wanglab/gogpt-training-data huggingface dataset:
Protein: Serine/threonine-protein kinase minibrain (EC 2.7.12.1) (P49657)
Organism: Drosophila melanogaster (Fruit fly)
Function: Role in the specific control of proper proliferation of optic lobe neuronal progeny.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- DDB1- and CUL4-associated factor 7
- Serine/threonine-protein kinase polo
- GH05923p
Sequence:
MYRLEDTNSGGVMDKNKQKLSAYGSSGGSVDAAQGSGSGGGRQRHAPLYGRFVDAEDLPATHRDVMHHHSSPSSSSEVRAMQARIPNHFREPASGPLRKLSVDLIKTYKHINEVYYAKKKRRAQQTQGDDDSSNKKERKLYNDGYDDDNHDYIIKNGEKFLDRYEIDSLIGKGSFGQVVKAYDHEEQCHVAIKIIKNKKPFLNQAQIEVKLLEMMNRADAENKYYIVKLKRHFMWRNHLCLVFELLSYNLYDLLRNTNFRGVSLNLTRKFAQQLCTALLFLSTPELNIIHCDLKPENILLCNPKRSAIKIVDFGSSCQLGQRIYHYIQSRFYRSPEVLLGIQYDLAIDMWSLGCILVEMHTGEPLFSGCNEVDQMNKIVEVLGMPPKYLLDQAHKTRKFFDKIVADGSYVLKKNQNGRKYKPPGSRKLHDILGVETGGPGGRRLDEPGHSVSDYLKFKDLILRMLDFDPKTRVTPYYALQHNFFKRTADEATNTSGAGATANAGAGGSGSSGAGGSSGGGVGGGLGASNSSSGAVSSSSAAAPTAATAAATAAGSSGSGSSVGGGSSAAQQQQAMPLPLPLPLPLPPLAGPGGASDGQCHGLLMHSVAANAMNNFSALSLQSNAHPPPSLANSHHSTNSLGSLNHISPGSTGCHNNNSNSSNNNTRHSRLYGSNMVNMVGHHNSGSSNNHNSISYPHAMECDPPQMPPPPPNGHGRMRVPAIMQLQPNSYAPNSVPYYGNMSSSSVAAAAAAAAAAASHLMMTDSSVISASAAGGGQGGGNPGQNPVTPSAAAFLFPSQPAGTLYGTALGSLSDLPLPMPLPMSVPLQLPPSSSSSVSSGSASVGSGGVGVGVVGQRRHITGPAAQVGISQSVGSGSSGSATGASSSDASSSSPMVGVCVQQNPVVIH
Protein: Candida glabrata strain CBS138 chromosome G complete sequence (Q6FSI9)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Candida glabrata strain CBS138 chromosome A complete sequence
Sequence:
MKGIFICLWILLLRHTLSADTGISNDNNIHIFTNDDPKYEHTGDIGSPTIAWYMVDGPNLKEITYNGNVQLDSYFLLKATEGNTGYQFNYHGGSFEVGGGQGIFNELASGPTIVNMQGDSFNGKGTSNYTAGVREGSTIYMDFTNYYTQDSYIENFQSVTYSATTNATIDKYILINTDVYILGPVLLSPTYYDSPVLHKSNIWLDSPDIADISGSNFQFGGEGNSGLYIKDSAATKDKEIKLSDSFLDSNNTIAFDTPIQSLNWLHTGLFPGRSGILVVHTTKNTYNISFRALGHHYCLTDKNFKITKTDVNHNGTSIEMFQVTYDPTSNVQCPPPYTVTQEYNIIPTNCFVEDIWVISFIGTTSISYIEETMITICKKEDYTTTIDKGNGDFETDLVSHITTKDSNGNPTTIVTTIPLTKPSGEADYTTTIDKGNGDFETDLVSHITTKDSNGNPTTIVTTIPLTKPSGEADYTTTIDKGNGDFETDLVSHITTKDSNGNPTTIVTTIPLTKPSGEADYTTTIDKGNGDFETDLVSHITTKDSNGNPTTIVTTIPLTKPSGEADYTTTIDKGNGDFETDLVSHITTKDSNGKPTTIITTVTLVEEPVYTAVFVSDGHTITAVVSHVTTTNDIGQTVTTTVTVISYDQVGEGVYTSAPAYSQPPVTTTTVSADTTTATVVISYFPSIGVDGVTRTGTTTVSTVSVGGEADYTTTVDRGNGSIETDVISHITTTDSNGNPTTITTTITNAPAPSISKANIGSDYTTTVVSNGHTFTEVVSHSTGTDEHGHTIVSTVTQTVGVQSHGSTVSSAAPASTVSGAESNAPGTAGVGGIVNSQKPQSQNVAGQGSGNEKPTQAAGTAGGSRSGSGSGSGSGSVHQSAGNIVPSGSPSVQSAKGTASPVSGIHGSQTPHSVPSQAQQQGQGQGQGQAPSSRQQAATTVLLSSGSSVDNIGSGFSSTQTASVLQGKGASIRVASSSIVFSMIVVIVFGMI
Protein: Interferon regulatory factor 3 (M0QZB7)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGTPKPRILPWLVSQLDLGQLEGVAWVNKSRTRFRIPWKHGLRQDAQQEDFGIFQAWAEATGAYVPGRDKPDLPTWKRNFRSALNRKEGLRLAEDRSKDPHDPHKIYEFVNSGVGDFSQPDTSPDTNGGGSTSDTQEDILDELLGNMVLAPLPDPGPPSLAVAPEPCPQPLRSPSLDNPTPFPNLGPSENPLKRLLVPGEEWEFEVTAFYRGRQVFQQTISCPEGLRLVGSEVGDRTLPGWPVTLPDPGMSLTDRGVMSYVRHVLSCLGGGLALWRAGQWLWAQRLGHCHTYWAVSEELLPNSGHGPDGEVPKDKEGGVFDLGPFIVGCAHVPQGLGRNGPGRGCLLPGEYCGPAHFQQPPTLPHLRPVQGLPAGLGGGHGFPGPWGELSPRSSWCASNPPVPHHLNQ
Protein: Novel plant SNARE 12 (AtNPSN12) (Q9LNH6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Vesicle trafficking protein that functions in the secretory pathway.
Subcellular location: Membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}.
Interaction partners:
- Syntaxin-73
- Syntaxin-72
- Syntaxin-71
- Vesicle transport v-SNARE 12
- Syntaxin-32
- Syntaxin-112
- Golgi SNAP receptor complex member 1-1
- Syntaxin-61
- Membrin-12
- Syntaxin-132
Sequence:
MASELPMSPHLEQIHGEIRDHFRALANGFQRLDKIKDSSRQSKQLEELAEKMRDCKRLVKEFDRELKDGEARNSPQVNKQLNDEKQSMIKELNSYVALRKTYLNTLGNKKVELFDTGAGVSGEPTAEENVQMASTMSNQELVDAGMKRMDETDQAIERSKQVVHQTLEVGTQTASNLKGQTDQMGRVVNDLDTIQFSLKKASQLVKEIGRQVATDKCIMAFLFLIVCGVIAIIIVKIVNPNNKDIRDIPGLAPPAQSRKLLYFRE
Protein: Phenolphthiocerol/phthiocerol polyketide synthase subunit A (EC 2.3.1.292) ((Phenol)carboxyphthiodiolenone synthase subunit A) (Beta-ketoacyl-acyl-carrier-protein synthase I) (Phthiocerol synthesis polyketide synthase type I PpsA) (Q7TXM0)
Organism: Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Function: Part of the PpsABCDE complex involved in the biosynthesis of the lipid core common to phthiocerols and phenolphthiocerols by successive additions of malonyl-CoA or methylmalonyl-CoA extender units. PpsA can accept as substrate the activated forms of either icosanoyl (C20), docosanoyl (C22) or lignoceroyl (C24) groups from FadD26, or a (4-hydroxyphenyl)-C17 or (4-hydroxyphenyl)-C19 fatty acyl from FadD29 (By similarity). PpsA initiates the biosynthesis and extends its substrate using a malonyl-CoA extender unit. The PpsB and PpsC proteins add the second and third malonyl-CoA extender units. PpsD adds an (R)-methylmalonyl unit and PpsE adds a second (R)-methylmalonyl unit. The incorporation of the methylmalonyl units results in formation of two branched methyl groups in the elongated product (By similarity).
Interaction partners:
Sequence:
MTGSISGEADLRHWLIDYLVTNIGCTPDEVDPDLSLADLGVSSRDAVVLSGELSELLGRTVSPIDFWEHPTINALAAYLAAPEPSPDSDAAVKRGARNSLDEPIAVVGMGCRFPGGISCPEALWDFLCERRSSISQVPPQRWQPFEGGPPEVAAALARTTRWGSFLPDIDAFDAEFFEISPSEADKMDPQQRLLLEVAWEALEHAGIPPGTLRRSATGVFAGACLSEYGAMASADLSQVDGWSNSGGAMSIIANRLSYFLDLRGPSVAVDTACSSSLVAIHLACQSLRTQDCHLAIAAGVNLLLSPAVFRGFDQVGALSPTGQCRAFDATADGFVRGEGAGVVVLKRLTDAQRDGDRVLAVICGSAVTQDGRSNGLMAPNPAAQMAVLRAAYTNAGMQPSEVDYVEAHGTGTLLGDPIEARALGTVLGRGRPEDSPLLIGSVKTNLGHTEAAAGIAGFIKTVLAVQHGQIPPNQHFETANPHIPFTDLRMKVVDTQTEWPATGHPRRAGVSSFGFGGTNAHVVIEQGQEVRPAPGQGLSPAVSTLVVAGKTMQRVSATAGMLADWMEGPGADVALADVAHTLNHHRSRQPKFGTVVARDRTQAIAGLRALAAGQHAPGVVNPAEGSPGPGTVFVYSGRGSQWAGMGRQLLADEPAFAAAVAELEPVFVEQAGFSLHDVLANGEELVGIEQIQLGLIGMQLALTELWCSYGVQPDLVIGHSMGEVAAAVVAGALTPAEGLRVTATRSRLMAPLSGQGGMALLELDAPTTEALIADFPQVTLGIYNSPRQTVIAGPTEQIDELITRVRARDRFASRVNIEVAPHNPAMDALQPAMRSELADLTPRTPTIGIISTTYADLHTQPVFDAEHWATNMRNPVHFQQAIASAGSGADGAYHTFIEISAHPLLTQAIIDTLHSAQPGARYTSLGTLQRDTDDVVTFRTNLNKAHTIHPPHTPHPPEPHPPIPTTPWQHTRHWITTKYPAGSVGSAPRAGTLLGQHTTVATVSASPPSHLWQARLAPDAKPYQGGHRFHQVEVVPASVVLHTILSAATELGYSALSEVRFEQPIFADRPRLIQVVADNRAISLASSPAAGTPSDRWTRHVTAQLSSSPSDSASSLNEHHRANGQPPERAHRDLIPDLAELLAMRGIDGLPFSWTVASWTQHSSNLTVAIDLPEALPEGSTGPLLDAAVHLAALSDVADSRLYVPASIEQISLGDVVTGPRSSVTLNRTAHDDDGITVDVTVAAHGEVPSLSMRSLRYRALDFGLDVGRAQPPASTGPVEAYCDATNFVHTIDWQPQTVPDATHPGAEQVTHPGPVAIIGDDGAALCETLEGAGYQPAVMSDGVSQARYVVYVADSDPAGADETDVDFAVRICTEITGLVRTLAERDADKPAALWILTRGVHESVAPSALRQSFLWGLAGVIAAEHPELWGGLVDLAINDDLGEFGPALAELLAKPSKSILVRRDGVVLAPALAPVRGEPARKSLQCRPDAAYLITGGLGALGLLMADWLADRGAHRLVLTGRTPLPPRRDWQLDTLDTELRRRIDAIRALEMRGVTVEAVAADVGCREDVQALLAARDRDGAAPIRGIIHAAGITNDQLVTSMTGDAVRQVMWPKIGGSQVLHDAFPPGSVDFFYLTASAAGIFGIPGQGSYAAANSYLDALARARRQQGCHTMSLDWVAWRGLGLAADAQLVSEELARMGSRDITPSEAFTAWEFVDGYDVAQAVVVPMPAPAGADGSGANAYLLPARNWSVMAATEVRSELEQGLRRIIAAELRVPEKELDTDRPFAELGLNSLMAMAIRREAEQFVGIELSATMLFNHPTVKSLASYLAKRVAPHDVSQDNQISALSSSAGSVLDSLFDRIESAPPEAERSV
Protein: General receptor for phosphoinositides 1-associated scaffold protein (GRP1-associated scaffold protein) (95 kDa postsynaptic density protein discs-large ZO-1 domain-containing protein) (PSD-95 PDZ domain-containing protein) (Tamalin) (Q8R4T5)
Organism: Rattus norvegicus (Rat)
Function: Plays a role in intracellular trafficking and contributes to the macromolecular organization of group 1 metabotropic glutamate receptors (mGluRs) at synapses.
Subcellular location: Cytoplasm, perinuclear region {ECO:0000269|PubMed:11850456}. Cell membrane {ECO:0000269|PubMed:11850456}; Peripheral membrane protein {ECO:0000269|PubMed:11850456}; Cytoplasmic side {ECO:0000269|PubMed:11850456}. Postsynaptic cell membrane {ECO:0000269|PubMed:11850456}.
Interaction partners:
- Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2
- Cytohesin-2
- Disks large homolog 4
- Amyloid-beta A4 precursor protein-binding family A member 2
- NT-3 growth factor receptor
- Metabotropic glutamate receptor 5
- Neurochondrin
- PEX5-related protein
- Disks large-associated protein 3
Sequence:
MTLRRLRKLQQKEEATAAPDLAGRAPDSEAARAAPTPSGPPAAAAPPGAPGDELYAALEDYHPAELYRALAVSGGTLPRRKGSGFRWKNFTQSPEQQRKVLTLEKGDNQTFGFEIQTYGLHHREEQRVEMVTFVCRVHESSPAQLAGLTPGDTIASVNGLNVEGIRHREIVDIIKASGNVLRLETLYGTSIRKAELEARLQYLKQTLYEKWGEYRSLMVQEQRLVHGLVVKDPSIYDTLESVRSCLYGAGLLPGSLPFGPLLAAPGGARGGSRRAKGDTDDAVYHTCFFGGAEPQALPPPPPPARAPGPGSAETPASVLCPAPRATLSRSASVRCAGPGGGGGGGAPGALWTEAREQALCGAGLRKTKYRSFRRRLLKFIPGLNRSLEEEESQL
Protein: Potassium voltage-gated channel subfamily E member 1 (Delayed rectifier potassium channel subunit IsK) (IKs producing slow voltage-gated potassium channel subunit beta Mink) (Minimal potassium channel) (MinK) (P15383)
Organism: Rattus norvegicus (Rat)
Function: Ancillary protein that assembles as a beta subunit with a voltage-gated potassium channel complex of pore-forming alpha subunits. Modulates the gating kinetics and enhances stability of the channel complex. Assembled with KCNB1 modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1. Assembled with KCNQ1/KVLQT1 is proposed to form the slowly activating delayed rectifier cardiac potassium (IKs) channel. The outward current reaches its steady state only after 50 seconds. Assembled with KCNH2/HERG may modulate the rapidly activating component of the delayed rectifying potassium current in heart (IKr) (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:14679187, ECO:0000269|PubMed:19219384}; Single-pass type I membrane protein {ECO:0000305}. Apical cell membrane {ECO:0000269|PubMed:19219384}. Membrane raft {ECO:0000250|UniProtKB:P15382}. Note=Colocalizes with KCNB1 at the plasma membrane. Restrictively localized in the apical membrane portion of epithelial cells. Targets to the membrane raft when associated with KCNQ1 (By similarity). {ECO:0000250|UniProtKB:P15382, ECO:0000269|PubMed:19219384}.
Interaction partners:
- Potassium voltage-gated channel subfamily KQT member 1
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit alpha
- Potassium voltage-gated channel subfamily E member 3
- Potassium voltage-gated channel subfamily E regulatory subunit 4
- Potassium voltage-gated channel subfamily E regulatory subunit 5
- Voltage-gated inwardly rectifying potassium channel KCNH2
- Sodium channel protein type 5 subunit alpha
- A-type voltage-gated potassium channel KCND3
- Potassium voltage-gated channel subfamily KQT member 4
Sequence:
MALSNSTTVLPFLASLWQETDEPGGNMSADLARRSQLRDDSKLEALYILMVLGFFGFFTLGIMLSYIRSKKLEHSHDPFNVYIESDAWQEKGKALFQARVLESFRACYVIENQAAVEQPATHLPELKPLS
Protein: [histone H3]-trimethyl-L-lysine(4) demethylase (EC 1.14.11.67) (V9GW19)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MELGSDDFLPPPECPVFEPSWAEFRDPLGYIAKIRPIAEKSGICKIRPPADWQPPFAVEVDNFRFTPRIQRLNELEAQTRVKLNYLDQIAKFWEIQGSSLKIPNVERRILDLYSLSKIVVEEGGYETICKDRRWARVAQRLNYPPGKNIGSLLRSHYERIVYPYEMYQSGANLVQCNTRPFDNEEKDKEYKPHSIPLRQSVQPSKFNSYGRRAKRLQPDPEPTEEDIEKNPELKKLQIYGAGPKMMGLGLMAKDKNLRKKDKEGPECPPTVVVKEELGGDVKMESASPKTFLEGKEELSHSPEPCTKMTMRLRRNHSNAQFIESYVCRMCSRGDEDDKLLLCDGCDDNYHIFCLLPPLPEIPKGVWRCPKCVMAECKRPPEAFGFEQATREYTLQSFGEMADSFKADYFNMPVHMVPTELVEKEFWRLVNSIEEDVTVEYGADIHSKEFGSGFPVSDSKRHLTPEEEEYATSGWNLNVMPVLEQSVLCHINADISGMKVPWLYVGMVFSAFCWHIEDHWSYSINYLHWGEPKTWYGVPSLAAEHLEEVMKKLTPELFDSQPDLLHQLVTLMNPNTLMSHGVPVVRTNQCAGEFVITFPRAYHSGFNQGYNFAEAVNFCTADWLPAGRQCIEHYRRLRRYCVFSHEELICKMAACPEKLDLNLAAAVHKEMFIMVQEERRLRKALLEKGITEAEREAFELLPDDERQCIKCKTTCFLSALACYDCPDGLVCLSHINDLCKCSSSRQYLRYRYTLDELPAMLHKLKVRAESFDTWANKVRVALEVEDGRKRSLEELRALESEARERRFPNSELLQRLKNCLSEAEACVSRALGLVSGQEAGPDRVAGVQMTLAELQDFLGQMNNLPCAMHQIGDVKGILEQVEAYQTEAREALVSQPSSPGLLQSLLERGQQLGVEVPEAQQLQRQVEQARWLDEVKRTLAPSARRGTLAIMRGLLVAGASVAPSPAVDKAQAELQELLTIAERWEEKAHLCLEARQKHPPATLEAIIHEAENIPVHLPNIQSLKEALAKARAWIADVDEIQNGDHYPCLDDLEGLVAVGRDLPVGLEELRQLELQVLTAHSWREKASKTFLKKNSCYTLLEVLCPCADAGSDSTKRSRWMEKELGLYKSDTELLGLSAQDLRDPGSVIVAFKEGEQKEKEGILQLRRTNSAKPSPLASLTTNSSTASICVCGQVPAGVGALQCDLCQDWFHGRCVTVPRLLSSQRSSLTSSPLLAWWEWDTKFLCPLCMRSRRPRLETILALLVALQRLPVRLPEGEALQCLTERAISWQGRARQVLASEEVTALLGRLAELRQRLQAESKPEESLAYSSDGGDGTGNMPKVQGLLENGDSVTSPEKVATEEGSDLELLSSLLPQLTGPVLELPEATRAPLEELMMEGDLLEVTLDENHSIWQLLQAGQPPDLKRVQTLLELEKAERHGSRTRGRALERRRRRKVDRGGEPDDPAREELEPKRVRSSGPEAEEVQEEEELEEETGGEVPPVPFPNNGSPSTQEDQDGLEPVLDAGSDTSAPFSTLTSRLLMSCPQQPSLQQL
Protein: Chromogranin-A (CgA) [Cleaved into: Pancreastatin; Beta-granin; WE-14; Catestatin; GE-25; Serpinin-RRG; Serpinin (AL26); p-Glu serpinin precursor] (P26339)
Organism: Mus musculus (Mouse)
Function: Strongly inhibits glucose induced insulin release from the pancreas.
Subcellular location: Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:12388744}. Cytoplasmic vesicle, secretory vesicle, neuronal dense core vesicle {ECO:0000250|UniProtKB:P10354}. Secreted {ECO:0000269|PubMed:12388744}. Note=Associated with the secretory granule membrane through direct interaction to SCG3 that in turn binds to cholesterol-enriched lipid rafts in intragranular conditions.; SUBCELLULAR LOCATION: [Serpinin]: Secreted {ECO:0000269|PubMed:21436258, ECO:0000269|PubMed:21537909}. Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:21537909}. Note=Pyroglutaminated serpinin localizes to secretory vesicle. {ECO:0000269|PubMed:21537909}.
Interaction partners:
- Secretogranin-1
- Secretogranin-3
- Secretogranin-2
- Synaptophysin
- Gamma-enolase
- Somatostatin
- Leucine-rich repeat-containing G-protein coupled receptor 5
- Carboxypeptidase E
- Pro-glucagon
- Gastrin
Sequence:
MRSTAVLALLLCAGQVFALPVNSPMTKGDTKVMKCVLEVISDSLSKPSPMPVSPECLETLQGDERILSILRHQNLLKELQDLALQGAKERAQQPLKQQQPPKQQQQQQQQQQQEQQHSSFEDELSEVFENQSPDAKHRDAAAEVPSRDTMEKRKDSDKGQQDGFEATTEGPRPQAFPEPNQESPMMGDSESPGEDTATNTQSPTSLPSQEHVDPQATGDSERGLSAQQQARKAKQEEKEEEEEEEAVAREKAGPEEVPTAASSSHFHAGYKAIQKDDGQSDSQAVDGDGKTEASEALPSEGKGELEHSQQEEDGEEAMVGTPQGLFPQGGKGRELEHKQEEEEEEEERLSREWEDKRWSRMDQLAKELTAEKRLEGEDDPDRSMKLSFRTRAYGFRDPGPQLRRGWRPSSREDSVEARSDFEEKKEEEGSANRRAEDQELESLSAIEAELEKVAHQLQALRRG
Protein: Cardiac myosin light chain-1 (Cmlc1 protein) (Q5XJC3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MAPKKVEPKKPEPKKPEAKKEEAPAPAPVPETPKEPEVDLKSVPLDFSPDQIEEFRDAFTLFDETPTGEMKIRYAQCGDVMRALGHNPTNADVLTVLGKPKAEEMNTKYLDFETFLPMLQHVSRAKDQGTFEDFVEGLRVFDKEGNGTVMGAELRHVLATLGEKMTEDEADRLMAGQEDANGCINYTSFIKHILSG
Protein: Mediator of RNA polymerase II transcription subunit 14 (Cofactor required for Sp1 transcriptional activation subunit 2) (CRSP complex subunit 2) (Mediator complex subunit 14) (Thyroid hormone receptor-associated protein complex 170 kDa component) (Trap170) (A2ABV5)
Organism: Mus musculus (Mouse)
Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 16
- Mediator of RNA polymerase II transcription subunit 20
- Mediator of RNA polymerase II transcription subunit 10
- Mediator of RNA polymerase II transcription subunit 18
- Mediator of RNA polymerase II transcription subunit 19
- Mediator of RNA polymerase II transcription subunit 27
- Mediator of RNA polymerase II transcription subunit 31
- Mediator of RNA polymerase II transcription subunit 21
- Mediator of RNA polymerase II transcription subunit 22
- Mediator of RNA polymerase II transcription subunit 24
Sequence:
MAPVQLDNHQLIPPGGGGGSSGGGGSSSGSASAPAPPPPAAAVAAAAAAAASPGYRLSTLIEFLLHRAYSELMVLTDLLPRKSDVERKIEIVQFASRTRQLFVRLLALVKWANDAGKVEKCAMISSFLDQQAILFVDTADRLASLARDALVHARLPSFAIPYAIDVLTTGSYPRLPTCIRDKIIPPDPITKIEKQATLHQLNQILRHRLVTTDLPPQLANLTVANGRVKFRVEGEFEATLTVMGDDPEVPWRLLKLEILVEDKETGDGRALVHSMQIDFIHQLVQSRLFADEKPLQDMYNCLHCFCLSLQLEVLHSQTLMLIRERWGDLVQVERYHAGKSLSLSVWNQQVLGRKTGTASVHKVTIKIDENDVSKPLQIFHDPPLPASDSKLVERAMKIDHLSIEKLLIDSVHARAHQRLQELKAILRSFNANESSSIETALPALIVPILEPCGNSECLHIFVDLHSGMFQLMLYGLDPATLEDMEKSLNDDMKRIIPWIQQLKFWLGQQRCKQSIKHLPTITTETLQLANYSTHPIGSLSKNKLFIKLTRLPQYYIVVEMLEVPNKPTQLSYNYYFMSVSTADREDSPVMALLLQQFKDNIQDLMSYTKTGKQTRTGTKHKLSDDPCPIDSKKAKRSGEMCAFNKVLAHFVAMCDTNMPFVGLRLELSNLEIPHQGVQVEGDGFNHAIRLLKIPPCKGISEETQKALDRSLLDCTFRLQGRNNRTWVAELVFANCPLNGTSTREQGPSRHVYLTYENLLSEPVGGRKVVEMFLNDWSSIARLYECVLEFARSLPEIPAHLNIFSEVRVYNYRKLILCYGTTKGSSISIQWNSIHQKFHIALGTVGPNSGCSNCHNTILHQLQEMFNKTPNVVQLLQVLFDTQAPLNAINKLPTVPMLGLTQRTNTAYQCFSILPQSSTHIRLAFRNMYCIDIYCRSRGVVAIRDGAYSLFDNSKLVEGFYPAPGLKTFLNMFVDSNQDARRRSVNEDDNPPSPIGGDMMDSLISQLQPPQQQPFPKQPGTSGAYPLTSPPTSYHSTVNQSPSMMHTQSPGNLHAASSPSGALRAPSPASFVPTPPPSSHGISIGPGASFASPHGTLDPSSPYTMVSPSGRAGNWPGSPQVSGPSPATRLPGMSPANPSLHSPVPDVSHSPRAGTSSQTMPTNMPPPRKLPQRSWAASIPTILTHSALNILLLPSPTPGLVPGLAGSYLCSPLERFLGSVIMRRHLQRIIQQETLQLINSNEPGVIMFKTDALKCRVALSPKTNQTLQLKVTPENAGQWKPDELQVLEKFFETRVAGPPFKANTLIAFTKLLGAPTHILRDCVHIMKLELFPDQATQLKWNVQFCLTIPPSAPPIAPPGTPAVVLKSKMLFFLQLTQKTSVPPQEPVSIIVPIIYDMASGTTQQADIPRQQNSSVAAPMMVSNILKRFAEMNPPRQGECTIFAAVRDLMANLTLPPGGRP
Protein: Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase (EC 2.4.1.143) (Beta-1,2-N-acetylglucosaminyltransferase II) (GlcNAc-T II) (Mannoside acetylglucosaminyltransferase 2) (N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase II) (Q711U4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004323}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004323}.
Interaction partners:
Sequence:
MGRKRNNFYMRSLFLLALGIFGLLQYNNFNYLDSRDNVLGDAVTNDSDDAILAMVPATLHKYLTPHSRNHSASGAGVLNGAALLLNASSPGAATASTISFDVYHPPNITEIKRQIVRYNDMQMVLNEDVFGPLQNDSVIIVVQVHTRITYLRHLIVSLAQARDISKVLLVFSHDYYDDDINDLVQQIDFCKVMQIFYPYSIQTHPNEYPGVDPNDCPRNIKKEQALITNCNNAMYPDLYGHYREAKFTQTKHHWIWKANRVFNELEVTRYHTGLVLFLEEDHYVAEDFLYLLAMMQQRTKDLCPQCNVLSLGTYLKTFNYYTYHSKTNKKSYASSLISTNSLLGYNRNNNRNSVQLAVSSSYSSSSSAQSPPPSKVYVGDTSDNQRASDSSSRRGNLINTVTATATATAATSDTSNNEQSSHSSSKNGAQTWNYHVLPSLYSVYQKVEVMPWVSSKHNMGFAFNRTTWSNIRKCARHFCTYDDYNWDWSLQHVSQQCLRRKLHAMIVKGPRVFHIGECGVHHKNKNCESNQVISKVQHVLRIARNSHQLFPRSLTLTVPSLMKKSKLRKGNGGWGDMRDHELCLNMTLATR
Protein: RAN GTPase-activating protein 1 (AtRanGAP1) (RanGAP1) (Q9LE82)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: GTPase activator for the nuclear Ras-related regulatory protein Ran, converting it to the putatively inactive GDP-bound state. Plays a role in spatial signaling during cell division.
Subcellular location: Cytoplasm. Nucleus envelope {ECO:0000269|PubMed:22270916}. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, phragmoplast. Note=Localized in patchy areas at the nuclear envelope (NE) of interphase cells. Concentrates at the preprophase band (PPB) and remains associated with the cortical division site (CDS) during mitosis and cytokinesis. During mitosis, associates with mitotic spindles at the anaphase. Associated to the microtubular phragmoplast and the surface of the daughter nuclei at the telophase.
Interaction partners:
- SUMO-conjugating enzyme SCE1
- Ran-binding protein 1 homolog c
- SUMO-conjugating enzyme UBC9
- Ran-binding protein 1 homolog a
- Ran-binding protein 1 homolog b
- Small ubiquitin-related modifier 1
- WPP domain-interacting tail-anchored protein 1
- Small ubiquitin-related modifier 2
- Nuclear pore complex protein NUP35
- Nuclear pore complex protein NUP205
Sequence:
MDHSAKTTQNRVLSVKMWPPSKSTRLMLVERMTKNITTPSIFSRKYGLLSVEEAEQDAKRIEDLAFATANKHFQNEPDGDGTSAVHVYAKESSKLMLDVIKRGPQEESEVEVSKDGDVFFDISGGSRAFIEEEEARDLLRPLADPRNSYTKIRFSNRSFGSEAAKFAASVLSSIKDQLTEVDLSDFVAGRPEAEALEVMNMFSSALEGSKLRYLNLSDNALGEKGIRAFASLINSQHDLEELYLMNDGISEDAARAVRELLPSTDKIRVLQFHNNMTGDEGATAIAEIVRECPSLEDFRCSSTRIGSEGGVALAEALEHCSHLKKLDLRDNMFGVEGGIALAKTLSVLTHLTEIYMSYLNLEDEGTEALSEALLKSAPSLEVLELAGNDITVKSTGNLAACIASKQSLAKLNLSENELKDEGTILIAKAVEGHDQLVEVDLSTNMIRRAGARALAQTVVKKNTFKLLNINGNFISEEGIDEVNDMFKDCLDKLVPLDDNDPEGEDFEDEDEEEEGEDGNELESKLGSLKIKQGEE
Protein: Phenoloxidase-activating factor 3 (EC 3.4.21.-) (Prophenoloxidase-activating factor III) (Serine protease-like protein PPAF-3) [Cleaved into: Phenoloxidase-activating factor 3 light chain; Phenoloxidase-activating factor 3 heavy chain] (Q8I6K0)
Organism: Holotrichia diomphalia (Korean black chafer)
Function: Serine endopeptidase which, by cleaving prophenoloxidase activating factor PPAF2, is required for the activation of the prophenoloxidase cascade probably following the recognition of pathogen-derived products.
Subcellular location: Secreted {ECO:0000269|PubMed:12185078}. Note=Secreted in the hemolymph. {ECO:0000269|PubMed:12185078}.
Interaction partners:
Sequence:
MWLSLVILGVASAIVNVSTQESCTTPNGETATCLPIESCKIFWDYVVTSGADPEINSFLRASLCRQGNYVVCCGSTLKFNSALPDRTECGLQDDFKVLGGEDTDLGEYPWMALLQQTKTSGAKSFGCGGSLISDRYVLTAAHCVVSSSYTVTMVRLGEWDLRATQDCVGSGSYQYCSPPPQDIGIESITSHPNYEKSSRGVFNDIALIRLARPVNRNKYVQPICLPLPTERTPVGENLLVAGWGATETKAQSDKKQKLKLPVTDLPACKTLYAKHNKIINDKMICAGGLKGKDSCKGDSGGPLFGQTGAGNAQFYIEGIVSYGAICGTEGFPAIYTRVSDHLDWIKQNVRV
Protein: Dual specificity protein phosphatase MPK-4 (EC 3.1.3.16) (EC 3.1.3.48) (Q9VWF4)
Organism: Drosophila melanogaster (Fruit fly)
Function: Dual specificity phosphatase; can dephosphorylate both phosphotyrosine and phosphoserine or phosphothreonine residues. May suppress bsk/JNK activation during the immune response.
Subcellular location: Nucleus {ECO:0000269|PubMed:18456458}. Cytoplasm {ECO:0000269|PubMed:18456458}. Note=Mainly found in the nucleus. {ECO:0000269|PubMed:18456458}.
Interaction partners:
Sequence:
MEQSQSQRQAWPSSSAGGGKAQDSGVLTREDFDGGPVSIDEVDTGLFLGNLTAATHMETLRSFKITHILTLDSVPLPQHILEASFLTTKYIQIADMPREDILQHLEGCVDFISSALAQQGNVLVHCYFGVSRSSSTVIAYMMKRHNLDFLPAYELVKAKRRFVQPNAGFVSQLKLFRRMGCKIDPNCQRYKIHRLRLAGEQMRKAKILPQSFHSVVRPDPDITRENPEPIVFRCRRCRRVLASKSHVLEHKPRDRPPQEVVPKEKEEVAAAKLPAQSHDQAENHHGARMLEQLSERIRQSSLGSPGHESTPNYCRSILFVEPIAWMHRIMLNTQGRLYCPKCEQKLGNFSWINACKCPCGETMTPAFYLIPSKVELSKAVQNVQTTV
Protein: Triglyceride lipase (F4JT30)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MTSLQLHFSVHFLRPKHRLRYSPIFNTRTFNFPGKITFRLRAKPNSLRCFAQSETKEENIGKREVNAAGCNTLYLSESFVREIYDGQLFIKLKRGFEFPALDPWGTSDPYVVMDLDGQVAKSKTKWGTKEPKWNEDFVFNIKLPPAKKIEIAAWDANLVTPHKRMGNSEINLESVCDGNLHKVLVELDGIGGGGKVQLEIKYKGFGEVEEEKKWWRFPFVSEFLQRNEIKSVLKNFVDSEAVESVLKNLVDSEAVPARQFVEYAFGQLKSLNDAPLKNTELLNNTAEDSEGASSEDSSDQHRSTNLSSSGKLSKDKDGDGDGHGNELEDDNESGSIQSESNFWDNIPDIVGQNIVQKLGLPSPEKLKWNGTELLENFGLQSRKTAEAGYIESGLATADTREADDEKEDGQVAINASKSSLADMKNATQELLKQADNVFGALMVLKAVVPHLSKDSVGSEKVIEKNGSSSVTDDVSGSSKTEKISGLVNVDGADEKNAEEMKTLFSSAESAMEAWAMLATALGHPSFIKSEFEKLCFLENDITDTQVAIWRDARRKRVVIAFRGTEQTKWKDLQTDLMLVPAGLNPERIGGDFKQEVQVHSGFLSAYDSVRIRIISLLKMTIGYIDDVTEREDKWHVYVTGHSLGGALATLLALELSSSQLAKRGAITVTMYNFGSPRVGNKQFAEIYNQKVKDSWRVVNHRDIIPTVPRLMGYCHVAHPVYLSAGDVEDIEFQKDGYHAEVIGEATPDILVSRFMKGEKELVEKILQTEIKIFNALRDGSALMQHMEDFYYITLLESVKLYYKTVEDPKGVESTTIQSVGES
Protein: Methylthioribulose-1-phosphate dehydratase (MTRu-1-P dehydratase) (EC 4.2.1.109) (Q9HE08)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03116, ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Enolase-phosphatase E1
- Acireductone dioxygenase-requiring))
- Methylthioribose-1-phosphate isomerase
- Adenosylhomocysteinase
- Pdp3-interacting factor 1
- Xylulose kinase
Sequence:
MDDFLKKDLGCLRSGDLKKCGELICEICRDLYTSGWVTGTGGGITIRSGDAIVIAPSGVQKERMELHHLFVMSLITREYMRMPALRLKPSQCTPLFLAVYTLRDAYACIHTHSQEAILLSTLFADSDHFSATGFEVLSYIPKGSKNNGFHKPTDKIKIPFINNTAHESDLHDSLQEAINLYPDTCAVIVRDHGIYCWGDTWQDTKMNTEAVEFLFQAYLRRRRLQKPE