQLFVDNNGSCEDMGPRAFPVKEVQKIAILDIRLANADRHAGNILVCQDGEDHLKLIPIDHGYCLPEKFEDCTFEWLYWPQAREPFGPETAAYIGSLDADKDIALLKFHGWALSPQCARVLRISTMLLKKGAERGLTPYDIGSILCRQTVKKESEIEAIIEEAEDAILPGTSEETFLETISEIMDFHLDKLAVKLKKF
Protein: Spatacsin (C4B7M4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAAEEGVASAASAGGSWGTAAMGRVLPMLLVPVPAEAMGQLGSRAQLRTQPEALGSLTAAGSLQVLSLTPGSRGGGRCCLEGPFWHFLWEDSRNSSTPTEKPKLLALGENYELLIYEFNLKDGRCDATILYSCSREALQKLIDDQDISISLLSLRILSFHNNTSLLFINKCVILHIIFPERDAAIRVLNCFTLPLPAQAVDMIIDTQLCRGILFVLSSLGWIYIFDVVDGTYVAHVDLALHKEDMCNEQQQEPAKISSFTSLKVSQDLDVAVIVSSSNSAVALNLNLYFRQHPGHLLCERILEDLPIQGPKGVDEDDPVNSAYNMKLAKFSFQIDRSWKAQLSSLNETIKNSKLEVSCCAPWFQDILHLESPESGNHSTSVQSWAFIPQDIMHGQYNVLQKDHAKTSDPGRSWKIMHISEQEEPIELKCVSVTGFTALFTWEVERMGYTITLWDLETQGMQCFSLGTKCIPVDSSGDQQLCFVLTENGLSLILFGLTQEEFLNRLMIHGSASTVDTLCHLNGWGRCSIPIHALEAGIENRQLDTVNFFLKSKENLFNPSSKSSVSDQFDHLSSHLYLRNVEELIPALDLLCSAIRESYSEPQSKHFSEQLLNLTLSFLNNQIKELFIHTEELDEHLQKGVNILTSYINELRTFMIKFPWKLTDAIDEYDVHENVPKVKESNIWKKLSFEEVIASAILNNKIPEAQTFFRIDSHSAQKLEELIGIGLNLVFDNLKKNNIKEASELLKNMGFDVKGQLLKICFYTTNKNIRDFLVEILKEKNYFSEKEKRTIDFVHQVEKLYLGHFQENMQIQSFPRYWIKEQDFFKHKSVLDSFLKYDCKDEFNKQDHRIVLNWALWWDQLTQESILLPRVSPEEYKSYSPEALWRYLTARHDWLNIILWIGEFQTQHSYASLQQNKWPLLTVDVINQNTSCNNYMRNEILDKLARNGVFLASELEDFECFLLRLSRIGGVIQDTLPVQNYKTKEGWDFHSQFILYCLEHSLQHLLYVYLDCYKLSPENCPFLEKKELHEAHPWFEFLVQCRQVASNLTDPKLIFQASLANAQILIPTNQASVSSMLLEGHTLLALATTMYSPGGVSQVVQNEENENCLKKVDPQLLKMALTPYPKLKTALFPQCTPPSVLPSDITIYHLIQSLSPFDPSRLFGWQSANTLAIGDAWSHLPHFSSPDLVNKYAIVERLNFAYYLHNGRPSFAFGTFLVQELIKSKTPKQLIQQVGNEAYVIGLSSFHIPSIGAACVCFLELLGLDSLKLRVDMKVANIILSYKCRNEDAQYSFIRESVAEKLSKLADGEKTTTEELLVLLEEGTWNSIQQQEIKRLSSESSSQWALVVQFCRLHNMKLSISYLRECAKANDWLQFIIHSQLHNYHPAEVKSLIQYFSPVIQDHLRLAFENLPSVPTSKMDSDQVCNKCPQELQGSKQEMTDLFEILLQCSEEPDSWHWLLVEAVKQQAPILSVLASCLQGASAISCLCVWIITSVEDNVATEAMGHIQDSTEDHTWNLEDLSVIWRTLLTRQKSKTLIRGFQLFFKDSPLLLVMEMYELCMFFRNYKEAEAKLLEFQKSLETLNTAATKVHPVIPAMWLEDQVCFLLKLMLQQCKTQYELGKLLQLFVEREHLFSDGPDVKKLCILCQILKDTSIAINHTIITSYSIENLQHECRSILERLQTDGQFALARRVAELAELPVDNLVIKEITQEMQTLKHIEQWSLKQARIDFWKKCHENFKKNSISSKAASSFFSTQAHVACEHPTGWSSMEERHLLLTLAGHWLAQEDVVPLDKLEELEKQIWLCRITQHTLGRNQEETEPRFSRQISTSGELSFDSLASEFSFSKLAALNTSKYLELNSLPSKETCENRLDWKEQESLNFLIGRLLDDGCVHEASRVCRYFHFYNPDVALVLHCRALASGEASMEDLHPEIHALLQSAELLEEEAPDIPLRRVHSTSSLDSQKFVTVPSSNEVVTNLEVLTSKCLHGKNYCRQVLCLYDLAKELGCSYTDVAAQDGEAMLRKILASQQPDRCKRAQAFISTQGLKPDTVAELVAEEVTRELLTSSQGTGHKQMFNPTEESQTFLQLTTLCQDRTLVGMKLLDKISSVPHGELSCTTELLILAHHCFTLTCHMEGIIRVLQAAHMLTDNHLAPSEEYGLVVRLLTGIGRYNEMTYIFDLLHKKHYFEVLMRKKLDPSGTLKTALLDYIKRCRPGDSEKHNMIALCFSMCREIGENHEAAARIQLKLIESQPWEDSLKDGHQLKQLLLKALTLMLDAAESYAKDSCVRQAQHCQRLTKLITLQIHFLNTGQNTMLINLGRHKLMDCILALPRFYQASIVAEAYDFVPDWAEILYQQVILKGDFNYLEEFKQQRLLKSSIFEEISKKYKQHQPTDMVMENLKKLLTYCEDVYLYYKLAYEHKFYEIVNVLLKDPQTGCCLKDMLAG
Protein: Sharpin (Shank-associated RH domain-interacting protein) (Shank-interacting protein-like 1) (hSIPL1) (Q9H0F6)
Organism: Homo sapiens (Human)
Function: Component of the LUBAC complex which conjugates linear polyubiquitin chains in a head-to-tail manner to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation. LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways. Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation. LUBAC is recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex. The LUBAC complex is also involved in innate immunity by conjugating linear polyubiquitin chains at the surface of bacteria invading the cytosol to form the ubiquitin coat surrounding bacteria. LUBAC is not able to initiate formation of the bacterial ubiquitin coat, and can only promote formation of linear polyubiquitins on pre-existing ubiquitin. The bacterial ubiquitin coat acts as an 'eat-me' signal for xenophagy and promotes NF-kappa-B activation. Together with OTULIN, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:20179993}. Synapse {ECO:0000250|UniProtKB:Q9EQL9}. Note=Enriched at synaptic sites in mature neurons where it colocalizes with SHANK1. {ECO:0000250|UniProtKB:Q9EQL9}.
Interaction partners:
- RanBP-type and C3HC4-type zinc finger-containing protein 1
- E3 ubiquitin-protein ligase RNF31
- Tumor necrosis factor
- NF-kappa-B essential modulator
- Tumor necrosis factor receptor superfamily member 1A
- Baculoviral IAP repeat-containing protein 2
- Spermatogenesis-associated protein 2
- Receptor-interacting serine/threonine-protein kinase 1
- Ubiquitin thioesterase otulin
- Baculoviral IAP repeat-containing protein 3
Sequence:
MAPPAGGAAAAASDLGSAAVLLAVHAAVRPLGAGPDAEAQLRRLQLSADPERPGRFRLELLGAGPGAVNLEWPLESVSYTIRGPTQHELQPPPGGPGTLSLHFLNPQEAQRWAVLVRGATVEGQNGSKSNSPPALGPEACPVSLPSPPEASTLKGPPPEADLPRSPGNLTEREELAGSLARAIAGGDEKGAAQVAAVLAQHRVALSVQLQEACFPPGPIRLQVTLEDAASAASAASSAHVALQVHPHCTVAALQEQVFSELGFPPAVQRWVIGRCLCVPERSLASYGVRQDGDPAFLYLLSAPREAPATGPSPQHPQKMDGELGRLFPPSLGLPPGPQPAASSLPSPLQPSWSCPSCTFINAPDRPGCEMCSTQRPCTWDPLAAAST
Protein: Uncharacterized transmembrane protein DDB_G0281067 (Q54UI0)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MRLLISCILILSILVNFISGHAVLVAPTPFSTNPSKTKLCGGGTKQTVAQITWCPNSSKTNRATWKIVVGDGAGAVTFKLATNGGTTEGDFTTTLTSKVLSGSDPKEVGTYYMDVRVPTGTTCTGTNGICTLQAYTESSGWYSCSAIKLDSSACDKAAEETALVEYNVQVKDNVKFCDQVVNKVVLLPAGTQLGEYDQRTQGVFKNNMANPLVIGQNSSQCGNLYEKVLCDVSFPLAPGSDGKPIYQVTQKQCEDFIEVCDVVSHVELYPCSIYGDGNGSNLIIIPTLLIISILSLILMF
Protein: Molecular chaperone MKKS (McKusick-Kaufman/Bardet-Biedl syndromes putative chaperonin) (Protein Bbs6 homolog) (Q9JI70)
Organism: Mus musculus (Mouse)
Function: Probable molecular chaperone that assists the folding of proteins upon ATP hydrolysis (By similarity). Plays a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. May play a role in protein processing in limb, cardiac and reproductive system development. May play a role in cytokinesis (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9NPJ1}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9NPJ1}. Nucleus {ECO:0000250|UniProtKB:Q9NPJ1}. Note=The majority of the protein resides within the pericentriolar material (PCM), a proteinaceous tube surrounding centrioles. During interphase, the protein is confined to the lateral surfaces of the PCM but during mitosis it relocalizes throughout the PCM and is found at the intercellular bridge. The MKSS protein is highly mobile and rapidly shuttles between the cytosol and centrosome. {ECO:0000250|UniProtKB:Q9NPJ1}.
Interaction partners:
- T-complex protein 1 subunit beta
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit eta
- T-complex protein 1 subunit zeta
- T-complex protein 1 subunit zeta-2
- T-complex protein 1 subunit delta
- Protein FAM161B
- T-complex protein 1 subunit theta
- Chaperonin-containing T-complex member BBS12
- Chaperonin containing TCP1 subunit 8-like 1
Sequence:
MSRLEAKKPSLCKTEPLTSEKVRSTLSVLKGVIASCYGPSGRLKQLHNGLGGCVYTTSQSSALLRNLSVTHPVLKILTSSVQNHVSCFSDCGLFTAILCCNLIENIQRLDLTPATAIKLNKYLLSLCTSYLKSEACSCRIPVDFRSTHTFLSLVHSILTSKPACMLTRKETDHIGALILKAFLLTIPESTEERMVLGKSIIVPLKGQRVTDSTVLPGLLIEASEVQLRRLLPTQKASGLRVALFCTSLSGDFSNAGEGVVVAHYQVSLENAVLEQLLNLGRRLVTDHVDLVLCQKVIHPSLKQFFSERHVMAIDRVGVTLMESLSKVTGATPIGSLNPIVSTTYGSVKDVCSARFGSKHFFHLLPNEATVCTLLLCSRNDTAWEELKLTCQTAMHVLQLTIKEPWVLLGGGCTETHLAAYVRHKVHHEAEAIVRDDGCTQAKLHVAAEAFCSALESVAGSLEHDGGEILIDTKYGHLWSCQADSASVGNWSDTLSRCGCGLYNSQEELSWSVLRSTYHPFAPQTCLPQAALGSASNLTVDCFTAKLSGLQVAVETANLILDLSYVIEDKN
Protein: Prophage integrase IntE (Int(Lambda)) (Prophage e14 integrase) (Prophage lambda integrase) (P75969)
Organism: Escherichia coli (strain K12)
Function: Integrase from the cryptic lambdoid prophage e14. Integrase is necessary for integration of the phage into the host genome by site-specific recombination. In conjunction with excisionase, integrase is also necessary for excision of the prophage from the host genome.
Interaction partners:
- Prophage excisionase-like protein
- Uncharacterized protein YmfJ
- Prophage transcriptional regulatory protein
- Uncharacterized protein YmfL
- Prophage integrase IntD
- Prophage integrase IntF
- Uncharacterized protein YmfR
- Uncharacterized protein YmfD
- Uncharacterized protein YmfM
- Uncharacterized protein StfP
Sequence:
MAARPRKNNVSVPNLYPLYSRKVNKVYWRYKHPVTGKFHALGTNEAEAIAIATEANTRLAEQRTRQILAISDRIATSKGKAITTSTWLDRYQAIQDDRLKSGDIRLNTYKQKAKPVSLLRERAGMKLISAVDVRDIAQLLDEYIAAGRPRMAQVVRSVLIDVFKEAQHYGEVPPGYNPALATKQPRRKITRQRLSLEEWKKIFDIADATHRYMGNAMLLALVTGQRLGDISRMKFSDIWDDHLHVIQEKTGSKIAIPLSLRLNAINWSLRDVVARCRDYAVSAYLVHFFRSTSQAERGAQVKANTLTMNFSKARDLARIDWGEGSPATFHEQRSLSERLYKEQGLDTQKLLGHKTQQQTDRYHDDRGKGWSKVAL
Protein: N-acetylglucosamine-1-phosphate transferase subunit gamma (B0BNH1)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- N-acetylglucosamine-1-phosphotransferase subunits alpha/beta
- N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase
- Neutral alpha-glucosidase AB
Sequence:
MAGRLTGFLMLLGLAAQGPAPTHAGKMKVVEEPNTFGLNNPFLPQASRLQPKREPSAVSGPPHLFRLAGKCFSLVESTYKYEFCPFHNVTQHEQTFRWNAYSGILGIWHEWEIVNNTFKGMWMTDGDSCHSRSRQSKVELTCGKTNRLAHVSEPSTCVYALTFETPLVCHPHSLLVYPTLSEALQQRWDQVEQDLADELITPQGYEKLLRALFEDAGYLKVPGETHPTQLAGDSKGLGLETLDICRKAHAELSREVQRLTSLLEQHGIPHTQPTETTHSQLLGQQLPVGEISEQLRGDPGLRGNIL
Protein: Beta-galactosidase (EC 3.2.1.23) (Acid beta-galactosidase) (Lactase) (Elastin receptor 1) (P16278)
Organism: Homo sapiens (Human)
Function: Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans.
Subcellular location: [Isoform 1]: Lysosome {ECO:0000269|PubMed:2511208, ECO:0000269|PubMed:3084261}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, perinuclear region {ECO:0000269|PubMed:2511208}. Note=Localized to the perinuclear area of the cytoplasm but not to lysosomes. {ECO:0000269|PubMed:2511208}.
Interaction partners:
- Sialidase-1
- Lysosomal protective protein
- N-acetylgalactosamine-6-sulfatase
- Lactase/phlorizin hydrolase
- Elastin
- Alpha-galactosidase A
- Lysosomal acid glucosylceramidase
- Beta-hexosaminidase subunit beta
- Beta-hexosaminidase subunit alpha
- N-acetylglucosamine-6-sulfatase
Sequence:
MPGFLVRILPLLLVLLLLGPTRGLRNATQRMFEIDYSRDSFLKDGQPFRYISGSIHYSRVPRFYWKDRLLKMKMAGLNAIQTYVPWNFHEPWPGQYQFSEDHDVEYFLRLAHELGLLVILRPGPYICAEWEMGGLPAWLLEKESILLRSSDPDYLAAVDKWLGVLLPKMKPLLYQNGGPVITVQVENEYGSYFACDFDYLRFLQKRFRHHLGDDVVLFTTDGAHKTFLKCGALQGLYTTVDFGTGSNITDAFLSQRKCEPKGPLINSEFYTGWLDHWGQPHSTIKTEAVASSLYDILARGASVNLYMFIGGTNFAYWNGANSPYAAQPTSYDYDAPLSEAGDLTEKYFALRNIIQKFEKVPEGPIPPSTPKFAYGKVTLEKLKTVGAALDILCPSGPIKSLYPLTFIQVKQHYGFVLYRTTLPQDCSNPAPLSSPLNGVHDRAYVAVDGIPQGVLERNNVITLNITGKAGATLDLLVENMGRVNYGAYINDFKGLVSNLTLSSNILTDWTIFPLDTEDAVRSHLGGWGHRDSGHHDEAWAHNSSNYTLPAFYMGNFSIPSGIPDLPQDTFIQFPGWTKGQVWINGFNLGRYWPARGPQLTLFVPQHILMTSAPNTITVLELEWAPCSSDDPELCAVTFVDRPVIGSSVTYDHPSKPVEKRLMPPPPQKNKDSWLDHV
Protein: Activin receptor type-2A (EC 2.7.11.30) (Activin receptor type IIA) (ACTR-IIA) (P27038)
Organism: Mus musculus (Mouse)
Function: On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for activin A, activin B and inhibin A. Mediates induction of adipogenesis by GDF6.
Subcellular location: Cell membrane {ECO:0000269|PubMed:1646080}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Inhibin beta A chain
- Bone morphogenetic protein 7
- Growth/differentiation factor 8
- Growth/differentiation factor 11
- Bone morphogenetic protein 6
- Activin receptor type-1B
- Activin receptor type-2B
- Bone morphogenetic protein 4
- Activin receptor type-1
- Bone morphogenetic protein 2
Sequence:
MGAAAKLAFAVFLISCSSGAILGRSETQECLFFNANWERDRTNQTGVEPCYGDKDKRRHCFATWKNISGSIEIVKQGCWLDDINCYDRTDCIEKKDSPEVYFCCCEGNMCNEKFSYFPEMEVTQPTSNPVTPKPPYYNILLYSLVPLMLIAGIVICAFWVYRHHKMAYPPVLVPTQDPGPPPPSPLLGLKPLQLLEVKARGRFGCVWKAQLLNEYVAVKIFPIQDKQSWQNEYEVYSLPGMKHENILQFIGAEKRGTSVDVDLWLITAFHEKGSLSDFLKANVVSWNELCHIAETMARGLAYLHEDIPGLKDGHKPAISHRDIKSKNVLLKNNLTACIADFGLALKFEAGKSAGDTHGQVGTRRYMAPEVLEGAINFQRDAFLRIDMYAMGLVLWELASRCTAADGPVDEYMLPFEEEIGQHPSLEDMQEVVVHKKKRPVLRDYWQKHAGMAMLCETIEECWDHDAEARLSAGCVGERITQMQRLTNIITTEDIVTVVTMVTNVDFPPKESSL
Protein: Suppressor of tumorigenicity 14 protein homolog (EC 3.4.21.109) (Serine protease 14) (Q1RLP8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
Interaction partners:
Sequence:
MRYTPVSTDKDWDQAVTFLPASDHKKMEKKKGPGKIGIIVGLVILAAVLALIIGLVVWHFHFRNDLKLQKIYTGSFRITNEAFVDAYENPQSPEFQNLADKVSTQLKLMYSESSQLSKYYVTSRVQAFSEGSVIAYYESEFAVPAAHEAAVDQAVSNLSEKYSSGKARKVSEQQGSLVLDSVVSSALDKRLISKARSSTRYNKHTSRFVEDIIFSPGFPDSPYPSNTFVQWQLRGDPDHVLKLTFDTFNLEQNCSNDFLRVYDSLVALDKFIMAEKCGYYSPSDPLSFISSRNVMLVTLVTNEEGAYPGFRARVSQIQAVTCGGRMIGNSGIFTSPNFPDYYPPNITCQWYIEVPAGKFIKLKFPKIMVSTGSECHGDFVEVVGQSKLCGQQLNTIVTVNSNTATVRFVSDSSNVDRGFSATFEDYSPSDPCQDLFLCNNKRCVKPSMRCDGWNDCGDTSDEQNCQCDAKMIQCKNGLCKPMFWRCDGVDDCGDSTDELNCGCRADQFKCKNDKCISEKQKCDGKDDCNDGSDEEGCARTDSCLVSTFLCGNSKCITKPNPECDGQDDCGDNSDESNCNCGTKAYKKSRIVGGQDAFEGEFPWQVSLHIKNIAHVCGGSIINERWIVTAAHCVQDDVKIKYSQPGTWEVFLGLHSQKDKLTATKRLLKQVIPHPYYNAYTYDNDIALMEMESPVTFSDTIRPVCLPTATDTFPAGTSVFISGWGATREGGSGATVLQKAEVRIINSTVCNQLMGGQITSRMTCAGVLSGGVDACQGDSGGPLSFPSGKRMFLAGVVSWGDGCARRNKPGIYSNVPKFRAWIKEKTGV
Protein: Ras-related protein Rab-14 (EC 3.6.5.2) (X6RFL8)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasmic vesicle, phagosome {ECO:0000256|ARBA:ARBA00004262}. Early endosome membrane {ECO:0000256|ARBA:ARBA00004438}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004438}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004438}. Golgi apparatus, trans-Golgi network membrane {ECO:0000256|ARBA:ARBA00004387}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004387}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004387}.
Interaction partners:
Sequence:
MATAPYNYSYIFKYIIIGDMGVGKSCLLHQFTEKKFMADCPHTIGVEFGTRIIEVSGQKIKLQIWDTAGQERFRAVTRSYYRGAAGALMVYDITRRSTYNHLSSWLTDARNLTNPNTVIILIGNKADLEAQRDVTYEEAKQFAEENGLLFLEASAKTGENVEDAFLEAAKKIYQNIQDGSL
Protein: Mitochondrial tRNA-specific 2-thiouridylase 1 (EC 2.8.1.14) (Q503J2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). Required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. ATP is required to activate the C2 atom of the wobble base.
Subcellular location: Mitochondrion {ECO:0000250}.
Interaction partners:
- 5-taurinomethyluridine-[tRNA] synthase subunit GTPB3, mitochondrial
- Mitochondrial tRNA translation optimization 1
- Cytoplasmic tRNA 2-thiolation protein 1
- Adenylyltransferase and sulfurtransferase MOCS3
- Cytoplasmic tRNA 2-thiolation protein 2
- Argininosuccinate lyase
- Elongation factor Tu
- tRNA dimethylallyltransferase
- Glutamyl-tRNA
- Lysine--tRNA ligase
Sequence:
MGVLRHVVCAMSGGVDSSVSALLLKRMGYHVTGVFMKNWDSQEEKGLCSSDRDCEDAYKVCKMLDIPFHEVSYVKEYWHEVFSNLLWEYERGRTPNPDIICNKHIKFKHFYQYAVNTLGADAMATGHYARTSQEDEEVFQQKLTEAPKSLFRDRFEIRKPVRLYQGADLLKDQTFFLSQISQDALRHTLFPLAGLTKGYVKKIAAEAGFQHVLKKKESMGICFIGKRDFENFILEYLEPRPGNFVSIEDGQIMGKHKGWFTLTLGQRARIGGRADAWFVVDKDVTTADVFVCPSTFHPALFRDTLQTDRFHWIAEEPPAELVHTQMMDCHFCFNNRMPLTPCTVTLNLDGSVWVMVKEPMRGMATGQFAVLYKGHECLGSGKIIRLGPTKFALQKDQSNTNCLHKDTNQQHPEPHS
Protein: Uncharacterized beta-glucan synthesis-associated protein C17G6.11c (O13789)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for synthesis of the major beta-glucans of the yeast cell wall.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Single-pass type II membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Uncharacterized protein P22H7.03
Sequence:
MYNVRGDLNRKTPSDGNVNEIGSMYASRDTSTSSFTNPTDSSTRLLYNNASNATFSSAALAAGVGGTRASGYTHRFSIRPSSQTYNRYPNGGNSAGSDMYSTSPQNNSIVDDIENINKLEAVAFAGPTAGESDFSLSREDKEIDDFLHYPLPAKDAKKLSYFVGGEGLMQLLFLLFLAAGTGMLFIGLPILTYTGHNSLASTRVTGITNHQFRILRLLRYGSLIDPDTPESAYTFDSQDLGTLDLVFSDEFNYPGRAFYDGDDQFWLATDLHYAATTDYEYYDADTPTTANGTLRLRMDAFYNHDLNFRSGMVTTWNKLCFKGGRIEVSASLGGSPYIPGFWPGIWTIGNLVRPGYLATSDGVWPYSYNSCDAGITPNQSDPSGISYLGGQRLNQCVCKGEDHPNVGTGRGGPEIDALEGTFGSGIPYNGSIYLETMPVVSQSAQYAPFDLYMYPNYDFVTIYNQSVSAMNGWAGGVYQQALSCASQLNNSWLSGNAYQKYGFDYKPGSGPDALISWFVGDEYTWTMRQPAVGQNGNIASRPVSEEPMIVVLNFGISPTWIYFYWYELTFPQTMYVDYVRIYQDSSDSSSVLGCDPEGFPTTEYIANHPKAYLNYNATSWSEAGYVRPKNSLMDGC
Protein: Deafness, autosomal dominant 5 (Dfna5) (Gasdermin Eb) (Q6J2R6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Caspase b
- Caspase 3, apoptosis-related cysteine peptidase a
- High mobility group box 1a
- Cytochrome c
- UDP-glucose 6-dehydrogenase
- Caspase a
Sequence:
MFAKATKNLLSEIDSEGFLIPVLCLNDSDGLSPQALVIKRNRYWFWQQPKYKPTDFKLSDVLVGDPINPVVVETEFLTYKGKVMDTKSGSAVAELGPGTINIGGSGSSKLQSSFGNLKKQELDLQKLLHDSKSRVLDMQHSLIQQTRNAKTEVLAVVKERIITTQPCTITEEVQEGGSCTGMFGFNKTIKVSSNDKGKPSIAYDTDVSIDIPPKTTLAYSVIELDIAHTGHYELCLLPAVKGGFEIDGPVKVKQAVTVSAAPGNPTHNMQKELVGLEGQFKVLSKLPSSTRFSLFQQISLLLQNSAVISILGSTLEDLCGGTQPDPSTLAEVPELKVTLELIQKSAGKKPSGQHQKQSTLTATHLLISALDEMSKPALFLLKSCCSYTTLQALLHLVQNMALNEKSSLKDAALDVLADEVVFKNITSLFNSCNVMLLKDDNSLITKISNPEDRLPLMLCIAVKGLASLAPHV
Protein: LIM/homeobox protein Lhx3 (LIM homeobox protein 3) (Homeobox protein LIM-3) (xLIM-3) (P36200)
Organism: Xenopus laevis (African clawed frog)
Function: Transcription factor (By similarity). May be involved in the specification and maintenance of differentiation of distinct neuronal and neuroendocrine tissues. Early marker for the pituitary and pineal lineages, it may be involved in specifying these lineages.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MLLERVRTGTQKSSDMCGYTGSPEIPQCAGCNQHIVDRFILKVLDRHWHSKCLKCNDCQIQLAEKCFSRGDSVYCKDDFFKRFGTKCAACQQGIPPTQVVRRAQEFVYHLHCFACIVCKRQLATGDEFYLMEDSRLVCKADYETAKQREAESTAKRPRTTITAKQLETLKNAYNNSPKPARHVREQLSSETGLDMRVVQVWFQNRRAKEKRLKKDAGRQRWGQYFRNMKRSRGNSKSDKDSIQEEGPDSDAEVSFTDEPSMSEMNHSNGIYNSLNDSSPVLGRQAGSNGPFSLEHGGIPTQDQYHNLRSNSPYGIPQSPASLQSMPGHQSLLSNLAFPDTGLGIIGQGGQGVAPTMRVIGVNGPSSDLSTGSSGGYPDFPVSPASWLDEVDHTQF
Protein: Lithostathine-1 (Islet of Langerhans regenerating protein 1) (REG 1) (Pancreatic stone protein 1) (PSP) (Pancreatic thread protein 1) (PTP) (Regenerating protein 1) (P43137)
Organism: Mus musculus (Mouse)
Function: Might act as an inhibitor of spontaneous calcium carbonate precipitation.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Chymotrypsin-like elastase family member 3B
- Carboxypeptidase A1
- Chymopasin
- Chymotrypsin-like elastase family member 2A
- Anionic trypsin-2
- Colipase
Sequence:
MARNAYFILLSCLIVLSPSQGQEAEEDLPSARISCPEGSNAYSSYCYYFTEDRLTWADADLFCQNMNSGYLVSVLSQAEGNFVASLIKESGTTDANVWTGLHDPKRNRRWHWSSGSLFLYKSWATGSPNSSNRGYCVSLTSNTGYKKWKDDNCDAQYSFVCKFKG
Protein: Methyl-CpG binding domain protein 3 (A0A8I6GL26)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
AAPAQADQPPSRSPSGKKFRSKPQLARYLGGSMDLSTFDFRTGKMLMNKMNKSRQRVRYDSSNQVKGKPDLNTALPVRQTASIFKQPVTKITNHPSNKVKSDPQKAVDQPRQLFWEKKLSGLSAFDIAEELVRTMDLPKGLQGVGPGCTDETLLSAIASALHTSTLPITGQLSAAVEKNPGVWLNTAQPLCKAFMVTDDDIRKQEELVQQVRKRLEEALMADMLAHVEELARDGEAPLDKACAEEEEEEEEEEEEEPEPERV
Protein: Kinesin light chain 2 (E9PP09)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MAMMVFPREEKLSQDEIVLGTKAVIQGLETLRGEHRALLAPLVAPEAGEAEPGSQERCILLRRSLEAIELGLGEAQVILALSSHLGAVESEKQKLRAQVRRLVQENQWLREELAGTQQKLQRSEQAVAQLEEEKQHLLFMSQIRK
Protein: Heme exporter protein C (Cytochrome c-type biogenesis protein CcmC) (Q9I3N5)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes.
Subcellular location: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Cytochrome c-type biogenesis protein CcmE
- Heme exporter protein D
- Cytochrome c biogenesis ATP-binding export protein CcmA
- Heme exporter protein B
- Thiol:disulfide interchange protein DsbE
- Cytochrome c-type biogenesis protein CcmH
- Cytochrome c-type biogenesis protein CcmF
- Cytochrome c-type biogenesis protein CycH
- NADH-quinone oxidoreductase subunit C/D
Sequence:
MMNWTWFHKLGSPKWFYEISGRWLPWFAVAAALLIVTGCVWGLAFAPPDYQQGNSFRIIYIHVPAAFLAQSCYVMLAVAGAVGLIWKMKIADVAVQCAAPIGAWMTFVALLTGAVWGKPTWGAWWVWDARLTAMLILLFLYFGIIALGQAISNRDSAAKACAVLAIVGVVNIPIIKYSVEWWNTLHQPATFTITEKPAMPVEMWLPLLIMVLGFYCFFAAMLLVRMRLEVLKRESRTAWAKAEVKALVEKAR
Protein: Seripauperin-10 (Q03050)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Seripauperin-18
- Seripauperin-20
- Seripauperin-11
- Seripauperin-16
- Seripauperin-12
- Seripauperin-13
- Seripauperin-24
- Seripauperin-14
- Seripauperin-2
- Seripauperin-4
Sequence:
MVKLTSIAAGVAAIAATASATTTLAQSDERVNLVELGVYVSDIRAHLAQYYMFQAAHPTETYPVEVAEAVFNYGDFTTMLTGIAPDQVTRMITGVPWYSSRLKPAISSALSKVGIYTIAN
Protein: SAFB like transcription modulator (H0YLE6)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAAATGAVAASAASGQAEGKKITDLRVIDLKSELKRRNLDITGVKTVLISRLKQAIEEEGGDPDNIELTVSTDTPNKKPTKGKGKKHEADELSGDASVEDDAFIKDGEEEENEKDIAGSGDGTQEVSKPLPSEGSLAEADHTAHEEMEAHTTVKEAEDDNISVTIQAEDAITLDFDGDDLLETGKNVKITDS