wanglab/gogpt-training-data huggingface dataset:
Protein: Large ribosomal subunit protein uL14m (39S ribosomal protein L14, mitochondrial) (L14mt) (MRP-L14) (39S ribosomal protein L32, mitochondrial) (L32mt) (MRP-L32) (Q6P1L8)
Organism: Homo sapiens (Human)
Function: Forms part of 2 intersubunit bridges in the assembled ribosome. Upon binding to MALSU1 intersubunit bridge formation is blocked, preventing ribosome formation and repressing translation (Probable).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:11543634, ECO:0000269|PubMed:22829778, ECO:0000269|PubMed:25278503, ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042}.
Interaction partners:
- Mitochondrial assembly of ribosomal large subunit protein 1
- Large ribosomal subunit protein bL36m
- Large ribosomal subunit protein bL19m
- Large ribosomal subunit protein mL65
- Large ribosomal subunit protein mL39
- Large ribosomal subunit protein mL64
- Large ribosomal subunit protein uL29m
- Large ribosomal subunit protein mL62
- Small ribosomal subunit protein mS37
- Acyl carrier protein, mitochondrial
Sequence:
MAFFTGLWGPFTCVSRVLSHHCFSTTGSLSAIQKMTRVRVVDNSALGNSPYHRAPRCIHVYKKNGVGKVGDQILLAIKGQKKKALIVGHCMPGPRMTPRFDSNNVVLIEDNGNPVGTRIKTPIPTSLRKREGEYSKVLAIAQNFV
Protein: Ribonuclease H2 subunit B (A0A2R8YCX2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAAGVDCGDGVGARQHVFLVSEYLKDASKKMKNGLMFVKLVNPCSGGLLHFATPVDPLFLLLHYLIKADKEGKFQPLDQVVVDNVFPNCILLLKLPGLEKLLHHVTEEKEIDNKKYYKYSKEKTLKWLEKKVNQTVAALKTNNVNVSSRVQSTAFFSGDQASTDKEEDYIRYAHGLISDYIPKELSDDLSKYLKLPEPSASLPNPPSKKIKLSDEPVEAKEDYTKFNTKDLKTEKKNSKMTAAQKALAKVDKSGMKSIDTFFGVKNKKKIGKV
Protein: Phospholipid scramblase (Q8IQD7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSIPTGIPNCPRGLEYLTTIDQLLVKQKVELLEAFTGFETNNKFTIKNALGQKVYFAAEDNDCCTRNCCGPARPFDMRVFDNFQQEVIHMHRPLACSSCLFPCCLQSIEVSAPPGNVIGTIEQEWSICSPSFRILNHVGDTVMRIEGPFCTFSLCGDVEFNVVSLTGEKIGKISKQWSGLAREIFTDADFFGINFPLDLDVRMKAVLLGATFLIDAMFFEKAGNQETDRPGML
Protein: B-cell CLL/lymphoma 6 member B protein (Bcl6-associated zinc finger protein) (Zinc finger protein 62) (Q8N143)
Organism: Homo sapiens (Human)
Function: Acts as a sequence-specific transcriptional repressor in association with BCL6. May function in a narrow stage or be related to some events in the early B-cell development.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- B-cell lymphoma 6 protein
- ETS translocation variant 5
Sequence:
MGSPAAPEGALGYVREFTRHSSDVLGNLNELRLRGILTDVTLLVGGQPLRAHKAVLIACSGFFYSIFRGRAGVGVDVLSLPGGPEARGFAPLLDFMYTSRLRLSPATAPAVLAAATYLQMEHVVQACHRFIQASYEPLGISLRPLEAEPPTPPTAPPPGSPRRSEGHPDPPTESRSCSQGPPSPASPDPKACNWKKYKYIVLNSQASQAGSLVGERSSGQPCPQARLPSGDEASSSSSSSSSSSEEGPIPGPQSRLSPTAATVQFKCGAPASTPYLLTSQAQDTSGSPSERARPLPGSEFFSCQNCEAVAGCSSGLDSLVPGDEDKPYKCQLCRSSFRYKGNLASHRTVHTGEKPYHCSICGARFNRPANLKTHSRIHSGEKPYKCETCGSRFVQVAHLRAHVLIHTGEKPYPCPTCGTRFRHLQTLKSHVRIHTGEKPYHCDPCGLHFRHKSQLRLHLRQKHGAATNTKVHYHILGGP
Protein: Cyclin (Q76NM8)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Cyclin-dependent kinase 2 homolog
- Signal recognition particle receptor subunit alpha, putative
Sequence:
MMNDIVLINKKKTPSEEKNIDKNEEIKLRIYGCQLLQEAGIILKLKAVTIVTSQILFHRFYFKKSFTDFDVNIIAPSALYLSCKLEEDFCRIYKIINTFHFLCKYENIKSKHIYFDIKNLNPEHFRINIESEEYKNMKVDIYTYELLILKEIGFLVHKINQHPHSFLLPYIHSLFNNLNTIHKDLTKKLAQMSWGFLNDSMRTTLCCEYQPRCIAVASIFLAAYKLNIPLMNNTNWFKLFDVEYEDIKKICIRILELYKIGRCHYIDVVVKKNK
Protein: GM08528p (Q95S58)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MEMQQENETGREGVIPNSEKEVALISNQETEKAAMISGGKEGSVRDLESPNETATTQKIEHTTKPLKLDGIFAMPATPPNKAGLATKSASSSRSSSLKKQRRGSRGSANLNVAGMGDGAPKRSAPGGGQLNYGTNSVGNDLMKQSQSMTSLKASNEEQQESRDVIQAKLHLERPYNSLKKNSHSNKMHRYSWGSGNSQCSSTSLHSSATLGLGSSGKDDLWAAIQTNYNYIMDTNLLDTCKEARCEIEGAATVLEKSSECSFKMLDETQRPEGLCEDPKELRRWLREMENKLESSPTITELTLFGNAELQRHLAVHSVLYHEIASHARVVSSCIRAAEKEQQLQQQQQLSSQQPASLTSNCSSESTSESATKSSSLSSGFASDPVTTPIGTAAAAPPSSSTHPSKKGEGNLERLRDRYHLLYLKAFELQLCLDNLLRKRSSAAVSFQKLLNALILFHLSYIKNKTINISVNTLPFDT
Protein: Profilin-4 (Profilin IV) (Q9D6I3)
Organism: Mus musculus (Mouse)
Function: Involved in male fertility. Required for manchette development and acrosome biogenesis during spermiogenesis. Binds in vitro to phospholipids, including phosphatidylinositol 3-phosphate (PtdIns(3)P), phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), phosphatidylinositol 4-phosphate (PtdIns(4)P) and phosphatidic acid (PA). Contrary to other profilin family members, does not bind to actin in vitro (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q5IRJ7}. Note=In round spermatids, mainly observed in the acroplaxome. During the progression of spermiogenesis, relocalizes to the developing manchette of spermatids step 8 (S8). Coinciding with the initiation of manchette disassembly in spermatids S14, seen in the cytoplasm subjacent to the disassembling manchette. {ECO:0000250|UniProtKB:Q5IRJ7}.
Interaction partners:
- Toll-like receptor 12
- Toll-like receptor 11
- Actin, cytoplasmic 1
- Vasodilator-stimulated phosphoprotein
- Protein diaphanous homolog 1
- Protein diaphanous homolog 2
- Actin, cytoplasmic 2
- Amyloid beta A4 precursor protein-binding family B member 1-interacting protein
- Cofilin-1
- Cofilin-2
Sequence:
MSHLQNLLLDTLLGTKHVDSAALIKLQEKTLCVTSPGFSVMPSDVRTLLNGFAKNPLLTRREGLYFKEKDYKCVRADDYSLYAKNENTGVVVVKTNMYLVVATYTAGMYPSVCVEATEKLGEYLRKKGN
Protein: LP09747p (Q9W0Z5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAARLEITVSLALAATLLCSILGHCEMSVYPGLRRRPIQPPVMDPQSEQEYAFLAQMMEQYARRRLQQQFDQQLHEINLKMDRQRQLLEQERYRQRQQELQVQREAEEDYESNGNNLNQQYDQYDNAEAEASYGSPMEAVSDLQSPPLYLPRLPNLPPLPSLPNRPSLGNSPNRNSVLRERIPFAVGPSDARFFDNPNDPSGELDSRALEDYEEYAPIEPTTEVATTASKTKIDTPVPAPVPVEPPKLLDAANTNFHRINPQSAAAAAVAGVNIPQSKEQPPHELNALINKLQKQSKAPSHLTLVNGGDSSQEQIVLRQHLGMNSEMGVYIVALIAGVSAAVTVGLLALGVTWFHNRHKAAADVEYPAYGVTGPNKDVSPSGDRKLAQSAQMYHYQHQKQQIIAMENQATDGSCGMSDVESDDDNEEGDYTVYECPGLAPTGEMEVKNPLFLDETPATPSNNLSSQTAGAANAAAATNNNITQATPQQPATLKKGTVKPNINLLNATGTAAAAASAASAASATGGEEPKQKRKSKK
Protein: Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS1 (AtMANIb) (EC 3.2.1.113) (EC 3.2.1.209) (Alpha-mannosidase IB) (Q9C512)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Class I alpha-mannosidase essential for early N-glycan processing. Progressively trims alpha-1,2-linked mannose residues. Produces Man(5)GlcNAc(2) from Man(8)GlcNAc(2), but only Man(6)GlcNAc(2) from Man(9)GlcNAc(2). Has difficulty acting on the terminal mannose of the b-branch. Involved in root development and cell wall biosynthesis.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:19914916, ECO:0000269|PubMed:20023195}; Single-pass type II membrane protein {ECO:0000269|PubMed:19914916, ECO:0000269|PubMed:20023195}.
Interaction partners:
- Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
- Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS3
- Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS2
- Alpha-mannosidase 2
- Protein OS-9 homolog
- Alpha-1,2-mannosyltransferase ALG9
- Mannosyl-oligosaccharide glucosidase GCS1
- Calnexin homolog 1
- Dolichol-phosphate mannosyltransferase subunit 1
- UDP-glucose:glycoprotein glucosyltransferase
Sequence:
MARSRSISGYGIWKYLNPAYYLRRPRRLALLFIVFVSVSMLVWDRINLAREHEVEVFKLNEEVSRLEQMLEELNGGVGNKPLKTLKDAPEDPVDKQRRQKVKEAMIHAWSSYEKYAWGKDELQPRTKDGTDSFGGLGATMVDSLDTLYIMGLDEQFQKAREWVASSLDFDKDYDASMFETTIRVVGGLLSAYDLSGDKMFLEKAKDIADRLLPAWNTPTGIPYNIINLRNGNAHNPSWAAGGDSILADSGTEQLEFIALSQRTGDPKYQQKVEKVITELNKNFPADGLLPIYINPDNANPSYSTTTFGAMGDSFYEYLLKVWVQGNKTSAVKPYRDMWEKSMKGLLSLVKKSTPSSFTYICEKNGNNLIDKMDELACFAPGMLALGASGYGPDEEKKFLSLAGELAWTCYNFYQSTPTKLAGENYFFTAGQDMSVGTSWNILRPETVESLFYLWRLTGNKTYQEWGWNIFQAFEKNSRVESGYVGLKDVNTGAKDNKMQSFFLAETLKYLYLLFSPSSVISLDEWVFNTEAHPLKIVARNDPRKPTIALRQRKFGHQINV
Protein: N-acetylglucosamine-6-sulfatase (EC 3.1.6.14) (Glucosamine-6-sulfatase) (G6S) (P15586)
Organism: Homo sapiens (Human)
Subcellular location: Lysosome.
Interaction partners:
- Alpha-N-acetylglucosaminidase
- Beta-galactosidase
- Beta-glucuronidase
- Beta-hexosaminidase subunit beta
- Beta-hexosaminidase subunit alpha
- Formylglycine-generating enzyme
- Heparan-alpha-glucosaminide N-acetyltransferase
- Cathepsin Z
Sequence:
MRLLPLAPGRLRRGSPRHLPSCSPALLLLVLGGCLGVFGVAAGTRRPNVVLLLTDDQDEVLGGMTPLKKTKALIGEMGMTFSSAYVPSALCCPSRASILTGKYPHNHHVVNNTLEGNCSSKSWQKIQEPNTFPAILRSMCGYQTFFAGKYLNEYGAPDAGGLEHVPLGWSYWYALEKNSKYYNYTLSINGKARKHGENYSVDYLTDVLANVSLDFLDYKSNFEPFFMMIATPAPHSPWTAAPQYQKAFQNVFAPRNKNFNIHGTNKHWLIRQAKTPMTNSSIQFLDNAFRKRWQTLLSVDDLVEKLVKRLEFTGELNNTYIFYTSDNGYHTGQFSLPIDKRQLYEFDIKVPLLVRGPGIKPNQTSKMLVANIDLGPTILDIAGYDLNKTQMDGMSLLPILRGASNLTWRSDVLVEYQGEGRNVTDPTCPSLSPGVSQCFPDCVCEDAYNNTYACVRTMSALWNLQYCEFDDQEVFVEVYNLTADPDQITNIAKTIDPELLGKMNYRLMMLQSCSGPTCRTPGVFDPGYRFDPRLMFSNRGSVRTRRFSKHLL
Protein: Complement factor I (EC 3.4.21.45) (C3B/C4B inactivator) [Cleaved into: Complement factor I heavy chain; Complement factor I light chain] (Q61129)
Organism: Mus musculus (Mouse)
Function: Trypsin-like serine protease that plays an essential role in regulating the immune response by controlling all complement pathways. Inhibits these pathways by cleaving three peptide bonds in the alpha-chain of C3b and two bonds in the alpha-chain of C4b thereby inactivating these proteins. Essential cofactors for these reactions include factor H and C4BP in the fluid phase and membrane cofactor protein/CD46 and CR1 on cell surfaces. The presence of these cofactors on healthy cells allows degradation of deposited C3b by CFI in order to prevent undesired complement activation, while in apoptotic cells or microbes, the absence of such cofactors leads to C3b-mediated complement activation and subsequent opsonization.
Subcellular location: Secreted, extracellular space {ECO:0000250|UniProtKB:P05156}.
Interaction partners:
- Complement factor H
- Complement C3
- Complement factor H-related 4
- Mannose-binding protein C
- Prothrombin
- Complement factor B
- Complement C4-B
- Membrane cofactor protein
- Complement component receptor 1-like protein
- Vitamin K-dependent protein C
Sequence:
MKLAHLSLFLLALHLSSSRSPSASDLPQEELVDQKCLLQKYTHRSCNKVFCQPWQRCIEGTCICKLPYQCPRAGTPVCAMNGRSYPTYCHQKSFECLHPEIKFSHNGTCAAEGKFNVSLIYGRTKTEGLVQVKLVDQDERMFICKNSWSMAEANVACVDLGFPLGVRDIQGSFNISGNLHINDTECLHVHCRGVETSLAECAFTKRRTELSNGLAGVVCYKQDADFPTSLSFQCVNGKHIPQEKACNGVNDCGDQSDELCCKGCRGNASLCKSGVCIPDQYKCNGEVDCITGEDESRCEEDRQQNIPKGLARSAQGEAEIETEETEMLTPGMDNERKRIKSLLPKLSCGVKRNTHTRRKRVIGGKPANVGDYPWQVAIKDGQRITCGGIYIGGCWILTAAHCVRPSRAHSYQVWTALLDWLKPNSQLGIQTVKRVIVHEKYNGATFQNDIALIEMKMHTGKKECELPNSVPACVPWSPYLFQPNDRCIISGWGRGKDNQKVYSLRWGEVDLIGNCSQFYPDRYYEKEMQCAGTRDGSIDACKGDSGGPLVCEDINNVTYVWGIVSWGENCGKPEFPGVYTRVANYFDWISYHVGRSLVSQHNV
Protein: SEC24 homolog B, COPII coat complex component (Sec24 related gene family, member B (S. cerevisiae)) (Q80ZX0)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000256|ARBA:ARBA00004299}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004299}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004299}. Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004397}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004397}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004397}.
Interaction partners:
- Protein transport protein Sec23A
- Protein SEC13 homolog
- Protein transport protein Sec16A
- Protein transport protein Sec31A
- Protein transport protein Sec31B
- Small COPII coat GTPase SAR1B
- Small COPII coat GTPase SAR1A
- SEC24 homolog D, COPII coat complex component)
- Protein transport protein Sec23B
- Guanine nucleotide-exchange factor SEC12
Sequence:
MSAPAGSPHPAAGARMPPKLGGAVSGLAPPQQNGPAQSPMQVPSGYGLPHQNYMVPSGHYSQGPGKMTSLPLDSQCDSYYSRPYTVPTQNSGTPSSANQPGAQQMYGRGPSAPHMGGSMPGSFQGIPASASHSYSSASQPYSSLGNRYSSPTTYSANASVASQGYPSTCSHYPISTVSNVVYPNVSYPSLPASEPYGQMFTSQSAPPPARPVKESYSGPSTALTYPSRPPPPPSQHQQQQQQQQQQQQQQQSHSGYSSLPWSGPALPPAQDSLIRNQMGSLATANSHPTNNENVQPPKSSSVVSTVLPGPSSTRMPPAPSHPVGPVPSAPPPPEQMQTKGMQYGDYGNNQASSTATPLSSASDDEEEQEEDEEAGVDSSSTTSSASPLPNSYDALEGGSYPDMHSSSASSPVPDHALEPSPTLAQALSAAPTPPAAQPAKVAKPFGYGYPALQPAYQNAAPPPMPAAHPSGPAYTGYPQHYPGVNQLSSGLGGLSLQSSPQPESLRPVNLTQEKNILPPTPIWAPVPNLSAELSKLNCSPDSFRCTLTSIPQTQALLNKAKLPLGLLLHPFRDLTQLPVITSNTIVRCRSCRTYINPFVSFIDQRRWKCNLCYRVNDVPEEFLYNPLTRSYGEPHKRPEVQNSTVEFIASSDYMLRPPQPAVYLFVLDVSHNAVEAGYLTVLCQSLLENLDKLPGDSRTRIGFMTFDSTIHFYNLQEGLSQPQMLIVSDIDDVFLPTPDSLLVNLYESKELIKDLLNALPSMFINTRETHSALGPALQAAFKLMSPTGGRVSVFQTQLPSLGAGLLQSREDPNQRSSTKVVHHLGPATDFYKKLALDCSGQQTAVDLFLLSSQYSDLASLACMSKYSAGCIFYYPSFHSTHNPSQAEKLQKDLKRYLTRKIGFEAVMRIRCTKGLSMHTFHGNFFVRSTDLLSLANINPDAGFAVQLSIEESLTDTALVCFQTALLYTSSKGERRIRVHTLCLPVVSSLADVYAGVDVQAAVCLLANMAVDRSVSSSLSDARDALVNAVVDPLSAYSSAVASVPRSTLTAPSSLKLLPLYVLALLKQKAFRTGTSTRLDDRVYAMCQMKSQPLVHLMKMIHPNLYRIDRLTDEGAIHVNDRVVPQPPLQKLSAEKLTREGAFLMDCGSVFYIWVGKGCDSNFIENVLGYPDFASIPQKMTHLPELDTLPSERTRSFVTWLRDSRPLSPVLHLVKDESPAKTDFFQHLLEDRTEAALSYYEFLIHIQQQVCK
Protein: RNA helicase (EC 3.6.4.13) (I3L3H2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MATTATMATSGSARKRLLKEEDMTKVEFETSEEVDVTPTFDTMGLREDLLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQGLLALGDYMNVQCHACIGGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRRRSLRTRAIKMLVLDEADEMLNKGFKEQIYDVYRYLPPATQVVLISATLPHEILEMTNKFMTDPIRILVKRDELTLEGIKQFFVAVEREEWKFDTLCDLYDTLTITQAVIFCNTKRKVDWLTEKMREANFTVSSMHGDMPQKERESIMKEFRSGASRVLISTDVWARGLDVPQVSLIINYDLPNNRELYIHRIGRSGRYGRKGVAINFVKNDDIRILRDIEQYYSTQIDEMPMNVADLI
Protein: Serine/arginine-rich splicing factor 4 (Q8IJI0)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Serine/arginine-rich splicing factor 1
- Alternative splicing factor ASF-1, putative
- Serine/arginine-rich splicing factor 12
- non-specific serine/threonine protein kinase
- Pre-mRNA-splicing factor CEF1, putative
- RNA-binding protein 25, putative
- Nuclear cap-binding protein subunit 2
- Splicing factor 3B subunit 1, putative
- Suppressor of forked domain-containing protein
- RNA-binding protein, putative
Sequence:
MSFKPRFSKSSSCIYVGNLPGNVIEEEVYDLFGKYGRIKYIDIKPSRSSSSSYAFVHYYDLKDADYAIERRDGYKFDGFRLRVEHSGENRSFGKYRKKDDGVGPPIRTENRVIVTNLPDNCRWQHLKDIMRQCGDVGYANIERGKGIVEFVSYDDMLYAIEKFDGAEFKVYDDVTNIKVRRDKRGSSYMKRYRNDYSPKYKKRRRYSNESGLSDRDRSRSRRYSKSSNSSNKRNNKYESHSQSLSDNRNSYRNRSKGKKRSGYKGKRSYSSYENQNDDVSRSRSDHGSRSGDRSYRKKKNKNESSSDVLSKHSSAYRDSDSEKNKSYRKRLSSDNRSHSRRRTVSEDRSERRRSLSEDRSNSRKRNASSDFKRELNSDDDKKSKKKRSYSASPGSAYKSSSRELKSQDKSNDRLSESKKSYKSQSASVRYNSTEEKKSDDETVKPKRGGRGNAKNTGKNKNTKGSKKGAKTEENHDSKSVSNDRNKSDKSEEKEKPEVVSKDEEDKKTGGAEVKPKRGRRGRKKANAADENANGNVSN
Protein: MAX interactor 1, dimerization protein (cDNA FLJ61042, highly similar to MAX-interacting protein 1) (B1ANN8)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MERVKMINVQRLLEAAEFLERRERECEHGYASSFPSMPSPRLQHSKPPRRLSRAQKHSSGSSNTSTANRRAHLRLCLERLKVLIPLGPDCTRHTTLGLLNKAKAHIKKLEEAERKSQHQLENLEREQRFLKWRLEQLQGPQEMERIRMDSIGSTISSDRSDSEREEIEVDVESTEFSHGEVDNISTTSISDIDDHSSLPSIGSDEGYSSASVKLSFTS
Protein: Interleukin-19 (IL-19) (Q8CJ70)
Organism: Mus musculus (Mouse)
Function: Cytokine that functions as an anti-inflammatory and proangiogenic factor. Polarizes adaptive immunity to an anti-inflammatory phenotype through induction of T-helper 2 responses by both down-regulation of IFN-gamma and up-regulation of IL4 and IL5. Produced by osteocytes, stimulates granulopoiesis and neutrophil formation. Exerts its biological effect through a receptor complex consisting of a heterodimer of IL20RA and IL20RB. In turn, activates the Janus kinase (JAK) and signal transducer and activator of transcription (STAT) pathway, and importantly, STAT3 (By similarity).
Subcellular location: Secreted.
Interaction partners:
- Interleukin-20 receptor subunit alpha
- Interleukin 20 receptor beta
- Interleukin-24
- Interleukin-20
- Interleukin-22 receptor subunit alpha-1
- Interleukin-10 receptor subunit beta
- Interleukin-10 receptor subunit alpha
- Interleukin-23 receptor
- Interleukin-22 receptor subunit alpha-2
- Interleukin-13 receptor subunit alpha-2
Sequence:
MKTQCASTWLLGMTLILCSVHIYSLRRCLISVDMRLIEKSFHEIKRAMQTKDTFKNVTILSLENLRSIKPGDVCCMTNNLLTFYRDRVFQDHQERSLEVLRRISSIANSFLCVQKSLERCQVHRQCNCSQEATNATRIIHDNYNQLEVSSAALKSLGELNILLAWIDRNHLETPAA
Protein: EF-hand domain-containing protein (Q57XA3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MDVLIAKAVERLGKKKLWVLVHVVDKLPESERTVGGVRNAFRSINVFINDIDFAMLASQFGRRCGGVGILRGVTTVTDESAPFDVETFKRSFLPSLSPRRQYVVSLSLKRVPTDGSGFITFDELMKVYDTARHPKLLLGWEAQALERMFLNDFWEAHSDGGITVEELTAYLVGISHKTVRDEDFELHCIRSFSLDRPKVSLEERMASAASTDIRLKSIHGTKQHPLYQASSSDYGKGWETVKYDGKFACKYTFTKNLQSQCTMGPNTMNM
Protein: Rac GTPase activating protein 1 (F8VV47)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDTMMLNVRNLFEQLVRRVEILSEGNEVQFIQLAKDFEDFRKKWQRTDHELGKYKDLLMKAETERSALDVKLKHARNQVDVEIKRRQRAEADCEKLERQIQLIREMLMCDTSGSIQLSEEQKSALAFLNRGQPSSSNAGNKRLSTIDESGSILSD
Protein: Variant surface glycoprotein (VSG, atypical), putative (Q57TR9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
Sequence:
MDCQNRAAIALVQWKTATTVAVALLYVAVTASASYEVLDFTTWPAHCSLAVTLRKVHGGMLTKLESQISYRNKLEEMEAKLRIYGLKGATAEEQTTVELLAETAALMRVSKQNKEQTNLQTAVTAVGFASEGAAAISSYLMTIDSLTHNTQTYCLSDSAAELSPTGCRHGKSSDYEAGNGPDNDDIVDSGFTKIAGQTNTANTGKKSKCGLFRHEANPESNGGIFITAASSKPSFGYGMLKIEAEDQSTGLKLSGIKARAGDEDQKFWSSCHAAVKAAQDMQDEPPLKVDQTLLAVLVGSTEMQYILKLEAAASQQKGPEEVTIDLASAKKTYFGSDNNKLEPLWTKIKGENIVDLTNAKGTTKELGTVTDTTELHKLLSYYYTVRKERQRKTAEQVEKLETELADQKDKSPESECNKISDEPKCNDEKICSWHKEVKAGEKNCQFNSKKAKEKGISVTQTQTVGGTETTTDKCKDKKKANCKDSCKWEGETCKESSILVNKKFALSAAAFAALLF
Protein: T. brucei spp.-specific protein (Q586J2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRLYKSSFFFFNYYYYFLPWRGDTSKANDFGDSINITISATGLQRGGGGVLCKLPCTSKQCLLKINGITCFRLFCQAYHLFSAVIDCFRYISPKGTSVLNSSIIKTFNVVFFFNHKTEAASAESHTRLGLKCDALLHSSNGATSFIMLDLMRTQFNE
Protein: SP1070 (Q9NGV4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MRTDSPASKGREQCKPVVCGEGACQHGGLCVPMGHDIQCFCPAGFSGRRCEQDIDECASQPCYNGGQCKDLPQGYRCECPAGYSGINCQEEASDCGNDTCPARAMCKNEPGYKNVTCLCRSGYTGDQCDVTIDPCTANGNPCGNGASCQALEQGRYKCECVPGWEGIHCEQNINDCSENPCLLGANCTDLVNDFQCACPPGFTGKRCEQKIDLCLSEPCKHGTCVDRLFDHECVCHPGWTGSACDINIDDCENRPCANEGTCVDLVDGYSCNCEPGYTGKNCQHTIDDCASNPCQHGATCVDQLDGFSCKCRPGYVGLSCEAEIDECLSDPCNPVGTERCLDLDNKFECVCRDGFKGPLCATDIDDCEAQPCLNNGICRDRVGGFECGCEPGWSGMRCEQQVTTCGAQAPCQNDASCIDLFQDYFCVCPSGTDGKNCETAPERCIGDPCMHGGKCQDFGSGLNCSCPADYSGIGCQYEYDACEEHVCQNGATCVDNGAGYSCQCPPGFTGRNCEQDIVDCKDNSCPPGATCVDLTNGFYCQCPFNMTGDDCRKAIQVDYDLYFSDPSRSTAAQVVPFPTGEANSLTVAMWVQFAQKDDRGIFFTLYGVQSARMTQQRRMLLQAHSSGVQVSLFEDQPDAFLSFGEYTSVNDGQWHHVAVVWDGISGQLQLITEGLIASKMEYGAGGSLPGYLWAVLGLPQPYGLSNELAYSDSGFQGTITKAQVWARALDITSEIQKQVRDCRSEPVLYPGLILNWAGYEVTSGGVERNVPSLCGQRKCPVGYTGANCQQLVVDKEPPVVEHCPGDLWVIAKNGSAVVSWDEPHFSDNIGVTKIYERNGHRSGTTLLWGTYDITYIASDAAGNTASCSFKVSLLTDFCPALADPVGGSQVCKDWGAGGQFKVCEIACNAGLRFSEPVPEFYTCGAEGFWRPTREPSMPLVYPSCSPSKPAQRVFRIKMLFPSDVLCNKAGQAVLRQKVTNSVNGLNRDWNFCSYAIEGTRECKDIQIDVKCDHYRGTQNNRVRRQAKDGGVYVMEAELPVVNDPVVHTSTGERSTVKQLLEKLILEDDQFAVQEILPNTVPDPASLELGSEYACPVGQVVMIPDCVPCAIGTFYDSANKTCIACSRGTYQSEAGQLQCSKCPVIAGRPGVTAGPGARSAADCKERCPAGKYFDAETGLCRSCGHGFYQPNEGSFSCELCGLGQTTRSTEATSRKECRDECSSGQQLGADGRCEPCPRGTYRLQGVQPSCAACPLGRTTPKVGASSVEECTLPVCSAGTYLNATQNMCIECRKGYYQSESQQTSCLQCPPNHSTKITGATSKSECTNPCEHIAEGKPHCDVNAYCIMVPETSDFKCECKPGFNGTGMACTDVCDGFCENSGACVKDLKGTPSCRCVGSFTGPHCAERSEFAYIAGGIAGAVIFIIIIVLLIWMICVRSTKRRDPKKMLTPAIDQTGSQVNFYYGAHTPYAESIAPSHHSTYAHYYDDEEDGWEMPNFYNETYMKDGLHGGKMSTLARSNASLYGTKEDLYDRLKRHAYTGKKEKSDSDSEVQ
Protein: Polycomb protein Sfmbt (Scm-like with four MBT domain-containing protein 1) (dSfmbt) (Q9VK33)
Organism: Drosophila melanogaster (Fruit fly)
Function: Polycomb group (PcG) protein that binds to the Polycomb response elements (PREs) found in the regulatory regions of many genes. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. PcG proteins are not required to initiate repression, but to maintain it during later stages of development. They probably act via the methylation of histones, rendering chromatin heritably changed in its expressibility. Necessary but not sufficient to recruit a functional PcG repressive complex that represses target genes, suggesting that the recruitment of the distinct PRC1 complex is also required to allow a subsequent repression.
Subcellular location: Nucleus {ECO:0000269|PubMed:16618800}.
Interaction partners:
- Polycomb protein PHO
- E3 ubiquitin-protein ligase RING1
- LD31045p
- Histone-lysine N-methyltransferase E
- GEO03726p1
- Polycomb protein Scm
- Polycomb group protein Pc
- Polycomb protein Su
- Polycomb protein esc
- Polycomb group protein Psc
Sequence:
MNPSELRMMWMSSQYNSERITLEDAATLLGHPTVGLSVMEDLSAHQPTLDMNPMMSLMGGDFTGQAAATAAALGVQPGTLIATNSNNLYGFAHMGGLQQQLLQQSAAAAVFQNYAEAMDNDVENGMVGMAMEAVVDDDDQVYGQRDNNFDDNGSELEPKQEIINIDDFVMMNEDNNSYDGTDFMTSSDKDISQSSSSCMAQMPGSLGVPGVEHDLLVPLPDGLLHHKLLGTTLVPAMGTLNGNAFGNIMVSTENTSSKQMQRTYSTAKGANSTATTATCSASTSSALRSQRKTRKIEPVNRPGLVLKTPIAYRGNIDPSVIPIQKDGMAVCKRCGAIGVKHTFYTKSRRFCSMACARGELYSLVLNTKMEGDQATTSSPDPGAGSESADLPGDQQQSQSDIELDLHAAHIKNANYRFRITDQSKITQLNSFGEPMSMGGDAAANNVQMAADETIAALNGGAVGDATAPGSTEEGASTPNSYLSAAPTPKALRLFKDIYPQDDLPQIPKYERLPVPCPQMEKIISIRRRMYDPTHSYDWLPRLSKENFNAAPVTCFPHAPGCEVWDNLGVGMKVEVENTDCDSIEVIQPGQTPTSFWVATILEIKGYKALMSYEGFDTDSHDFWVNLCNAEVHSVGWCATRGKPLIPPRTIEHKYKDWKDFLVGRLSGARTLPSNFYNKINDSLQSRFRLGLNLECVDKDRISQVRLATVTKIVGKRLFLRYFDSDDGFWCHEDSPIIHPVGWATTVGHNLAAPQDYLERMLAGREAMIEVHEDDATIELFKMNFTFDEYYSDGKTNSFVEGMKLEAVDPLNLSSICPATVMAVLKFGYMMIRIDSYQPDASGSDWFCYHEKSPCIFPAGFCSVNNISVTPPNGYDSRTFTWEGYLRDTGAVAAGQHLFHRIIPDHGFEVGMSLECADLMDPRLVCVATVARVVGRLLKVHFDGWTDEYDQWLDCESADIYPVGWCVLVNHKLEGPPRVAHQQAPKPAPKPKIQRKRKPKKGAAGGKTPTDNNTQSVKSRTIALKTTPHLPKLSIKLELKPEHHNAAFYENNQPEEEGDEEDPDADGDGDGSTSHISEQSTTQSSSDLIAGSGSGSGSASLVTLATGSNKTNSSATNNKYIPRLADIDSSEPHLELVPDTWNVYDVSQFLRVNDCTAHCDTFSRNKIDGKRLLQLTKDDIMPLLGMKVGPALKISDLIAQLKCKVNPGRARSHKTNKSPFL
Protein: Protein MTO1 homolog, mitochondrial (O13670)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in the 5-carboxymethylaminomethyl modification (mnm(5)s(2)U34) of the wobble uridine base in mitochondrial tRNAs.
Subcellular location: Mitochondrion {ECO:0000250}.
Interaction partners:
- tRNA modification GTPase mss1
- Vacuolar protein sorting-associated protein 45
- Mitochondrial tRNA-specific 2-thiouridylase 1
- Adenine phosphoribosyltransferase
- Ubiquitin-like modifier hub1
- Pseudouridine-metabolizing bifunctional protein C1861.05
Sequence:
MFRTTKRYFCTSFNRRKNVVVIGGGHAGVEAAAAASRLGAKTTLLTKSFDNIGQMSCNPAFGGIGKGTLMREIDALGGVVSGVCDESAIQFHMLNRSNGPAVWSPRAQMDRSVFKKNMQKTISTYRKNLQVREGAAVSINVLTEDDGKQVCDSIVLEDGTAIPASCIVITTGTFLGGQINVGLTQLAAGRYGERPSLPLSKCLSNLGFKMGRLKTGTPPRLSSPINISKMTEQTGDEIPETFSFLNLERDFSPALPQRSCYRTYTTELTHEIVRKNLAFAPHMLAGDILSPRYCPSLEAKVTRFPHKARHLIWLEPEGLDPNSWWYPNGLSNSMPEEIQHNIIRSIPGLENCNIVRPAYGVMYDYVIPTQLKATLETKKIQGLYLAGQINGTTGYEEAAAQGILAGLNAGLSALGREPVDIPRNTALLGVMVDDLITKGVKEPYRVFTSRSEYRLTTRADNADLRLTPLAQSIGLLDDQTHWESFQRTKSLLDFSNKIAKEFILSPQQWSKLGMPIPNDGKYRSAWDLLSFTNLDLFCVISCIPKLKDIPKRVLQRLIIEGKYTYYIKRQGTQNKQLNCRDESTVIPSDFDFDTLHSVSAEELMLLKTIRPATIGQLKRIQGIKPGTIIRLLRHTYYNPAKEAWLRKVYMPMYDMHSSEENQSTNL