wanglab/gogpt-training-data huggingface dataset:
Protein: Cytoplasmic polyadenylation element binding protein 3 (A0A8I6GA10)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MQDDLLMDKSKTQPQSQQQQQQQQQQQQQQQQQQQQRQQQQQQQQQLQPEPGAAEAPSTPLSSETPKPEDSSAVPALSPASAPPAPNGPDKMQMESPLLPGLSFHQPPQQPPPPQEPAAPGASLSPSFGSTWSTGTTNAVEDSFFQGITPVNGTMLFQNFPHHVNPVFGGTFSPQIGLAQTQHHQQPPPPAPQPPQPAQPPQAQPSQQRRSPASPSQAPYAQRSAAAYGHQPIMTSKPSSSSAAAAAAAAAAASSASSSWNTHQSVNAAWSAPSNPWGGLQAGRDPRRAVGVGVGVGVGVPSPLNPISPLKKPFSSNVIAPPKFPRAAPLTSKSWMEDNAFRTDNGNNLLPFQDRSRPYDTFNLHSLENSLMDMIRTDHEPLKGKHYPPSGPPMSFADIMWRNHFAGRMGINFHHPGTDNIMALNTRSYGRRRGRSSLFPFEDAFLDDSHGDQALSSGLSSPTRCQNGERVERYSRKVFVGGLPPDIDEDEITASFRRFGPLVVDWPHKAESKSYFPPKGYAFLLFQEESSVQALIDACLEEDGKLYLCVSSPTIKDKPVQIRPWNLSDSDFVMDGSQPLDPRKTIFVGGVPRPLRAVELAMIMDRLYGGVCYAGIDTDPELKYPKGAGRVAFSNQQSYIAAISARFVQLQHNDIDKRVEVKPYVLDDQMCDECQGTRCGGKFAPFFCANVTCLQYYCEYCWASIHSRAGREFHKPLVKEGGDRPRQVPFRWS
Protein: Mediator of RNA polymerase II transcription subunit 13 (F1LXU0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU364134}.
Interaction partners:
- Cyclin-C
- Mediator complex subunit 12
- Mediator of RNA polymerase II transcription subunit 1
- Mediator of RNA polymerase II transcription subunit 14
- cyclin-dependent kinase
- Mediator of RNA polymerase II transcription subunit 19
- Mediator complex subunit 12L
- Mediator of RNA polymerase II transcription subunit 4
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 24
Sequence:
MSSSFVSNGASLEDCHCNLFCLADLTGIKWKRYVWQGPTSAPILFPVTEEDPILSSFSRCLKADVLGVWRRDQRPGRRELWIFWWGKDPNFADLIHHDLSEEEDGVWENGLSYECRTLLFKAVHNLLERCLMNRNFVRIGKWFVKPYEKDEKPINKSEHLSCSFTFFLHGDSNVCTSVEINQHQPVYLLSEEHVTLAQQSNSPFQVILSPFGLNGTLTGQAFKMSDSATKKLIGEWKQFYPISCGLKEMSEEKQEDMDWEDDSLAAVEVLVAGVRMIYPACFVLVPQSDIPTPSSVGSSHCSASCLGIHQVPASTRDPAMSSVTLTPPTSPEEVQSVDPQSAQKWVKFSSVSDGFSTDSTSHHGGKIPRKLANHVVDRVWQECNMNRLQNKRKYSATSSGLCEEETADKIGSWDFVEATQRTSCSCLRHKSLKTRNTGQQGQAPSLGQQQQILPKHKTNEKQEKSEKPQKRPLTPFHHRVSISDDIGMDTDSASQRLVISAADSQVRFTNIRTNDVAKTPQMHGTELANSPQPPPLSPHPCDVVDEGVTKTPSTPQSQHFYQMPTPDPLVPTKPMEDRIDSLSQSFPPPFQEAVEPTVYVGTAVSLEEDEANVAWKYYKVPKKKDVEFLPPQLPNDKFKDDPVGPFGQESVTSVTELMVQCKKPLKVSDEIVQQYQIKNQYLSAIASDTEQEPKIDPYAFVEGDEEFIFTDKKDRQNSEREAGKKHKVEDGTSAVTVLSHEEDAMSLFSPSKQDAPRPANHARPPSTSLIYDSDLAVSYTDLDNLFNSDEDELTPGSKKSASGSDDKASSKESKTGSLDPLSCISTADLHKMYPTPPSLEQHIMGFSPMNMNNKEYGSMDPTPGGTVLEGSSSSVGTQFRIEVEEGFCSPKPSEIKDFSYVYKPENCQVLVGCSMFAPLKTLPSHCLPPIKLPEECVYRQSWTVGKLDLLPSGPSMPFIKEGDGSNLDQDYGPAYTPQIHTSFGMPPSSAPPSNGGAGILPSPSTPRFPTPRTPRTPRTPRGAGGPASAQGSVKYENSDLYSPASTPSTCRPLNSVEPATVPSIPEAHSLYVNLILSESVMNLFKDCNFDSCCICVCNMNIKGADVGVYIPDPTQEAQYRCTCGFSAVMNRKFGNNSGLFLEDELDIIGRNTDCGKEAEKRFEALRASSVENVNGSLKESEKVPDELILLLQDQCTNLFSPFGAADHDPFPKAGISSNWVRVEERDCCSDCCLALEHGRQFMDNMSGGKVDEALVRSSCLHPWAKQNDASVQCSQDILRMLLSLQPVLQDAIQKKRTVRPWGVQGPLTWQQFHKMAGRGSYGTDESPEPLPIPTFLLGYDYDFLVLSPFALPYWEKLMLEPYGSQRDIAYVVLCPENEALLNGARSFFRDLTAIYESCRLGQHRPISRLLTDGIMKVGATASKKLSEKFVTEWFSQAADGNNEAFSKLKLYAQVCRYDLGPYLASQPLDSSLLSQPNLVAPPNQSLVTAPQMTNTGNANAPSATLASAASSTMTLTPGVAISTSVATANSTLTTTSSSSSSSMSSGVSSNKLPSFPPFGSMNTSGTGSMSAQGSTVQSGQLGGQQSSSLQAAGISGESASLPTQPHPDVSESTMDRDKVGIPTDGDSHAITYPPAIVVYIIDPFTYENKDESTSSSNVWTLGLLRCFLEMLQTLPPHIKSTVSVQIVPCQYLLQPVKHDDRQIYSQHLKSLAFSAFTQCRRPLPTSTNVKTLTGFGPGLAMETALKSPDRPECIRLYTPPFILAPVKDKQTELGETFGEAGQKYNVLFVGYCLSHDQRWILASCTDLYGELLETCIINIDVPNRARRKKGSARRFGLQKLWEWCLGLVQMSSLPWRVVIGRLGRIGHGELKDWSCLLSRRNLQSLSKRLKDMCRMCGISAADSPSILSACLVAMEPQGSFVIMPDSVSTGSVFGRSTTLNMQTPQLNTPQDTSCTHILVFPTSASVQVASATYTTENLDLAFNPNNDGADGMGIFDLLDTGDDLDPDIINILPASPTTSPVHSPGSHYPHGGDAGKGQGTDRLLSTESHDEVTNILQQPLALGYFVSTAKAGPLPDWFWSACPQAQYQCPLFLKASLHLHVPSVQSDELLHSKHSHPLDSNQTSDVLRFVLEQYNALSWLTCDPAIQDRRSCLPIHFVVLNQLYNFIMNML
Protein: Leucine-rich repeat-containing protein 49 (Tubulin polyglutamylase complex subunit 4) (PGs4) (p79) (Q91YK0)
Organism: Mus musculus (Mouse)
Function: Subunit of the tubulin polyglutamylase complex (TPGC). The complex mediates cilia and flagella polyglutamylation which is essential for their biogenesis and motility.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q8IUZ0}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000250|UniProtKB:Q8IUZ0}. Note=Associated with microtubules. {ECO:0000250|UniProtKB:Q8IUZ0}.
Interaction partners:
- Tubulin polyglutamylase complex subunit 1
- Polyglutamylase complex subunit TTLL1
- Nicolin-1
Sequence:
MIPGKYRSVSGRAANNVNCGLHLVIQTSSLSDKNKVEFRLNRETPPFPGRLLQHDLERNYSSRQGDHISLVSSSMPAFPILQRSSEEKTLYSDRLTLERQKLTVCPIIDGEEHLRLLNFQHNFITRIQNISNLQRLIFLDLYDNQIEEISGLSTLKSLRVLLLGKNRIKKISNLENLKNLDVLDLHGNQITKIENVNHLCDLRVLNLARNLLSHVDNLNGLDSLTELNLRHNQITFVRDVDNLPCLQRLFLSFNNITSFESVSCLAESTSLSDITFDGNPIAQESWYKHTVLQNMMQLRQLDMKRITEEERRVASVVPKKEEEKKRESHKQSLLKEKKRLTINNVARKWDLQQRVANIASTQDRKDSESPPQESCQLDGGNISAFPEEAGSLDAGLSSALQGLSVTETHLVEIDGETLSLYGSGALECLDRNWSVQTAGMVTTVSFTFIEFDEIVQVLPKLKMKFPNSLHLKFRETNLVMLQQFNALAQLRRVDQLTIDPQGNPVVNFTLWKYYVLFRLSHFSMQKINGTEVTQNDMIMAERLFGILAHVASSELPQYRMISILGDARKKQFRYLLESKGKKPGIICEETSDSKRFLGENTNRATLNYTTREFYHEKLEEIKDKKKFCRLYVEDLVKEATAINMKNEALQKLWPQMFIELVRDAVIEIRSKDSYMKLCLQQITDQK
Protein: Prefoldin subunit 2 (Q9N5M2)
Organism: Caenorhabditis elegans
Function: Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins (By similarity).
Interaction partners:
- Probable prefoldin subunit 5
- Probable prefoldin subunit 6
- Probable prefoldin subunit 4
- Probable prefoldin subunit 3
- Probable prefoldin subunit 1
- Spindle and kinetochore-associated protein 2
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- Unconventional prefoldin RPB5 interactor
- EGF-like domain-containing protein
- EGF-like domain-containing protein
Sequence:
MSAAQTAAATPAEQEEQRKVVEKFKALRDQQQDIAAEVTRIEEERREFGRVLEVIKDLEPDQKCFRLISDTLVEYTVKDVIPDLQNNIANLTIVSKQLNDQLVEKGKELNTHKTTHNIRLLTEKESAELRKAEALGQLPKA
Protein: Nucleolin (C9JLB1)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
Sequence:
MAPPPKEVEEDSEDEEMSEDEEDDSSGEEVVIPQKKGKKAAATSAKKVVVSPTKKVAVATPAKKAAVTPGKKAAATPAKKTVTPAKAVTTPGKKGATPGKALVATPGKKGAAIPAKGAKNGKNAKKEDSDEEEDDDSEEDEEDDEDEDEDEDEIEPAAMKAAAAAPASEDEDDEDDEDDEDDDDDEEDDSEEEAMETTPAKGKKAAKVVPVKAKNVAEDEDEEEDDEDEDDDDDEDDEDDDDEDDEEEEEEEEEEPVKEAPGKRKKEMAKQKAAPEAKKQKVEGTEPTTAFNLFVGNLNFNKSAPELKTGISDVFAKNDLAVVDVRIGMTRKFGYVDFESAEDLEKALELTGLKVFGNEIKLEKPKGKDSKKERDARTLLAKNLPYKVTQDELKEVFEDAAEIRLVSKDGKSKGIAYIEFKTEADAEKTFEEKQGTEIDGRSISLYYTGEKGQNQDYRGGKNSTWSGESKTLVLSNLSYSATEETLQEVFEKATFIKVPQNQNGKSKGYAFIEFASFEDAKEALNSCNKREIEGRAIRLELQGPRGSPNARSQPSKTLFVKGLSEDTTEETLKESFDGSVRARIVTDRETGSSKGFGFVDFNSEEDAKAAKEAMEDGEIDGNKVTLDWAKPKGEGGFGGRGGGRGGFGGRGGGRGGRGGFGGRGRGGFGGRGGFRGGRGGGGDHKPQGKKTKFE
Protein: APOBEC1 complementation factor (F8W9F8)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MEAVCLGTCPEPEASMSTAIPGLKKGNNALQSIILQTLLEKENGQRKYGGPPPGWDAAPPERGCEIFIGKLPRDLFEDELIPLCEKIGKIYEMRMMMDFNGNNRGYAFVTFSNKVEAKNAIKQLNNYEIRNGRLLGVCASVDNCRLFVGGIPKTKKREEILSEMKKVTEGVVDVIVYPSAADKTKNRGFAFVEYESHRAAAMARRKLLPGRIQLWGHGIAVDWAEPEVEVDEDTMSSVKILYVRNLMLSTSEEMIEKEFNNIKPGAVERVKKIRDYAFVHFSNREDAVEAMKALNGKVLDGSPIEVTLAKPVDKDSYVRYTRGTGGRGTMLQGEYTYSLGQVYDPTTTYLGAPVFYAPQTYAAIPSLHFPATKGHLSNRAIIRAPSVREIYMNVPVGAAGVRGLGGRGYLAYTGLGRGYQVKGDKREDKLYDILPGMELTPMNPVTLKPQGIKLAPQILEEICQKNNWGQPVYQLHSAIGQDQRQLFLYKITIPALASQNPAIHPFTPPKLSAFVDEAKTYAAEYTLQTLGIPTDGGDGTMATAAAAATAFPGYAVPNATAPVSAAQLKQAVTLGQDLAAYTTYEVYPTFAVTARGDGYGTF
Protein: Cullin 1, putative (Q383D5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Elongin-C
- Ubiquitin, putative
- COP9 signalosome complex subunit 2, putative
- COP9 signalosome complex subunit 5
- COP9 signalosome complex subunit 3 N-terminal helical repeats domain-containing protein
- JAB1/MPN/MOV34 metalloenzyme domain-containing protein
- TATA-binding protein interacting
- RING-type domain-containing protein
- RING-type domain-containing protein
- COP9 signalosome complex subunit 4
Sequence:
MEQTNHDDVSSAEVARAYSGSLGASSFQFTPLWESVDYVCSIILSWYDFPDFKGGEALQQLVRAYTIVCRLVSSPCAGCPPLARPSVEGDIVTAAEVTQSLVVYSRICDMIRKRLDTVVGMRFRDAAEQPPPRLLEDYIVEWKRFITSVNMLKFVFSYLHGPWQKYGVPPGLMQSTEVIALNKWSEMLMNTNFQEALTNQIFELVAMDRHHHPNMERAQILREVGHALGVVSDARSNWYVTLVEERYLRQLTDFCKLKTEEMKLGDVEHYIEEALTIFRDETERAIRLLAQSSIQPVVQRIAEVLINDELSFLDEFISSEIVKNRVTQLRQLYSLLSQSQVGLRHLRDEFKKCVIEKGRREINEACERAKNSNTGVYQVALEKVISVYRDFQLPMKAFGDKGDFEKELIDGLHNVLTACSYLDPQNMLGREVARFAHNELISRKLGVRCEEDEGNMNNIVILFRVLPTKNLFVETYPMYLCSRLLSTEYVVENERLLIQEITQTGECTRDFMNKCATMLNDVGEVSERLSEQFREKAGLTDLNFHPTVLNSYFWPNFLPEPEMAIPGYLQMKLLEFGKFFQDVCPRRHISYVNRLSQGVLRFNLSDASPVQGLDICVGVRHLPVAELFNCCAEWELQELIQSVGNDNSNSCLSAINDFAKHGILDIHEEGGVTLKSHLREVLPGCRVSIGRTPDIRNRKIVLHETKLDRETKVDGAGSSDFSPERYDVNTTTEQMVALSTQATLIRAFKSEGTASFSQLFERVENESPAHLKPSIQQMKVALEFLISREFVRRNEDGTDTFSYVT
Protein: Small RNA 2'-O-methyltransferase (EC 2.1.1.386) (HEN1 methyltransferase homolog 1) (mHEN1) (Q8CAE2)
Organism: Mus musculus (Mouse)
Function: Methyltransferase that adds a 2'-O-methyl group at the 3'-end of piRNAs, a class of 24 to 30 nucleotide RNAs that are generated by a Dicer-independent mechanism and are primarily derived from transposons and other repeated sequence elements. This probably protects the 3'-end of piRNAs from uridylation activity and subsequent degradation. Stabilization of piRNAs is essential for gametogenesis.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q568P9}. Note=Component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis. {ECO:0000250|UniProtKB:Q568P9}.
Interaction partners:
- ATP-dependent RNA helicase TDRD9
- Mitochondrial cardiolipin hydrolase
- Tudor and KH domain-containing protein
- Piwi-like protein 2
- Tudor domain-containing protein 1
- Ankyrin repeat, SAM and basic leucine zipper domain-containing protein 1
- RNA helicase Mov10l1
- Piwi-like protein 1
- Protein maelstrom homolog
- Piwi-like protein 4
Sequence:
MEMAESIPCNSVVGGNFKEVSPEKVIRFKPPLYKQRYQFVRDLVDRHEPKKVADLGCGDAKLLKLLKIYPCIQLLVGVDINEEKLHSNGHRLSPYLGEFVKPRDLDLTVTLYHGSVVERDSRLLGFDLITCIELIEHLDSDDLARFPDVVFGYLSPAMVVISTPNAEFNPLFPTVTLRDADHKFEWSRMEFQTWALHVANCYNYRVEFTGVGTPPAGSEHVGYCTQIGVFTKNGGKLSKPSVSQQCDQHVYKPVYTTSYPSLQQEKVLKFVLVGELLIQVDRLRLRYQRMLRDREKDRGPKPGDMDSCPAPHLLLGAVFTEAEKARIESSPKPFCEGEKFYIPLQRLLTYPKLHRLCADEDRVRSLIADSVCLSSDGSAVVVDLHNSWDYRPEEN
Protein: RE46851p (Q8SYQ0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cleavage furrow {ECO:0000256|ARBA:ARBA00004626}. Midbody {ECO:0000256|ARBA:ARBA00004214}. Recycling endosome membrane {ECO:0000256|ARBA:ARBA00004654}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004654}.
Interaction partners:
Sequence:
MAPMPRIQLPNGNSSIKASTNDFLFAETMSGGSSPTPSSPPSSTAGVAKSQCSSLSDGESFEGYGENEYPTQLREARSSNSNGSHNMSNHINNNSNISVGNNSGHNHSGHSNDGNNNLNGSTGVELDLAPHVGSSTPQDDDELNIMPRDNWARRSLRRTPTSSGRRQISSNALASQLYRSSSFNSSGRSSNCDTTEDMYSDISLENRHDYDYRLELLQRKVDDLSDTQNIAEDRTTRTKTEYAVLQARYHMLEEQYRESELRAEERLAEEQKRHREILARVEREASLQNENCQMKIRATEIEATALREEAARLRVLCDKQANDLHRTEEQLELARDQIGVLQQEHEEQAQALRRHEQEKKSTEELMLELGRELQRAREESGARAMPTTSPESIRLEELHQELEEMRQKNRTLEEQNEELQATMLTNQATMLTNGVEQGRHLLNGTLNSLAQELEEMSQAQLQQAFQEKEDENVRLKHYIDTILLNIVENYPQLLEVKPMERK
Protein: Beta-glucosidase C (EC 3.2.1.21) (Beta-D-glucoside glucohydrolase C) (Cellobiase C) (Gentiobiase C) (Q5BCC6)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Probable glucan endo-1,3-beta-glucosidase eglC
- Glycosyl hydrolases family 32 superfamily
Sequence:
MRVDSTVLALVALATDCLGLAIKSNEPELLRRDALPIYKNASYCVDERVRDLLSRMTLEEKAGQLFHKQLSEGPLDDDSSGNSTETMIGKKHMTHFNLASDITNATQTAEFINLIQKRALQTRLGIPITISTDPRHSFTENVGTGFQAGVFSQWPESLGLAALRDPQLVREFAEVAREEYLAVGIRAALHPQVDLSTEPRWARISGTWGENSTLTSELIVEYIKGFQGEGKLGPKSVKTVTKHFPGGGPMENGEDSHFYYGKNQTYPGNNIDEHLIPFKAALAAGATEIMPYYSRPIGTNWEAVGFSFNKEIVTDLLRGELGFDGIVLTDWGLITDTYIGNQYMPARAWGVEYLSELQRAARILDAGCDQFGGEERPELIVQLVREGTISEDRIDVSVARLLKEKFLLGLFDNPFVNASAANNIVGNEHFVNLGRDAQRRSYTLLTNNQTILPLAKPGEGTRFYIEGFDSAFMSARNYTVVNTTEEADFALLRYNAPYEPRNGTFEANFHAGSLAFNATEKARQAKIYSSLPTIVDIILDRPAVIPEVVEQAQAVLASYGSDSEAFLDVVFGVSKPEGKLPFDLPRSMDAVEAQAEDLPFDTENPVFRYGHGLEYEDN
Protein: 26S proteasome regulatory subunit 6A (O14126)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex (By similarity).
Subcellular location: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
Interaction partners:
- 26S proteasome regulatory subunit rpn10
- 26S proteasome regulatory subunit 6B homolog
- Probable 26S proteasome regulatory subunit rpn6
- 26S proteasome regulatory subunit rpn12
- 26S proteasome regulatory subunit rpn1
- 26S proteasome regulatory subunit rpn2
- Probable 26S proteasome regulatory subunit rpn9
- 26S proteasome regulatory subunit rpn502
- 26S proteasome regulatory subunit 4 homolog
- 26S proteasome regulatory subunit rpn7
Sequence:
MSTLEELDALDQSQQGGSSNNEGLDGIEQEILAAGIDELNSRTRLLENDIKVMKSEFQRLTHEKSTMLEKIKENQEKISNNKMLPYLVGNVVEILDMQPDEVDVQESANQNSEATRVGKSAVIKTSTRQTIFLPLIGLVEPEELHPGDLIGVNKDSYLIIDKLPSEYDSRVKAMEVDEKPTERYSDIGGLSKQIEELFEAIVLPMQQADKFRKLGVKPPKGCLMFGPPGTGKTLLARACAAQSNATFLKLAAPQLVQMFIGDGAKLVRDAFALAKEKSPAIIFIDELDAIGTKRFDSEKAGDREVQRTMLELLNQLDGFSSDDRVKVIAATNRVDTLDPALLRSGRLDRKLEFPLPNEEARVGILRIHSRKMAIDDDINWEELARSTDEYNGAMLKSVCVEAGMIALRQGDTKINHEHFMDGILEVQMRKSKTLQYFA
Protein: Protein ROOT PRIMORDIUM DEFECTIVE 1 (Q689D6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in pre-arranging the maintenance of the active cell proliferation during root primordium development. Does not seem to be involved in cell cycle progression.
Interaction partners:
Sequence:
MKLFLRNAFKTLNPKRKLATTILPSINLILVKPFSQSTTIPKKQDRVRDHGYDNYMEVEKKIRKVVKFHSLILSQPNHTIAISLLDTLARRLGLGFKQHEPGAFLLKFPHVFEIYEHPVQRILYCRLTRKALDQIRHEHEAVLDQIPDAVTRLRKLVMMSNTGRIRLEHVRIARTEFGLPEDFEYSVILKHPQFFRLIDGEETRDKYIEIVEKDPNLSICAIERVREIEYRTKGIDAEDVRFSFVVNFPPGFKIGKYFRIAVWKWQRLPYWSPYEDISGYDLRSMEAQNRLEKRSVACIHELLSLTVEKKITLERIAHFRNVMNLPKKLKEFLLQHQGIFYISTRGNYGKLHTVFLREGYKRGELVEPNDVYLARRRLAELVLMSPRKAKVDAELVRYRDGLDDEDDVE
Protein: 2-(3-amino-3-carboxypropyl)histidine synthase (EC 2.5.1.108) (Diphthamide biosynthesis protein Dph2) (S-adenosyl-L-methionine:L-histidine 3-amino-3-carboxypropyltransferase) (O58832)
Organism: Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Function: Catalyzes the first step of diphthamide biosynthesis, i.e. the transfer of the 3-amino-3-carboxypropyl group from S-adenosyl-L-methionine (SAM) to the C2 position of the imidazole ring of the target histidine residue in translation elongation factor 2 (EF-2).
Interaction partners:
- Elongation factor 2
- Diphthine synthase
- Small ribosomal subunit protein eS8
- Uncharacterized protein
Sequence:
MLHEIPKSEILKELKRIGAKRVLIQSPEGLRREAEELAGFLEENNIEVFLHGEINYGACDPADREAKLVGCDALIHLGHSYMKLPLEVPTIFVPAFARVSVVEALKENIGEIKKLGRKIIVTTTAQHIHQLKEAKEFLESEGFEVSIGRGDSRISWPGQVLGCNYSVAKVRGEGILFIGSGIFHPLGLAVATRKKVLAIDPYTKAFSWIDPERFIRKRWAQIAKAMDAKKFGVIVSIKKGQLRLAEAKRIVKLLKKHGREARLIVMNDVNYHKLEGFPFEAYVVVACPRVPLDDYGAWRKPVLTPKEVEILLGLREEYEFDEILGGPRESDEPFGISIHSTR
Protein: Ceramide kinase-like isoform 5 (G0XYF3)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MFRGRRRSRVGALEEAPPENPKAAAEPERVLLRGIFEIRRESCDVALGERALRWRRIQPELPAGGTRHDLLSKEESLELEDIFSVKLKRRCWAKHPGRDTLLGITLFICLKEQRNKLKDSTLDLINFSEDHCDIWFRQFKKILDVTEYEGHALSLLDECELRGFDGVVCVGGDGSASEAARALLLRAQKNAGVEMDCIPTLVGAELPLGFIPAGSTNALAHSLFGTPHVVTATMHIILGHIRSVDVCTFSSAGKLLCFGFSAMFGFGGRTLALAEKYRWMSPSQRRDFAIIKALAKLKPEDCKISFLLAGCSQNKQERKSQRSAESDCGGHWQTIQGQFLNISIMAMPCPCSMAPRGFTPDTRLHNGSMALRVVRNTTRSEFVKHLKRHSSVKNQFNFPFVETYIIEEVKIHPKSNSNGYSPQEEGGNHTTASEHGFPWNVDGDLMEAASEVHIRLHPRLIRLYGGSLEEMNDCKVACDCI
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q26801)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MSDVPKSQVGTDAKVAVAKKYTGEYYVKGMVGDKKSFAIEHSRGRQKKHTVNEFCVGDAIGRGAFAEVFQCWRPEEPHIVYAMKKIRKDLIVKRKQSLNVHTERDLLSDAKLRQKRVSCPWITDLVVAFQDQDFLYIVTEYCSGGDLISWLIRYDVFPEETARFYFVELVLALNALHKMGYVRRDVKPDNVLIDREGHVKLADFGLSKRDPDQAESTSVADDSYLTEDVTVDDDVKKRFRDKKERKVMFFSTVGSPAYIAPEVLIGRGYDYSCDWWSAGVILYEMIFGYPPFFNDNNTATAKKIIQFKEHLEFPKDQTTVSKEAIDLISHLIADSKERYGFEEIIRHPFCKGVPLTDSIRNEEAPFSVVLNDPKDLQYFEPAPDNADIQKQPMTAVSREDQSVFVGFTSKLCDRNQSTTCSRALGRFHELQNFSDDD
Protein: Candida glabrata strain CBS138 chromosome J complete sequence (Q6FPF8)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Lysophospholipase NTE1
- Candida glabrata strain CBS138 chromosome I complete sequence
Sequence:
MKTQVLITDVPKNKFDSKWPDTLEKKLFKEKYPQYRKHLQYFTPLPFLDRVIIILDDEAATMEIYEYLQKEEPSVVNDKSIKLYLTESLLSNRFRSRSMGESSPEDSNAASNGSADSNSAIGDKPILSLDTNPVSTGINVQSLAMGSPSLSPDRRTSLESPTLLKFANDEKAHLYREPLPTKSDSSKESSPGTTELHKSQKLTVSTDAVNKMASNTPPPLSPSITVDEFFN
Protein: Syntaxin-binding protein 5-like (Lethal(2) giant larvae protein homolog 4) (Tomosyn-2) (Q9Y2K9)
Organism: Homo sapiens (Human)
Function: Plays a role in vesicle trafficking and exocytosis inhibition. In pancreatic beta-cells, inhibits insulin secretion probably by interacting with and regulating STX1A and STX4, key t-SNARE proteins involved in the fusion of insulin granules to the plasma membrane. Also plays a role in neurotransmitter release by inhibiting basal acetylcholine release from axon terminals and by preventing synaptic fatigue upon repetitive stimulation (By similarity). Promotes as well axonal outgrowth.
Subcellular location: Cytoplasm {ECO:0000305}. Cell membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=Cytoplasmic, and associated with vesicular membranes and the plasma membrane. {ECO:0000305}.
Interaction partners:
- Syntaxin-19
- Synaptosomal-associated protein 23
- Syntaxin-1A
- Syntaxin-4
- Syntaxin-11
- Synaptosomal-associated protein 25
- Syntaxin-2
- Syntaxin-1B
- Syntaxin-3
- Synaptosomal-associated protein 29
Sequence:
MKKFNFRKVLDGLTASSPGSGSSSGSNSGGGAGSGSVHPAGTAGVLREEIQETLTSEYFQICKTVRHGFPHQPTALAFDPVQKILAIGTRTGAIRILGRPGVDCYCQHESGAAVLQLQFLINEGALVSASSDDTLHLWNLRQKRPAILHSLKFNRERITYCHLPFQSKWLYVGTERGNTHIVNIESFILSGYVIMWNKAIELSTKTHPGPVVHLSDSPRDEGKLLIGYENGTVVFWDLKSKRAELRVYYDEAIHSIDWHHEGKQFMCSHSDGSLTLWNLKSPSRPFQTTIPHGKSQREGRKSESCKPILKVEYKTCKNSEPFIIFSGGLSYDKACRRPSLTIMHGKAITVLEMDHPIVEFLTLCETPYPNEFQEPYAVVVLLEKDLIVVDLTQSNFPIFENPYPMDIHESPVTCTAYFADCPPDLILVLYSIGVKHKKQGYSNKEWPISGGAWNLGAQTYPEIIITGHADGSIKFWDASAITLQMLYKLKTSKVFEKQKVGEGKQTCEIVEEDPFAIQMIYWCPESRIFCVSGVSAYVIIYKFSRHEITTEIVSLEVRLQYDVEDIITPEPETSPPFPDLSAQLPSSRSLSGSTNTVASEGVTKDSIPCLNVKTRPVRMPPGYQAELVIQLVWVDGEPPQQITSLAVSSAYGIVAFGNCNGLAVVDFIQKTVLLSMGTIDLYRSSDLYQRQPRSPRKNKQFIADNFCMRGLSNFYPDLTKRIRTSYQSLTELNDSPVPLELERCKSPTSDHVNGHCTSPTSQSCSSGKRLSSADVSKVNRWGPGRPPFRKAQSAACMEISLPVTTEENRENSYNRSRSSSISSIDKDSKEAITALYFMDSFARKNDSTISPCLFVGTSLGMVLIISLNLPLADEQRFTEPVMVLPSGTFLSLKGAVLTFSCMDRMGGLMQPPYEVWRDPNNIDENEKSWRRKVVMNSSSASQEIGDHQYTIICSEKQAKVFSLPSQTCLYVHNITETSFILQANVVVMCSSACLACFCANGHIMIMSLPSLRPMLDVNYLPLTDMRIARTFCFTNEGQALYLVSPTEIQRLTYSQEMCDNLQDMLGDLFTPIETPEAQNRGFLKGLFGGSGQTFDREELFGEASAGKASRSLAQHIPGPGSIEGMKGAAGGVMGELTRARIALDERGQRLGELEEKTAGMMTSAEAFSKHAHELMLKYKDKKWYQF
Protein: Serine/arginine-rich splicing factor 3 (Pre-mRNA-splicing factor SRP20) (Protein X16) (Splicing factor, arginine/serine-rich 3) (P84104)
Organism: Mus musculus (Mouse)
Function: Splicing factor that specifically promotes exon-inclusion during alternative splicing. Interaction with YTHDC1, a RNA-binding protein that recognizes and binds N6-methyladenosine (m6A)-containing RNAs, promotes recruitment of SRSF3 to its mRNA-binding elements adjacent to m6A sites, leading to exon-inclusion during alternative splicing. Also functions as export adapter involved in mRNA nuclear export. Binds mRNA which is thought to be transferred to the NXF1-NXT1 heterodimer for export (TAP/NXF1 pathway); enhances NXF1-NXT1 RNA-binding activity. Involved in nuclear export of m6A-containing mRNAs via interaction with YTHDC1: interaction with YTHDC1 facilitates m6A-containing mRNA-binding to both SRSF3 and NXF1, promoting mRNA nuclear export. RNA-binding is semi-sequence specific.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P84103}. Nucleus speckle {ECO:0000250|UniProtKB:P84103}. Cytoplasm {ECO:0000250|UniProtKB:P84103}. Note=Recruited to nuclear speckles following interaction with YTHDC1. {ECO:0000250|UniProtKB:P84103}.
Interaction partners:
- Serine/arginine-rich splicing factor 7
- Nuclear RNA export factor 1
- YTH domain-containing protein 1
- Transformer-2 protein homolog beta
- Serine/arginine-rich splicing factor 2
- Poly
- Serine/arginine-rich splicing factor 1
- Splicing factor U2AF 65 kDa subunit
- SRSF protein kinase 1
- Heterogeneous nuclear ribonucleoproteins C1/C2
Sequence:
MHRDSCPLDCKVYVGNLGNNGNKTELERAFGYYGPLRSVWVARNPPGFAFVEFEDPRDAADAVRELDGRTLCGCRVRVELSNGEKRSRNRGPPPSWGRRPRDDYRRRSPPPRRRSPRRRSFSRSRSRSLSRDRRRERSLSRERNHKPSRSFSRSRSRSRSNERK
Protein: CLK4-associating serine/arginine rich protein (Splicing factor, arginine/serine-rich 16) (Suppressor of white-apricot homolog 2) (Q8N2M8)
Organism: Homo sapiens (Human)
Function: Probably functions as an alternative splicing regulator. May regulate the mRNA splicing of genes such as CLK1. May act by regulating members of the CLK kinase family (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Pleckstrin homology-like domain family B member 2
- CAP-Gly domain-containing linker protein 2
- CAP-Gly domain-containing linker protein 1
- CLIP-associating protein 2
- CLIP-associating protein 1
- GRIP and coiled-coil domain-containing protein 2
- ELKS/Rab6-interacting/CAST family member 1
- Gephyrin
- Liprin-alpha-1
- Liprin-alpha-3
Sequence:
MWHEARKHERKLRGMMVDYKKRAERRREYYEKIKKDPAQFLQVHGRACKVHLDSAVALAAESPVNMMPWQGDTNNMIDRFDVRAHLDHIPDYTPPLLTTISPEQESDERKCNYERYRGLVQNDFAGISEEQCLYQIYIDELYGGLQRPSEDEKKKLAEKKASIGYTYEDSTVAEVEKAAEKPEEEESAAEEESNSDEDEVIPDIDVEVDVDELNQEQVADLNKQATTYGMADGDFVRMLRKDKEEAEAIKHAKALEEEKAMYSGRRSRRQRREFREKRLRGRKISPPSYARRDSPTYDPYKRSPSESSSESRSRSRSPTPGREEKITFITSFGGSDEEAAAAAAAAAASGVTTGKPPAPPQPGGPAPGRNASARRRSSSSSSSSSASRTSSSRSSSRSSSRSRRGGGYYRSGRHARSRSRSWSRSRSRSRRYSRSRSRGRRHSGGGSRDGHRYSRSPARRGGYGPRRRSRSRSHSGDRYRRGGRGLRHHSSSRSRSSWSLSPSRSRSLTRSRSHSPSPSQSRSRSRSRSQSPSPSPAREKLTRPAASPAVGEKLKKTEPAAGKETGAAKPKLTPQEKLKLRMQKALNRQFKADKKAAQEKMIQQEHERQEREDELRAMARKIRMKERERREKEREEWERQYSRQSRSPSPRYSREYSSSRRRSRSRSRSPHYRH
Protein: Sperm surface protein Sp17 (Sperm autoantigenic protein 17) (P36425)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Sperm surface zona pellucida binding protein. Helps to bind spermatozoa to the zona pellucida with high affinity. Might function in binding zona pellucida and carbohydrates.
Subcellular location: Membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- Ropporin-1A
- Calcium binding tyrosine phosphorylation regulated
- A-kinase anchoring protein 3
- Ropporin-1-like protein
- Uncharacterized protein
Sequence:
MSIPFSNTHYRIPQGFGNLLEGLTREILREQPDNIPAFAAAYFENLLEKREKTNFDPAEWGAKVDDRFYNNHAFQEHESEKCEAEEKSQSVTEEETPVLTIDSEDDKDKEEMAALKIQAAFRGHLAREDVKKIRTNKAEEETEENN