wanglab/gogpt-training-data huggingface dataset:
Protein: Small ribosomal subunit protein eS28 (40S ribosomal protein S28) (P62858)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P62857}. Cytoplasm {ECO:0000269|PubMed:36517592}. Rough endoplasmic reticulum {ECO:0000250|UniProtKB:Q6QAT1}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P62857}. Note=Detected on cytosolic polysomes (By similarity). Detected in ribosomes that are associated with the rough endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:P62857, ECO:0000250|UniProtKB:Q6QAT1}.
Interaction partners:
- Large ribosomal subunit protein eL31
- Large ribosomal subunit protein uL1
- Large ribosomal subunit protein eL43
- Large ribosomal subunit protein eL24
- Large ribosomal subunit protein eL33
- Small ribosomal subunit protein uS19
- Large ribosomal subunit protein eL6
- Large ribosomal subunit protein eL32
- Small ribosomal subunit protein uS17
- Large ribosomal subunit protein eL37
Sequence:
MDTSRVQPIKLARVTKVLGRTGSQGQCTQVRVEFMDDTSRSIIRNVKGPVREGDVLTLLESEREARRLR
Protein: Target of wingless, isoform F (Q9VRZ4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGCGQSKIHLYPRKSKSKANGKKGGHADSDAETDEDEGHIEDAEKAQQRDREKHDESEELSNKDIQESDEDVAVSLLRAKNLSLLQSHQQNFFRMLDKKIDEGPDYDSASETEIALEEARLNALRQHWESASITASICSSASRSLQTTPIRQVQVPLKQPPRGAGLLIQPSSASAVTASTSSSSSSTIVALPTTEYLPQHVLTGRQVVQQQQQQQQQQAAVLYQQQQQQLILLPQLDPNVVNTSTAAAAAQLVQLQQQHQQQQQQLQLQQQQQLQLNQQQQQQLYQQQQQQYLLTLPAGSKPQSVSPKRLIYGGPAATTLLCATGIKCNAPETYEPPTAPHSQIQQQQPPPPPPGAYYGEMMHGVQAAPAAEYKFPPAISVQRLAPQVQRQLRETQELIKDSCPQLYAAGYGSPGPPIRNPSRNPTRTRPTLETQFSQELS
Protein: Translation initiation factor IF-1 (P0A3K4)
Organism: Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis)
Function: One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00075}.
Interaction partners:
Sequence:
MAKDDVIEVDGKVVDTMPNAMFTVELENGHQVLATISGKIRKNYIRILPGDKVQVELSPYDLTRGRITYRFK
Protein: Erbb2 interacting protein (A0A8I6AE43)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MTTKRSLFVRLVPCRCLRGEEETVTTLDYSHCSLEQVPKEIFTFEKTLEELYLDANQIEELPKQLFNCQSLHKLSLPDNDLTTLPASIANLINLRELDVSKNGIQEFPENIKNCKVLTVVEASVNPISKLPDGFSQLLNLTQLYLNDAFLEFLPANFGRLTKLQILELRENQLKMLPKTMNRLTQLERLDLGSNEFTEVPEVLEQLSGLREFWMDGNRLTFIPGFIGSLRQLTYLDVSKNNIEMVEEGISTCENLQDFLLSSNSLQQLPETIGSLKNVTTLKIDENQLMYLPDSIGGLRSIEELDCSFNEIEALPSSIGQLTNIRTFAADHNYLQQLPPEIGNWKNVTVLFLHSNKLETLPEEMGDMQKLKVINLSDNRLKNLPFSFTKLQQLTAMWLSDNQSKPLIPLQKETDSETQKMVLTNYMFPQQPRTEDVMFISDNESFNPALWEEQRKQRAQVAFECDEDKDEREAPPREGNLKRYPTPYPDELKNMVKTVQTIVHRLKDEETNEESGRDLKQHEDQQVVNKDKGVKPSESITTKSKLDEREKYMNSVPKTSEPEAETNAGNSPVTTNRKSSGNMKHLVNHDDVFEESEELSSDEEMKMAEMRPPLIETSINQPKVVALSNNKKDDAKDTDSLSDEVTHNSNQNNSNCSSPSRMSDSVSLNTDSSQDTALCSPAKQIPIDSNSKIRQEDENFNSLLQNGVNLNNSPEEKFKINDKKDFKLPEYDLNIEEQLVLIEKDVDSKATSEDSHQLDHINMNLNKLVTNNIFQPEIMERSKMQDIVLGTGFLSIHSKSEAEHIENGNKFLNSESINKVNGLSEDTAQSPGRIEPQNTSPADVGISKSTEDLSPQRSGPAGSVVKSHSITNMETGGLKIYDILSDDGPQPPGATVKVASTMDGKNIVRSKSATLLYDQPLQVFTASSSSSELLSGTKAVFKFDSNHNPEDPDIIRASIVPGPQSIPQLYGPPQYNVQYSGSAAMKDTLWHPKQNPQIDPVSFPPQRLPRSESAENHSYTKHSANMNFSNHNNVRANTAYHLHQRLAPTRHGEMWAVSPNDRLVPAVSRTTVQRQSSVSSTASVNLGDPGPTRRTEGDYLSYRELHSMGRTPVTSGSQRPLSARAFSIDGPSTSRPQSARPSISEIPERTMSVSDFNYSRTSPSKRPNARVGSEHSLLDPPGKSKVPHDWREQVLRHIEAKKLEKSMLSRSFSSNLTAVSSSHYGSSRDLHGSQGSLALNVADGRGSGGHSFRHPQTSSPGDCCQDDRFMSGEQNHPLGALSHRDLRDSLMKMPLSNGQMGQPLRPQANYSQTHHPPQASVARHPSREQLIDYLMLKVAHQPPYTHPHCSPRQGHELAKQEIRVRVEKDPELGFSISGGVGGRGNPFRPDDDGIFVTRVQPEGPASKLLQPGDKIIQANGYSFINIEHGQAVSLLKTFHNAVELIIVREVSS
Protein: Ubiquitin carboxyl-terminal hydrolase 17-like protein 6 (EC 3.4.19.12) (Deubiquitinating enzyme 17-like protein 6) (Ubiquitin thioesterase 17-like protein 6) (Ubiquitin-specific-processing protease 17-like protein 6) (Q6QN14)
Organism: Homo sapiens (Human)
Function: Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes that may include cell proliferation, progression through the cell cycle, cell migration, and the cellular response to viral infection. Seems to be non-functional in the regulation of apoptosis.
Subcellular location: Nucleus {ECO:0000269|PubMed:17109758}. Cytoplasm {ECO:0000269|PubMed:17109758}.
Interaction partners:
Sequence:
MEDDSLYLRGEWQFNHFSKLTSSRPDAAFAEIQRTSLPEKSPLSCETRVDLCDDLAPVARQLAPREKLPLSSRRPAAVGAGLQNMGNTCYVNASLQCLTYTPPLANYMLSREHSQTCHRHKGCMLCTMQAHITRALHNPGHVIQPSQALAAGFHRGKQEDAHEFLMFTVDAMKKACLPGHKQVDHHSKDTTLIHQIFGGYWRSQIKCLHCHGISDTFDPYLDIALDIQAAQSVQQALEQLVKPEELNGENAYHCGVCLQRAPASKTLTLHTSAKVLILVLKRFSDVTGNKIAKNVQYPECLDMQPYMSQQNTGPLVYVLYAVLVHAGWSCHNGHYFSYVKAQEGQWYKMDDAEVTASSITSVLSQQAYVLFYIQKSEWERHSESVSRGREPRALGSED
Protein: receptor protein serine/threonine kinase (EC 2.7.11.30) (Q8JFB0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MKASVMLAVLFVLVYSGSYATTADHLMETSTLKNDESSLQCSCENTNLCENNSCWGRICFYTSVHERVVRGCFQTAEQCYVPAIPGVYTKCCYTHHCNANLTMPEKPVEKPIRVILLVGVPLLVLLVIAMAACGLVLWLRTRRQYCHPVEHDTSMLKVPSGGDPTYGDIFDEFCTSGSGTGLPYLVQRTMARQISLVECVGKGRYGEVWRGTWMGESVAVKIFSSRDEQSWFRETEIYNTVQLRHENILGFIASDMTSKNSSTQLWLVTHFHELGSLYDFLQYSTLDPEGCLRMCLSIASGLVHLHTEILSTQGKPAIAHRDLKSRNILVKRNGQCCIADLGLAVIHSQSTDYLDVGTNPRVGTKRYMAPEVLDETIRVDVFESYKQTDIWALGLVLWEITRRTIVNGIVEEYRPPFFDMVPSDPSFEEMKKVVCVDQHRPSLHNRLHSHPILSAIAKIMKECWFQSPSARLTALRVRKSLSKLDQDHDYDIDKLKLDL
Protein: Neurofilament light polypeptide (NF-L) (68 kDa neurofilament protein) (Neurofilament triplet L protein) (P19527)
Organism: Rattus norvegicus (Rat)
Function: Neurofilaments usually contain three intermediate filament proteins: NEFL, NEFM, and NEFH which are involved in the maintenance of neuronal caliber. May additionally cooperate with the neuronal intermediate filament proteins PRPH and INA to form neuronal filamentous networks (By similarity).
Subcellular location: Cell projection, axon {ECO:0000250|UniProtKB:P08551}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P08551}.
Interaction partners:
- Neurofilament medium polypeptide
- Alpha-internexin
- Glutamate receptor ionotropic, NMDA 1
- Superoxide dismutase
- Kinesin heavy chain isoform 5A
- Kinesin heavy chain isoform 5C
- Kinesin light chain 1
- Kinesin light chain 3
- Kinesin light chain
- Kinesin light chain 4
Sequence:
MSSFSYEPYFSTSYKRRYVETPRVHISSVRSGYSTARSAYSSYSAPVSSSLSVRRSYSSSSGSLMPSLENLDLSQVAAISNDLKSIRTQEKAQLQDLNDRFASFIERVHELEQQNKVLEAELLVLRQKHSEPSRFRALYEQEIRDLRLAAEDATNEKQALQGEREGLEETLRNLQARYEEEVLSREDAEGRLMEARKGADEAALARAELEKRIDSLMDEIAFLKKVHEEEIAELQAQIQYAQISVEMDVSSKPDLSAALKDIRAQYEKLAAKNMQNAEEWFKSRFTVLTESAAKNTDAVRAAKDEVSESRRLLKAKTLEIEACRGMNEALEKQLQELEDKQNADISAMQDTINKLENELRSTKSEMARYLKEYQDLLNVKMALDIEIAAYRKLLEGEETRLSFTSVGSITSGYSQSSQVFGRSAYSGLQSSSYLMSARAFPAYYTSHVQEEQSEVEETIEATKAEEAKDEPPSEGEAEEEEKEKEEGEEEEGAEEEEAAKDESEDAKEEEGGEGEEEDTKESEEEEKKEESAGEEQAAKKKD
Protein: Protein-S-isoprenylcysteine O-methyltransferase (EC 2.1.1.100) (Q38DE5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU362022}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU362022}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- intramembrane prenyl-peptidase Rce1
- CAAX prenyl protease
- Small GTPase, putative
- GTP binding protein
Sequence:
MHWGYRHALEVALISFYLGVCFTLGVSLMIHSVYYTGSVAEYAVGAYVISSIVLFHMSEFLVAVYFLRHDAHPGAFMIFHSREYTVAGAAAWLEFFTELFFCSEGWKVSATSRWGWLFRLNYTMVNCAAVLTIFFYLVRVCGMAHCGCNFSLLIETRRRSNHVLVTDGIYSILRHPAYFGYFWTALFSQLVLANPFCFMAYAIVLIRFFKERITYEETVLSSVEFFGESYMKYKAGTWVGIPFIR
Protein: Zsf1p (Q5A5R5)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Importin N-terminal domain-containing protein
- Exosome non-catalytic core subunit
- 5'-3' exoribonuclease 1
- General negative regulator of transcription subunit 1
- Decapping enzyme complex catalytic subunit
- U2 snRNP complex subunit
- 14-3-3 protein homolog
Sequence:
MMSTLKDSKHFAFNGTKSSIASSSSSTTDFDDLLPDLWQTSSNESDIKHSSQSLFNSPHHYLFQQQPQQNWFNVSVSPANSVSSPLRSTSSLWEDPPAEQQQQQPQPIFYLPQDDDLFNFEQVHHPQHHTKTQINTQLYKTELCASFMKTGVCPYANKCQFAHGENELKHVERPPKWRSKPCANWTKYGSCRYGNRCCFKHGD
Protein: ATP synthase subunit O, mitochondrial (Oligomycin sensitivity conferral protein) (Q7JNG1)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- ATP synthase subunit a
- Putative ATP synthase subunit f
- ATP synthase subunit delta, mitochondrial
- ATP synthase-coupling factor 6
- ATP synthase F
- ATP synthase subunit alpha, mitochondrial
- ATP synthase F
- ATP synthase subunit beta, mitochondrial
- ATP synthase c subunit
- ATP synthase subunit d
Sequence:
MRIFIPSKPLYLYLTILHEKVMAQLMKRGFSTSAALAKAQLVKTPIQVHGVEGRYAAALYSAGHKQNKLDQISTDLNNVRSVYKDNKKFQEFVLDPTLKANKKKTAIEAISTKLGLTKETGNFLGLLAENGRLNKLESVVSSFESIMRAHRGELFVQVTSAEELSSSNQKALSDALSKIGKSGQKLTVTYAVKPSILGGLVVTIGDKYVDLSIASRVKKYKDALATAI
Protein: Protein NEDD1 (Zgc:63491) (Q6PEI2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MEDVTRLVSSGDCLKIWDSSSMTVVEQFNPHSATHPVAQVCWSSSNQYVVSASSIGDKLVVSSLKSSPVPVMELGEGKKQTRVSLNSTSQFLVSGGLDNTVNIWDLKTKRLHRTLKDHKEEVTCVSFNGGDSYIASGSTSGDIILHSITTNLSSKPFGHGPNVPIHDLRYSLVKRSLLGTVSDSGSVALWDANTQKELHLFEGAHKAPCSGLAFSPANDLLFVTVGLDKKIVCYDTSSKIVFRNKQVESPLTAIDFTPDGAGLVVGSTQGRIYLYDLRNLSAPVKINTAHKTSVTCIRFQNSTSKLKSTKSSSKSSQSNKRISVKLGSSQQTGPSTPTSTVTPIVSGSEFPGDGQAQVPGPSAEVFSREAEGQLSQDQMPNVEKFSSIGRNSLNLDIFSPLNDGFKSHGFADTSRNGGSIDVFSREAEGQQTADRFRVGRNSLDIFSPVRDDYKGHRLSDVSSGKKDFEYLPHFPGGSSQRKTPLGTPGSRCYSPSVVQTPPIKEEESTTTPPQQTDVQNGTKVEKSNGVRQEYDAITTPPAAQSTRIQSVQPQFNTPEPSQRRDLSTQLTYDSPISRAPAPAPPAAAAAPAAAVESAPLTSVQMNFVRNMIHEALEDFRDTCHRDIINLQVEMVRQFYIQLNEIHGLIEKYSVNDSLVEEIERLKEENKRLRANY
Protein: Protein scalloped (P30052)
Organism: Drosophila melanogaster (Fruit fly)
Function: Transcription factor which plays a key role in the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein Hippo (Hpo), in complex with its regulatory protein Salvador (Sav), phosphorylates and activates Warts (Wts) in complex with its regulatory protein Mats, which in turn phosphorylates and inactivates the Yorkie (Yki) oncoprotein. The Hippo/SWH signaling pathway inhibits the activity of the transcriptional complex formed by Scalloped (sd) and Yki and the target genes of this pathway include cyclin-E (cycE), diap1 and bantam. Sd promotes nuclear localization of Yki. Involved in the regulation of cell-specific gene expression during development, particularly in the differentiation of the nervous system. When in combination with vestigial (vg) it acts as a transcriptional activation complex that regulates gene expression in the wing. Binding to vg switches the DNA target selectivity of sd. Required autonomously for cell proliferation and viability within the wing blade. Required for proper sensory organ precursor (SOP) differentiation at the wing margin; required for correct expression of sens.
Subcellular location: Nucleus.
Interaction partners:
Sequence:
MKNITSSSTCSTGLLQLQNNLSCSELEVAEKTEQQAVGPGTIPSPWTPVNAGPPGALGSADTNGSMVDSKNLDVGDMSDDEKDLSSADAEGVWSPDIEQSFQEALSIYPPCGRRKIILSDEGKMYGRNELIARYIKLRTGKTRTRKQVSSHIQVLARRKLREIQAKIKVQFWQPGLQPSTSQDFYDYSIKPFPQPPYPAGKTSTAVSGDETGIPPSQLPWEGRAIATHKFRLLEFTAFMEIQRDEIYHRHLFVQLGGKPSFSDPLLETVDIRQIFDKFPEKSGGLKDLYEKGPQNAFYLVKCWADLNTDLTTGSETGDFYGVTSQYESNENVVLVCSTIVCSFGKQVVEKVESEYSRLENNRYVYRIQRSPMCEYMINFIQKLKNLPERYMMNSVLENFTILQVMRARETQETLLCIAYVFEVAAQNSGTTHHIYRLIKE
Protein: Serine and arginine rich splicing factor 5 (cDNA FLJ57437, highly similar to Splicing factor, arginine/serine-rich 5) (B4DUA4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSGCRVFIGRLNPAAREKDVERFFKGYGRIRDIDLKRGFGFVEFEDPRDADDAVYELDGKELCSERVTIEHARARSRGGRGRGRYSDRFSSRRPRNDRRNAPPVRTENRLIVENLSSRVSWQPVCVVGLMTRSACGLS
Protein: Mitochondrial import receptor subunit tomm-70 (Translocase of outer mitochondrial membrane 70) (Q02335)
Organism: Caenorhabditis elegans
Function: Receptor that accelerates the import of all mitochondrial precursor proteins.
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:23727266}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q75Q39}.
Interaction partners:
- Mitochondrial import receptor subunit TOM20 homolog
- Mitochondrial import receptor subunit TOM22 homolog
- Mitochondrial import receptor subunit TOM40 homolog
- Mitochondrial import inner membrane translocase subunit TIM50
- TPR_REGION domain-containing protein
- Heat shock protein 90
- Probable voltage-dependent anion-selective channel
- RNA polymerase II-associated protein 3
- Histidine kinase/HSP90-like ATPase domain-containing protein
- Probable mitochondrial import inner membrane translocase subunit tin-44
Sequence:
MVETTGISDQTKKVLIGVAAAATVAGVGYLVYKSFGGSDLERDLEEIKALGNLKFKEKQYDSALEAFTKGVEKAGPNSSDQIVAMLYQNRAACREKVGHSPFDILNDCMAALKVDKKYTKAYLRAAKALNDVGKKQDALAYLLAAFTLDSSLNKTNFEFFGKLLAIEPMSDCHIGKPLKIEDVKPQPVALFRIQQWCDTWDILDLFKTDLTRFEPEVLSEDQKQYQLALEKFKKGKYEELIDLLTEENSYPPAMILRGKMLSYSTDPNEATRYIDKVGAKINELIGSEEDEERKKLMRDAFDILKIELMYTMADLDKFLESVPKDDKERLFKLYSFASIFVVIRLNHFYSLKIWFQYNGCVLDTAVTNHEQQMMADTNNANRLLTEAEKNGTLTPHLSMIVTFLKLCTSEDYADVHRRIREMEELAESRSTHFNLVLMSKVYMMTNNEESSKKLLEEAARITTRYLVPSRHLQTADLHVHKPEAERLRLTTESANAAIAVDPFNFSAHVLHLLGTNGPEPMIKKENYERAMESIRNAALFAPPRELLMLKRMIPLMNAKKRAAEMLDMY
Protein: Patched-related protein 9 (Q03602)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MKSLNFQSVVSQFFEYESTVVVRWPLPFIIIPPLLTFSIVTLTVTNFHLNVTNDTLQVFLPDDMRSLRDLKELLRLFPPRDAQRDTYSIFGSKFVYTVIEDDSSDGNILSSSGIQRMSKLHKFVMGLETSLGDNVASNCLRNKDDEACTMHPIAFALEDTTPEFAIQFLLRYPNLKFGDFVIDNAMVFGDVRIEPKSQDRDGNSPIRSSKAVRMTYILESSESTERWIDLFLSAIPRYKETNSTIFWSSSKSLAKEMERNGELLIPWMPWTSLVLVVFCMFACSSLNIVKSQPFIGFFAMFNATMATIASTSLLLYLQYPFLPLVFIMPFLVVSIGTDNMFLMLKSWRMTKKSSNEEQRYIHALTESAASLFLTSLTDGLSFAIGSISDFHAVRVFCTYCAMAILFMFLFQVTFFNAVMSLCCRREVSGKHPVFCCYEITPPEETQVLEKQSNFDFSSIVAKHLFKILNPLPSRIGVFFIFLAYLFISIHFAIGLPLGLDLKLLAPDDSYVSKELEAQERLFADYGGFCFALVRAENISLKDPMVRRNLIGLYRDLGGSEYSSPSEFWLDPFEKKNRGKKYSESDFSDELHTFLAKEPHLKFRNDIRFTMMGKIEAMKMMFRVRKLGKDNDAPRAEYMRKVMENSQFNGFVYDTSFLLVDQQMTTVYNVIVDVVSAILTMLSICVLMVPRPVSAMCIAFAILSVNIGVIGALAATNTRLDIISMITIVMSVGFSVDYVTHTTFHFVIQRDNRLEKCLLVMTEPILQSALSTAIGVSLLSFVHSYIVRTFVNTVFFVVGLGILHGLIFLPVLLDTIVPDSEYMVPYEPQHEDEENPNHYEDLYGL
Protein: Kell metallo-endopeptidase (Kell blood group) (E9PHG0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEGGDQSEEEPRERSQAGGMGTLWSQESTPEERLPVEGSRPWAVARRVLTAILILGLLLCFSVLLFYNFQNCGPRPCETSVCLDLRDHYLASGNTSVAPCTDFFSFACGRAKETNNSFQELATKNKNRLRRILEVQNSWHPGSGEEKAFQFYNSCMDTLAIEAAGTGPLRQVIEEIFREYLTYL
Protein: Zinc finger protein 212 (G3X8R7)
Organism: Mus musculus (Mouse)
Interaction partners:
- Transcription intermediary factor 1-beta
Sequence:
MAESTPTRHRRKRRATPLAPATPPSQTTEKSPYFQTTEISLWTVVAAIQAVEKKMESQAARLQSLEGRAGSAEKKLADFEKTAVEFSNQLEGKWAVLGTLLQEYGLLQRRLENVENLLRNKNFWVLRLPPGSKGETPKVSGSLENDGVCFSEQEWENLEDWQKELYRNVMESNYETLVSLKVLGQPEEEVELGAEMVGDLVEEGTHLADRAMVKQEMLYKQEGPAGLPNMFSSAVEQQAFFGAEQAMFWNSPGDSALLESGPGDSNPESVETSRDPAPGRNLDCPRKQKSHRQVQLGQECGQGLKVKRDSSPYKCPECQISFRYKQQLTAHLQSHAGRESYSATEPEESLRPRPRLKPQAKRSKLHQCDVCHRSFSCKVSLVTHQRCHQQEGPSTSPQIQERFSPNSLVALPGHIPWRKSRSSLICGYCGKSFSHPSDLVRHQRIHTGERPYSCPECEKSFVQKQHLLQHQKIHQRERGGLASESARPNGLL
Protein: Jumonji, AT rich interactive domain 1B (RBP2-like), isoform CRA_a (Lysine demethylase 5B) (cDNA FLJ16281 fis, clone NT2RI3003104, highly similar to Homo sapiens Jumonji, AT rich interactive domain 1B (RBP2-like) (JARID1B), mRNA) (B3KV94)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGFAPGKAVGSHIRGHYERILNPYNLFLSGDSLRCLQKPNLTTDTKDKEYKPHDIPQRQSVQPSETCPPARRAKRMRAEAMNIKIEPEETTEARTHNLRRRMGCPTPKCENEKEMKSSIKQEPIERKDYIVENEKEKPKSRSKKATNAVDLYVCLLCGSGNDEDRLLLCDGCDDSYHTFCLIPPLHDVPKGDWRCPKCLAQECSKPQEAFGFEQAARDYTLRTFGEMADAFKSDYFNMPVHMVPTELVEKEFWRLVSTIEEDVTVEYGADIASKEFGSGFPVRDGKIKLSPEEEEYLDSGWNLNNMPVMEQSVLAHITADICGMKLPWLYVGMCFSSFCWHIEDHWSYSINYLHWGEPKTWYGVPGYAAEQLENVMKKLAPELFVSQPDLLHQLVTIMNPNTLMTHEVPVYRTNQCAGEFVITFPRAYHSGFNQGFNFAEAVNFCTVDWLPLGRQCVEHYRLLHRYCVFSHDEMICKMASKADVLDVVVASTVQKDMAIMIEDEKALRETVRKLGVIDSERMDFELLPDDERQCVKCKTTCFMSAISCSCKPGLLVCLHHVKELCSCPPYKYKLRYRYTLDDLYPMMNALKLRAESYNEWALNVNEALEAKINKKKSLVSFKALIEESEMKKFPDNDLLRHLRLVTQDAEKCASVAQQLLNGKRQTRYRSGGGKSQNQLTVNELRQFVTQLYALPCVLSQTPLLKDLLNRVEDFQQHSQKLLSEETPSAAELQDLLDVSFEFDVELPQLAEMRIRLEQARWLEEVQQACLDPSSLTLDDMRRLIDLGVGLAPYSAVEKAMARLQELLTVSEHWDDKAKSLLKARPRHSLNSLATAVKEIEEIPAYLPNGAALKDSVQRARDWLQDVEGLQAGGRVPVLDTLIELVTRGRSIPVHLNSLPRLETLVAEVQAWKECAVNTFLTENSPYSLLEVLCPRCDIGLLGLKRKQRKLKEPLPNGKKKSTKLESLSDLERALTESKETASAMATLGEARLREMEALQSLRLANEGKLLSPLQDVDIKICLCQKAPAAPMIQCELCRDAFHTSCVAVPSISQGLRIWLCPHCRRSEKPPLEKILPLLASLQRIRVRLPEGDALRYMIERTVNWQHRAQQLLSSGNLKFVQDRVGSGLLYSRWQASAGQVSDTNKVSQPPGTTSFSLPDDWDNRTSYLHSPFSTGRSCIPLHGVSPEVNELLMEAQLLQVSLPEIQELYQTLLAKPSPAQQTDRSSPVRPSSEKNDCCRGKRDGINSLERKLKRRLEREGLSSERWERVKKMRTP
Protein: E1B 55 kDa protein (E1B-55K) (E1b55K) (E1B protein, large T-antigen) (E1B-495R) (P03243)
Organism: Human adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5)
Function: Plays a major role to prevent cellular inhibition of viral genome replication. Assembles an SCF-like E3 ubiquitin ligase complex based on the cellular proteins ELOB, ELOC, CUL5 and RBX1, in cooperation with viral E4orf6. This viral RING-type ligase ubiquitinates cellular substrates and targets them to proteasomal degradation: TP53/p53, LIG4, MRE11-RAD50-NBS1 (MRN) complex, ITGA3, DAXX and BLM. Degradation of host TP53/p53 activity is essential for preventing E1A-induced TP53 accumulation that would otherwise lead to cell apoptosis and growth arrest. E1B-55K also inactivates TP53 transcription-factor activity by binding its transactivation domain. E1B-55K also functions as a SUMO1 E3 ligase for TP53 which causes the latter to be sequestered in promyelocytic leukemia (PML) nuclear bodies thereby contributing to maximal inhibition of TP53 function.
Subcellular location: Host nucleus {ECO:0000269|PubMed:10211970, ECO:0000269|PubMed:20861261}. Host cytoplasm {ECO:0000269|PubMed:10211970, ECO:0000269|PubMed:18614635}. Note=Colocalizes with host TP53 to host PML nuclear bodies. PML localization of E1B-55K is necessary for E1B-55K-dependent SUMOylation of TP53. {ECO:0000269|PubMed:20861261}.
Interaction partners:
Sequence:
MERRNPSERGVPAGFSGHASVESGCETQESPATVVFRPPGDNTDGGAAAAAGGSQAAAAGAEPMEPESRPGPSGMNVVQVAELYPELRRILTITEDGQGLKGVKRERGACEATEEARNLAFSLMTRHRPECITFQQIKDNCANELDLLAQKYSIEQLTTYWLQPGDDFEEAIRVYAKVALRPDCKYKISKLVNIRNCCYISGNGAEVEIDTEDRVAFRCSMINMWPGVLGMDGVVIMNVRFTGPNFSGTVFLANTNLILHGVSFYGFNNTCVEAWTDVRVRGCAFYCCWKGVVCRPKSRASIKKCLFERCTLGILSEGNSRVRHNVASDCGCFMLVKSVAVIKHNMVCGNCEDRASQMLTCSDGNCHLLKTIHVASHSRKAWPVFEHNILTRCSLHLGNRRGVFLPYQCNLSHTKILLEPESMSKVNLNGVFDMTMKIWKVLRYDETRTRCRPCECGGKHIRNQPVMLDVTEELRPDHLVLACTRAEFGSSDEDTD
Protein: Charged multivesicular body protein 2a (Chromatin-modifying protein 2a) (CHMP2a) (Vacuolar protein sorting-associated protein 2) (mVps2) (Q9DB34)
Organism: Mus musculus (Mouse)
Function: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis. Together with SPAST, the ESCRT-III complex promotes nuclear envelope sealing and mitotic spindle disassembly during late anaphase. Recruited to the reforming nuclear envelope (NE) during anaphase by LEMD2 (By similarity). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4.
Subcellular location: Late endosome membrane {ECO:0000250|UniProtKB:O43633}; Peripheral membrane protein {ECO:0000250|UniProtKB:O43633}; Cytoplasmic side {ECO:0000250|UniProtKB:O43633}. Cytoplasm {ECO:0000269|PubMed:15173323}. Nucleus envelope {ECO:0000250|UniProtKB:O43633}. Note=Localizes to the midbody of dividing cells. Localized in two distinct rings on either side of the Fleming body. Localizes to the reforming nuclear envelope on chromatin disks during late anaphase (By similarity). {ECO:0000250|UniProtKB:O43633}.
Interaction partners:
- Charged multivesicular body protein 3
- Charged multivesicular body protein 6
- Charged multivesicular body protein 4b
- Charged multivesicular body protein 1a
- Charged multivesicular body protein 1B1
- Charged multivesicular body protein 1B2
- Charged multivesicular body protein 5
- Vacuolar protein sorting-associated protein 4B
- Charged multivesicular body protein 4c
- Charged multivesicular body protein 2b
Sequence:
MDLLFGRRKTPEELLRQNQRALNRAMRELDRERQKLETQEKKIIADIKKMAKQGQMDAVRIMAKDLVRTRRYVRKFVLMRANIQAVSLKIQTLKSNNSMAQAMKGVTKAMGTMNRQLKLPQIQKIMMEFERQAEIMDMKEEMMNDAIDDAMGDEEDEEESDAVVSQVLDELGLSLTDELSNLPSTGGSLSVAAGGKKAEATASALADADADLEERLKNLRRD
Protein: Early E1A protein (Early E1A 32 kDa protein) (P03255)
Organism: Human adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5)
Function: Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle. Stimulation of progression from G1 to S phase allows the virus to efficiently use the cellular DNA replicating machinery to achieve viral genome replication. E1A protein has both transforming and trans-activating activities. Induces the disassembly of the E2F1 transcription factor from RB1 by direct competition for the same binding site on RB1, with subsequent transcriptional activation of E2F1-regulated S-phase genes and of the E2 region of the adenoviral genome. Release of E2F1 leads to the ARF-mediated inhibition of MDM2 and causes TP53/p53 to accumulate because it is not targeted for degradation by MDM2-mediated ubiquitination anymore. This increase in TP53, in turn, would arrest the cell proliferation and direct its death but this effect is counteracted by the viral protein E1B-55K. Inactivation of the ability of RB1 to arrest the cell cycle is critical for cellular transformation, uncontrolled cellular growth and proliferation induced by viral infection. Interaction with RBX1 and CUL1 inhibits ubiquitination of the proteins targeted by SCF(FBXW7) ubiquitin ligase complex, and may be linked to unregulated host cell proliferation. The tumorigenesis-restraining activity of E1A may be related to the disruption of the host CtBP-CtIP complex through the CtBP binding motif. Interaction with host TMEM173/STING impairs the ability of TMEM173/STING to sense cytosolic DNA and promote the production of type I interferon (IFN-alpha and IFN-beta). Promotes the sumoylation of host ZBED1/hDREF with SUMO1.
Subcellular location: Host nucleus {ECO:0000269|PubMed:25194920, ECO:0000269|PubMed:25210186}.
Interaction partners:
Sequence:
MRHIICHGGVITEEMAASLLDQLIEEVLADNLPPPSHFEPPTLHELYDLDVTAPEDPNEEAVSQIFPDSVMLAVQEGIDLLTFPPAPGSPEPPHLSRQPEQPEQRALGPVSMPNLVPEVIDLTCHEAGFPPSDDEDEEGEEFVLDYVEHPGHGCRSCHYHRRNTGDPDIMCSLCYMRTCGMFVYSPVSEPEPEPEPEPEPARPTRRPKMAPAILRRPTSPVSRECNSSTDSCDSGPSNTPPEIHPVVPLCPIKPVAVRVGGRRQAVECIEDLLNEPGQPLDLSCKRPRP