wanglab/gogpt-training-data huggingface dataset:
Protein: Copper-transporting ATPase (EC 7.2.2.9) (Q59467)
Organism: Helicobacter pylori (Campylobacter pylori)
Function: Probably involved in copper export.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
Sequence:
MKESFYIEGMTCTACSSGIERSLGRKSFVKKIEVSLLNKSANIEFNENETNLDEIFKLIEKLGYSPKKTLAEEKKEFFSPNVKLALAVIFTLFVVYLSMGAMLSPSLLPESLLTINNHSNFLNACLQLIGTLIVMHLGRDFYIQGFKALWHRQPNMSSLIAIGTSAALISSLWQLYFVYTSQWSYGHYYFESVCVILMFVMVGKRIENVSKDKALDAMQALMKNAPKTALKMHNNQQIEVLVDSIVVGDILKVLPGSAIAVDGEIIEGEGELDESMLSGEALPVYKKVGDKVFSGTFNSHTSFLMKATQDNKNSTLSQIVEMIHNAQSSKAEISRLADKVSSVFVPSVIAIAILAFVVWLIIAPKPDFWWNFGIALEVFVSVLVISCPCALGLATPMSILVANQKASSLGLFFKDAKSLEKARLVNTIVFDKTGTLTNGKPVVKSVHSNIELLELLSLAGSIEKSSEHVIAKGIVEYAKEHNAPLKEMSEVKVKTGFGISAKTDYQGAKEVIKVGNSEFFNPINALEIQENGILVFVGRVISEKEDELLGAFVLEDLPKKGVKEHIAQIKKLGINTFLLSGDNRENVKKCALELGIDGYISNAKPQDKLNKIKELKEKGQIVMMVGDGLNDAPSLAMSDVAVVMAKGSDVSVQAADIVSFNNDIKSVYSAIKLSQATIKNIKENLFWAFCYNSVFIPLACGVLYKANIMLSPAIAGLAMSLSSVSVVLNSQRLRNFKIKDH
Protein: Candida glabrata strain CBS138 chromosome C complete sequence (Q6FWR0)
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 D complete sequence
- Candida glabrata strain CBS138 chromosome J complete sequence
- Candida glabrata strain CBS138 chromosome G complete sequence
- Candida glabrata strain CBS138 chromosome D complete sequence
- Candida glabrata strain CBS138 chromosome L complete sequence
- Candida glabrata strain CBS138 chromosome E complete sequence
- Histone-lysine N-methyltransferase, H3 lysine-4 specific
- Histone deacetylase
- Candida glabrata strain CBS138 chromosome K complete sequence
- Nucleoporin NSP1
Sequence:
MAKEKDVIGGHAAKLEELLGAVRREFEAVSQEVSSYQQQNQKNYDFKINQQLAEMQQIRNTVYELELTHRKMKDVYEEEIGRLKAEIEKRDQQLSEFGAHSAAPPQPALPAPQITAEGTHLQDSKAGLTPLVSVLSSQNQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAVHAAQVAQQTPAAQYQMTLPPMQQPQQYQQGYQLNSMSPQQAKTEPVDKKPETQVATTTATAEKQETAYNQWANQAKPIPPFLLDLDAENTSAEFKKQTEDYYVLYNPTQPKDIDIELHRTLLHDSVVCCVKFSNNGEYLATGCNKTTKIFEVATGNLVTELVDDTKTGTEDANSASSADLYIRSVCFSPDGKFLATGAEDKLIRIWDIAQRKIVMVLRGHEQDIYSLDYFQSGNKLVSGSGDRTIRIWDLHTGQCSLTLSIEDGVTTVAVSPGNGNYVAAGSLDRTVRVWDSNSGFLVERLDSEGETGVGHKDSVYSVVFTRDGKNIVSGSLDRSVKLWNLRNINGASTSPQPKTEGNCEMTYIGHKDFVLSVTTTENDQYILSGSKDRGVIFWDKVSGVPLLMLQGHRNSVISVAVANGKPLGANYNVFATGSGDCKAKIWKFQTIRK
Protein: Betaine--homocysteine S-methyltransferase 1 (EC 2.1.1.5) (Q95332)
Organism: Sus scrofa (Pig)
Function: Involved in the regulation of homocysteine metabolism. Converts betaine and homocysteine to dimethylglycine and methionine, respectively. This reaction is also required for the irreversible oxidation of choline.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:O09171}. Nucleus {ECO:0000250|UniProtKB:O09171}. Note=Predominantly localized in the cytoplasm with a small fraction detected in the nucleus. Translocates into the nucleus upon oxidative stress. {ECO:0000250|UniProtKB:O09171}.
Interaction partners:
- Cystathionine gamma-lyase
- Dimethylglycine dehydrogenase, mitochondrial
- Adenosylhomocysteinase like 1
- S-adenosylmethionine synthase
- Adenosylhomocysteinase like 2
- Adenosylhomocysteinase
- Methylenetetrahydrofolate reductase
- Cystathionine beta-synthase
- Methionine adenosyltransferase 2 subunit beta
- Methionine synthase
Sequence:
MAPVGDKKAKKGILERLNSGEVVIGDGGFVFALEKRGYVKAGPWTPEAAVEHPEAVRQLHREFLRAGSNVMQTFTFYASEDKLENRGNYVAEKISGQKVNEAACDIARQVADEGDALVAGGVSQTPSYLSCKSETEVKKVFRQQLEVFMKKNVDFLIAEYFEHVEEAVWAVEALKASGKPVAATMCIGPEGDLHGVTPGQCAVRLVKAGASIVGVNCHFDPTISLQTVKLMKEGLQAAGLKAHLMSQPLAYHTPDCGKQGFIDLPEFPFGLEPRVATR
Protein: Septin (A0JMF4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Chromosome, centromere, kinetochore {ECO:0000256|ARBA:ARBA00004629}. Cleavage furrow {ECO:0000256|ARBA:ARBA00004626}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000256|ARBA:ARBA00004430}. Cytoplasm, cytoskeleton, spindle {ECO:0000256|ARBA:ARBA00004186}. Midbody {ECO:0000256|ARBA:ARBA00004214}.
Interaction partners:
- Septin 2
- Uncharacterized protein LOC393431
- Septin 6
- Septin-8-B
- Septin-8-A
- Septin 9a
- Sept9b protein
- Neuronal-specific septin-3
- Septin 12
- Septin-type G domain-containing protein.
Sequence:
MIERPDSAVSSVAQRNLEGYVGFANLPNQVYRKSVKRGFEFTLMVVGESGLGKSTLINSLFLTDLYSKDYPGPSQRIKKTVQVEQSKVLIKEGGVQLTLTIVDTPGFGDAVDNSNCWQPVINYIDSKFEDFLNAESRVNRRQMPDNRVHCCLYFIAPSGHGLKPLDIEFMKRLHDKVNVIPLIAKADTLTPEECQLFKKQIMKEIQEHKIKIYEFPDTEDDEDSKLIRKIKEKMPLAVVGSNVVIEVNGRKVRGRQYPWGVAEVENGEHCDFTVLRNMLIRTHMQDLKDVTNNVHYENYRSKKLAAVTCNGVDATKNKGQLTKSPLAQMEEERREHVMKMKKMETEMEQVFEMKVKEKKQKLKDSEAELERRHEQMKKNLEAQYKELEEKRRQFEDEKANWEAQQRILEQQKLDASKTMEKNKKKGKIF
Protein: EP3-2 procyclin (Q581F6)
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:
MAPRSLYLLAILLFSANLFSGVGFAAAAEGPEDKGLTKGGKGGKGTKVSDDDTNGTDPDPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPEPGAATLKSVALPFAIAAVGLVAAF
Protein: Coagulation factor IX (EC 3.4.21.22) (Christmas factor) [Cleaved into: Coagulation factor IXa light chain; Coagulation factor IXa heavy chain] (P00741)
Organism: Bos taurus (Bovine)
Function: Factor IX is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active form in the presence of Ca(2+) ions, phospholipids, and factor VIIIa.
Subcellular location: Secreted {ECO:0000269|PubMed:12695512}.
Interaction partners:
- Coagulation factor XI
- Coagulation factor X
- Tissue factor
- Coagulation factor VIII
- Prothrombin
- Thyroxine-binding globulin
- Vitamin K-dependent gamma-carboxylase
- Coagulation factor VII
- Furin
- Coagulation factor XII
Sequence:
MWCLNMIMAESPGLVTICLLGYLLSAECTVFLDRENATKILHRPKRYNSGKLEEFVRGNLERECKEEKCSFEEAREVFENTEKTTEFWKQYVDGDQCESNPCLNGGMCKDDINSYECWCQAGFEGTNCELDATCSIKNGRCKQFCKRDTDNKVVCSCTDGYRLAEDQKSCEPAVPFPCGRVSVSHISKKLTRAETIFSNTNYENSSEAEIIWDNVTQSNQSFDEFSRVVGGEDAERGQFPWQVLLHGEIAAFCGGSIVNEKWVVTAAHCIKPGVKITVVAGEHNTEKPEPTEQKRNVIRAIPYHSYNASINKYSHDIALLELDEPLELNSYVTPICIADRDYTNIFLKFGYGYVSGWGKVFNRGRSASILQYLKVPLVDRATCLRSTKFSIYSHMFCAGYHEGGKDSCQGDSGGPHVTEVEGTSFLTGIISWGEECAMKGKYGIYTKVSRYVNWIKEKTKLT
Protein: Vacuolar protein sorting-associated protein 28 homolog (Q6PH25)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Endosome {ECO:0000256|ARBA:ARBA00004177}.
Interaction partners:
- Tumor susceptibility 101a.
- Vacuolar protein-sorting-associated protein 25
- Vacuolar protein-sorting-associated protein 36
- Vacuolar protein sorting 37A.
- Multivesicular body subunit 12A
- VPS37B subunit of ESCRT-I
- VPS37C subunit of ESCRT-I
- Zgc:114173.
- Charged multivesicular body protein 3
- Ubiquitin-conjugating enzyme E2 variant 3
Sequence:
MFHGIPASGVMGGAPANKPELYEEVKLYKNAREREKYDNMAELFAVVKTLQALEKAYIKDCVTPNEYTGACSRLLVQYKAAFKQVQGSDVGSIDDFCRKYRLDCPLAMERIKEDRPITIKDDKGNLNRCIADIVSLFITVMDKLRLEIRAMDEIQPDLRELMETMNRMSNMPPDSEAKDKVSLWLTTLSSMSASDELDDSQVRQMLFDLESAYNAFNRFLHSS
Protein: Delta-6 fatty acid desaturase (A7UFH0)
Organism: Ceratodon purpureus (Fire moss) (Dicranum purpureum)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
TLGQWSLSTTFAFKRLTTKKHSSDISVEAQKESVARGPVENISQSVAQPIRRRWVQDKKPVTYSLKDVASHDMPQDCWIIIKEKVYDVSTFAEQHPGGTVINTYFGRDATDVFSTFHASTSWKILQNFYIGNLVREEPTLELLKEYRELRALFLREQLFKSSKSYYLFKTLINVSIVATSIAIISLYKSYRAVLLSA
Protein: Probable inactive linolenate hydroperoxide lyase (Cytochrome P450 74B2) (Hydroperoxide lyase 1) (B3LF83)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Lipoxygenase 2, chloroplastic
- Lipoxygenase 4, chloroplastic
- Lipoxygenase 6, chloroplastic
- Lipoxygenase 3, chloroplastic
- Alcohol dehydrogenase class-P
- Allene oxide synthase, chloroplastic
- Allene oxide cyclase 2, chloroplastic
- Alcohol dehydrogenase-like 6
- Allene oxide cyclase 1, chloroplastic
- Alcohol dehydrogenase-like 4
Sequence:
MDLVDKRDVLIGDFRPSLGFYGGVRVGVYLDTTEPKHAKIKGFAMETLKRSSKVWLQELRSNLNIFWGTIESEISKNGAASYIFPLQRCIFSFLCASLAGVDASVSPDIAENGWKTINTWLALQVIPTAKLGVVPQPLEEILLHTWPYPSLLIAGNYKKLYNFIDENAGDCLRLGQEEFGLTRDEAIQNLLFVLGFNAYGGFSVFLPSLIGRITGDNSGLQERIRTEVRRVCGSGSDLNFKTVNEMELVKSVVYETLRFSPPVPLQFARARKDFQISSHDAVFEVKKGELLCGYQPLVMRDANVFDEPEEFKPDRYVGETGSELLNYLYWSNGPQTGTPSASNKQCAAKDIVTLTASLLVADLFLRYDTITGDSGSIKAVVKAK
Protein: Tachykinin-related peptide 4 (TKRP-4) (P86566)
Organism: Banasa dimiata (Banasa stink bug) (Pentatoma dimiata)
Subcellular location: Secreted {ECO:0000269|PubMed:19084564, ECO:0000305}.
Interaction partners:
Sequence:
SPASGFFGMR
Protein: Ubiquitin receptor RAD23 (DNA repair protein RAD23) (F4KCN6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU367049}. Cytoplasm {ECO:0000256|RuleBase:RU367049}.
Interaction partners:
- DNA repair protein RAD4
- Peptide-N
- 26S proteasome non-ATPase regulatory subunit 4 homolog
- Ubiquitin-ribosomal protein eL40z fusion protein
- Ubiquitin-ribosomal protein eL40y fusion protein
- Probable ubiquitin conjugation factor E4
- Protein NBR1 homolog
- Cyclin-dependent kinase D-1
- E3 ubiquitin-protein ligase PRT1
- cyclin-dependent kinase
Sequence:
MKIIVKTLKGIRFEIEVKPNDSVAEVKKNIETVMGASEYPAAQQILIHKREKLRDETTMEANKVFDKSVIAIIITKGCLEEMEKQNPPLFQMIRHNSAGFVPVLNKESFERDNELAQPEEDLLQLQVTAVDDEAINRLEAMGFERRVVLEVFLACNKNEQLAANFLLDHIH
Protein: Photosystem II reaction center protein T (PSII-T) (P74787)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Function: Seems to play a role in the dimerization of PSII.
Subcellular location: Cellular thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_00808, ECO:0000269|PubMed:12069591, ECO:0000269|PubMed:34937700}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00808, ECO:0000269|PubMed:34937700}.
Interaction partners:
- Photosystem II CP47 reaction center protein
- Photosystem II reaction center protein L
- Photosystem II reaction center protein M
- Cytochrome b559 subunit beta
- Photosystem II reaction center protein J
- Photosystem II CP43 reaction center protein
- Photosystem II reaction center protein H
- Photosystem II extrinsic protein V
- Photosystem II reaction center protein I
- Photosystem II reaction center protein K
Sequence:
MESVAYILVLTMALAVLFFAIAFREPPRIEK
Protein: LD15563p (Link) (Q7K275)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- GEO09613p1
- Uncharacterized protein
- GEO04221p1
- Uncharacterized protein, isoform A
- Scavenger receptor class C, type II, isoform A
- Insulin-like peptide 4
- Protein spalt-accessory
- Bearded
- Uncharacterized protein, isoform A
- RE70333p
Sequence:
MIGVLMRFLWSLAMVQCIQARVSMLPRFYGQDSAVIVDINRKFPPRMDSKLQNALYYNLPVYKLIKPTTTTTTTTTAAPTSGYPADLLNIAHNKLGLKDLPNLEELGEMIGTDGASETIDYIRTLTGTEEGLALMKQYLDALHFEEAEEENVAEEQEKAEDDDDDDDDNTMGNASYDEMPQEKSTTTADPRPELSLMQRFGDFVKQYNLWSGQVTTTTTPAPFIARPSGSFQPVFVAPPPAGLKPFRPILVRQPLPYHYPIPLRPVSLATTKPIQVTTTTTTTTTPAPVTKPHLNTPKLIMQEDAEGKYSTLPPYIQQLAKMANISPQVVEIFLERQPKLAELAKRLSTLALSPEQTQAMDTQVLKAVQHALSNNDDLQRLIEASQALK
Protein: DNA polymerase kappa (D6RDX9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDSTKEKCDSYKDDLLLRMGLNDNKAGMEGLDKEKINKIIMEATKGSRFYGNELKKEKQVNQRIENMMQQKAQITSQQLRKAQLQVDRFAMELEQSRNLSNTIVHIDMDAFYAAVEMRDNPELKDKPIAVGSMSMLSTSNY
Protein: Leucine rich repeat protein GP150 (Q95PA9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSRQSTCRLVLLLAFTLALIHASHSNTVGPKIHFIHDDLTENELNSGEEVSPTESLPKISTPKVKDLPVETTTRSPTKKTTSSGTEKSLSEEAWNDLMEAAKHSQALADDPHFNKMLNTTVAAGEKNSTDTDDSEYYDYDDDYHYFDEETVTISPSPKKAKSNPKLQPIVDATITKSKSKSNDQKTKESANDIDSDSQYDYDEGLDDDDDEDDAADDLLTDDEQVVFSEDVPCPRFCQCARNVNSYLVATCSRLDMGIQKFGSDITDLVVTNVGPKYPILMGPNFFQNLGLKNVASIKIANCTLEYLHAEAFHGLNELYAVNLTDVGLAIINPDTFVGNKKLRMLTISGNDLSVMSSIHYLLKSSSIEELDFSRNNLMELNPKAFSHLSNVVYINLSQNSLKKLPEKAFEKVTLLEELDLSYNSLTELPRDIFNGTTLSILHLKYNTSNGDLHFGTKDLQQLDLSFNSIVQVHHSMFDKMPGLTNLNLKGNGIKKIQPDSFLTLKNLRHIDLSINDLDQISGMLFFKNSELDVIRLNDNPRLSQLPTDGFLSYSGEFTVYYLDISNCAIGPLGHKAFSTMPHLTTLKLAWNNINHLPREIFTGLHKLIDLDLSNNLITRMDDLIFMDNGELTKLSLAGNPISRLSVRLFLPLHQLRCLDVNDCELTTLLSDRDLGAGYKIFDSLRSFNASGNLIKKISSEDVKSFKNLRSLDITNNPLKCTPDFQEFISYVTLQMQMTPKRLPVLANLEDDATIVQLETLAQAGWSSLAHEVCKHAEGSDLLDEKKADSAEAKLEKRLKESVKKLNEDEAKLLSVLDKSVLDKSRLSSMQKIMKGSVNTETAKPEEDADEENLNNGGEDKEDDSSDYDSEEDDDDDDEDDDDDNNDDDRFEEAKKNAKAKADANKAFDTFVNKELKPVLKTDGIQAEEVDMSQETRDKFLLEKLGFDSESEESDEYTEKMIFHGELSYDLVVPLIVVSFCLLMIVLSIARVIYVVLRKRGERYRMALLASKNSFVYQKLSEDIVKPTSKEQKEPKHLKQPKVHRYAPINQV
Protein: BAG family molecular chaperone regulator 3 (BAG-3) (Bcl-2-associated athanogene 3) (Bcl-2-binding protein Bis) (Q9JLV1)
Organism: Mus musculus (Mouse)
Function: Co-chaperone for HSP70 and HSC70 chaperone proteins. Acts as a nucleotide-exchange factor (NEF) promoting the release of ADP from the HSP70 and HSC70 proteins thereby triggering client/substrate protein release. Nucleotide release is mediated via its binding to the nucleotide-binding domain (NBD) of HSPA8/HSC70 where as the substrate release is mediated via its binding to the substrate-binding domain (SBD) of HSPA8/HSC70. Has anti-apoptotic activity. Plays a role in the HSF1 nucleocytoplasmic transport.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O95817}. Cytoplasm {ECO:0000250|UniProtKB:O95817}. Note=Colocalizes with HSF1 to the nucleus upon heat stress. {ECO:0000250|UniProtKB:O95817}.
Interaction partners:
- Heat shock cognate 71 kDa protein
- Heat shock protein beta-8
- Heat shock 70 kDa protein 1B
- E3 ubiquitin-protein ligase CHIP
- Apoptosis regulator Bcl-2
- BAG family molecular chaperone regulator 2
- Heat shock protein HSP 90-beta
- Heat shock protein beta-1
- Heat shock 70 kDa protein 4
- Heat shock factor protein 1
Sequence:
MSAATQSPMMQMASGNGASDRDPLPPGWEIKIDPQTGWPFFVDHNSRTTTWNDPRVPPEGPKDTASSANGPSRDGSRLLPIREGHPIYPQLRPGYIPIPVLHEGSENRQPHLFHAYSQPGVQRFRTEAAAATPQRSQSPLRGGMTEAAQTDKQCGQMPATATTAAAQPPTAHGPERSQSPAASDCSSSSSSASLPSSGRSSLGSHQLPRGYIPIPVIHEQNITRPAAQPSFHQAQKTHYPAQQGEYQPQQPVYHKIQGDDWEPRPLRAASPFRSPVRGASSREGSPARSGTPVHCPSPIRVHTVVDRPQPMTHREPPPVTQPENKPESKPGPAGPDLPPGHIPIQVIRREADSKPVSQKSPPPAEKVEVKVSSAPIPCPSPSPAPSAVPSPPKNVAAEQKAAPSPAPAEPAAPKSGEAETPPKHPGVLKVEAILEKVQGLEQAVDSFEGKKTDKKYLMIEEYLTKELLALDSVDPEGRADVRQARRDGVRKVQTILEKLEQKAIDVPGQVQVYELQPSNLEAEQPLQEIMGAVVADKDKKGPENKDPQTESQQLEAKAATPPNPSNPADSAGNLVAP
Protein: Acyl carrier protein (ACP) (Q72CS8)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Function: Carrier of the growing fatty acid chain in fatty acid biosynthesis.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01217}.
Interaction partners:
- Malonyl CoA-acyl carrier protein transacylase
- 3-oxoacyl-[acyl-carrier-protein] synthase 2
- Large ribosomal subunit protein bL32
- Large ribosomal subunit protein bL21
- Large ribosomal subunit protein uL13
- 3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ
- Alginate o-acetyltransferase AlgI, putative
- Large ribosomal subunit protein bL36
- Large ribosomal subunit protein uL14
- Enoyl-[acyl-carrier-protein] reductase
Sequence:
MSVEEKVKKIIMDQLGVSAEEVKPEASFVEDLGADSLDLTELIMAMEEEFGVEIDDDDAQKILKVKDAIDYVSNKQ
Protein: Filamentous haemagglutinin FhaB/tRNA nuclease CdiA-like TPS domain-containing protein (Q9HVG6)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- POTRA domain-containing protein
- ShlB/FhaC/HecB family hemolysin secretion/activation protein
- Uncharacterized protein
- POTRA domain-containing protein
- ShlB/FhaC/HecB family hemolysin secretion/activation protein
- POTRA domain-containing protein
- DUF3077 domain-containing protein
Sequence:
MVRPDSQRGKRTSSKAGREGRFVLAASSTLMFAIASINAAMAAPTGAQFNPNEIKISQQGKTTLIDQSTQRAIINWKGFDVSADEAVRFNQPGVTSSTLNRVTAGQESVIAGRISAPGQVIIYNSNGVVFSGSAKVDVGSLITTTANISDEHFRQGKLIFDQPGNPDARIVNDGSISVAEKGLAAFVAPSVANNGVINARLGTVAMAAGNAATIDLYGDGLVSIAVTDPVTRKPQDAQALVSNGGAIQADGGSVLITAEQASRVVDNAVNLSGVILARGTEVREGSVALVSKSGDIQIAGKIDVSGPKNGGDVLVSGQQVALASTASIDARGTAQGGSVRIGGDFQGRGELPRAKNATLAKGASIDVSATGKGNGGLAVVWSDGNTRMDGRILARGGAQGGNGGLVETSGKVNLSIADSAYVSVAAPYGNGGTWLLDPTTLRIVASGGTSGSVGGANGASGDATVNASVVTGALAGGKVTLSASDRLSVEAPLITSNLGGASRGLELIATGPAGAVDISAPILFRNGSLAIRAGGNINFLSGGTPQTSGIVDLGSGTLWMQTSTAGKISQQAGTALIAANLAGRAGSIDLASWDNYAGNLALQTFNGTLKYRQSNATGVTTSGTVFDPFINQSMTGTAQNIVSSVGTRILEANSVGTTGNYTLTADGNSEFDRLVFTALPYRRVSGSASFPTNDSSDYLVTNLRYQVNGSNVTATPNGGAPSGFTVAAGNGSVTTWTGNWGTSWGVKGFGGVIGVTDELQYDVGTGLTEELIFGLGGKTSRVDTRLDLFMREGAFNSFAERAQVEMFKTTTTAGDILSRQQTATLTANDATRVYGDVNPTLTATMSGINAIDAYVNSQFNDLYQATASTTATQASNVGQYAITGNANGSEYFSQRYQLVRQDGRLTVTPAQLIVSADAKTKVYGDADPTLTYQVSGLKNSDTAAGVLSGNLGRVAGENVGNYGILQGGLGLNTANYTLSYVGNDLRITPAQLNVIADAKTKVYGDLDPALTYQVSGLKRGDTAGAVLNGGSLSRVAGENVGVYGINQGGLGLVSSNYTLNYQGNNLTITKALLNVIADAKTKVYGDADPALTYQVSGLKNGDTAGAVLNGGSLSRVAGENVGVYGINQGGLGLLSANYDLSYQGNNLTITKALLNVIADAKTKVYGDADPSLTYQVSGLKNGDTAGSILTGGLNRAAGENVGVYGINQGDLALNSGNYDLSYQGNNLTITKALLNVIADAKTKVYGDADPSLTYQVSGLKNGDTAGAVLNGGGLVRVSGENVGNYAIQQGGLGLVSGNYDLAYQGNNLTITKALLNVIADAKTKVYGDADPSLTYQVSGLKNGDSAGSILTGGLNRAAGENVGVYGINQGDLALNSGNYDLSYQGNNLTITKALLNVIADAKTKVYGDADPSLTYQVSGLKNGDTAGAVLNGGGLVRVSGENVGNYAIQQGGLGLVSGNYDLAYQGNNLTITKALLNVIADAKTKVYGDADPSLTYQVSGLKNGDTAGAVLNGGSLSRVAGENVGVYGINQGDLALNSGNYDLSYQGNNLTITKALLNVIADAKTKVYGDADPSLTYQVSGLKNGDTAGAVLNGGGLVRVSGENVGNYAIQQGGLGLVSGNYDLAYQGNNLTITKALLNVIADAKTKVYGDADPSLTYQVSGLKNGDSAGSILTGGLNRAAGENVGVYGINQGDLALNSGNYDLSYQGNNLTITKALLNVIADAKTKVYGDADPSLTYQVSGLKNGDTAGAVLNGGGLVRVSGENVGNYAIQQGGLGLVSGNYDLAYQGNNLTITKALLNVIADAKTKVYGDADPSLTYQVSGLKNGDTAGAVLNGGSLSRVAGENVGVYGINQGGLGLVSGNYDLAYQGNNLTITKALLNVIADGKTKVYGDADPSLTYQVSGLKNGDSAGSILTGGLNRDAGENVGVYGINQGGLVLTSGNYDLAYQGNDLTITKALLNVFADAKSKQVGTADPALTYQVSGLKNGDSAGQVLAGGLGRVGGEAVGQYDILQGGLALTSGNYQLNYQGNLLSILPLPVTPGDLGQLAALSDLRELQKGRDPDTPGDAVYRTTTLENPFLENPFLRAYALGMDVSDPNLLPATAAGPAEDASAKRVGQFTDRPLRAEAESGAGCSNQSYLADYWSCFNKPLNF
Protein: Ski oncogene (Proto-oncogene c-Ski) (Q60698)
Organism: Mus musculus (Mouse)
Function: May play a role in terminal differentiation of skeletal muscle cells but not in the determination of cells to the myogenic lineage. Functions as a repressor of TGF-beta signaling.
Subcellular location: Nucleus.
Interaction partners:
- Mothers against decapentaplegic homolog 4
- Mothers against decapentaplegic homolog 2
- Mothers against decapentaplegic homolog 3
- Nuclear receptor corepressor 1
- Mothers against decapentaplegic homolog 5
- Mothers against decapentaplegic homolog 1
- Mothers against decapentaplegic homolog 9
- Nuclear receptor corepressor 2
- Paired amphipathic helix protein Sin3a
Sequence:
MEAAAAGRGGFQQPGLQKTLEQFHLSSMSSLGGPAVSRRAGQEAYKKESAKEAGAATVPAPVPTAAEPPPVLHLPAIQPPPPVLPGPFFMPSDRSTERCETVLEGETISCFVVGGEKRLCLPQILNSVLRDFSLQQINSVCDELHIYCSRCTADQLEILKVMGILPFSAPSCGLITKTDAERLCNALLYGGAYPPPCKKELAASLALGLELSERSVRVYHECFGKCKGLLVPELYSSPSAACIQCLDCRLMYPPHKFVVHSHKALENRTCHWGFDSANWRAYILLSQDYTGKEEQARLGRCLDDVKEKFDYANKYKRRVPRVSEPPASIRPKTDDTSSQSPASSEKDKQSTWLRTLAGSSNKSLGCTHPRQRLSAFRPWSPAVSASEKETSPHLPALIRDSFYSYKSFETAVAPNVALAPPTQQKVVNSPPCTTVVSRAPEPLTTCIQPRKRKLTLDTAGAPDMLTPVAAAEEDKDSEAEVEVESREEFTSSLSSLSSPSFTSSSSAKDLSSPGMHAPPVVAPDAAAHVDAPSGLEAELEHLRQALEGGLDTKEAKEKFLHEVVKMRVKQEEKLTAALQAKRTLHQELEFLRVAKKEKLREATEAKRNLRKEIERLRAENEKKMKEANESRVRLKRELEQARQVRVCDKGCEAGRLRAKYSAQVEDLQAKLQHAEADREQLRADLLREREAREHLEKVVRELQEQLRPRPRPEHPGGESNAELGP
Protein: Interleukin-25 (IL-25) (Interleukin-17E) (IL-17E) (Q9H293)
Organism: Homo sapiens (Human)
Function: Cytokine produced by various cells such as eosinophils, T-helper type 2 (Th2) cells or epithelial cells that plays a role in internal safety of adaptive immune responses by regulating cytokine production. Promotes and augments T-helper type 2 responses locally or systemically. Exerts its activity via its receptor composed of IL17RA and IL17RB for signal transduction (By similarity). In turn, stimulates the JAK2-STAT5A pathway and promotes the secretion of type-2 associated cytokines including IL4, IL9 and IL13. Induces also the release of IL8, and IL6 from eosinophils through the combined activation of MAPK and NF-kappa-B pathways. Inhibits the differentiation of T-helper (Th17) cells via the production of IL4, IL5 and IL13.
Subcellular location: Secreted.
Interaction partners:
- Interleukin-17 receptor B
- Interleukin-17 receptor A
- Interleukin-17B
- Interleukin-17D
- Interleukin-17F
- Interleukin-17 receptor C
- Interleukin-17A
- Interleukin-22
- Interleukin-33
- Interleukin-17 receptor E
Sequence:
MRERPRLGEDSSLISLFLQVVAFLAMVMGTHTYSHWPSCCPSKGQDTSEELLRWSTVPVPPLEPARPNRHPESCRASEDGPLNSRAISPWRYELDRDLNRLPQDLYHARCLCPHCVSLQTGSHMDPRGNSELLYHNQTVFYRRPCHGEKGTHKGYCLERRLYRVSLACVCVRPRVMG
Protein: E3 ubiquitin-protein ligase RING2 (EC 2.3.2.27) (RING finger protein 1B) (RING1b) (RING finger protein 2) (RING-type E3 ubiquitin transferase RING2) (Q803I4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: E3 ubiquitin-protein ligase that mediates monoubiquitination of 'Lys-119' of histone H2A (H2AK119Ub), thereby playing a central role in histone code and gene regulation. H2AK119Ub gives a specific tag for epigenetic transcriptional repression. Essential component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones, rendering chromatin heritably changed in its expressibility.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9CQJ4}. Cytoplasm {ECO:0000250|UniProtKB:Q9CQJ4}. Chromosome {ECO:0000250|UniProtKB:Q9CQJ4}.
Interaction partners:
- Polycomb complex protein BMI-1-A
- Polycomb group RING finger protein 1
- Polycomb complex protein BMI-1-B
- Polycomb group RING finger protein 6
- Chromobox homolog 2
- YY1-associated factor 2.
- RING1 and YY1-binding protein A
- Chromobox homolog 8a
- Polycomb group RING finger protein 5-B
- Polycomb protein eed
Sequence:
MTQTVQTNGVQPLSKTWELSLYELQRTPQEAITDGLEIAVSPRSLHSELMCPICLDMLKNTMTTKECLHRFCADCIITALRSGNKECPTCRKKLVSKRSLRPDPNFDALISKIYPSRDEYEAHQERVLARISKHNNQQALSHSIEEGLKIQAMNRLQRGKKHQIENGSGAEDNGDSSHCSNASVHSNQEAGPSIKRTKTSDDSGLDMDNATENGGGDIALDGVSEIELVFRPHPTLMEKEDAAQTRYIKTSGNATVDHLSKYLAVRLALEEMRKNGEASPINVEAASEKQYTIYIPTASNQFTVLNGSFSLELVSEKYWKVNKPMELYFAPTKEHK
Protein: Histone H2B type 1 (Q00715)
Organism: Rattus norvegicus (Rat)
Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Subcellular location: Nucleus. Chromosome.
Interaction partners:
- Histone H3.1
- Histone H3
- Histone H3.3
- Histone H3
- Histone H4
- Histone H3
- Histone H3
- Similar to H3 histone, family 3B.
- Breast cancer type 1 susceptibility protein homolog
- Histone H2A type 2-A
Sequence:
MPEPAKSRPAPKKGSKKAVTKAQKKDGKERKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGERRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK
Protein: Thromboxane A2 receptor (Prostanoid TP receptor) (T2HVK6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MASTNVTPLCFSTNTPPFKHNHTIASAYFSAVFSGLGLSSNLFALLVLAKTFHHTKSRSRSSFLLFLGGLVFTDFMGLLVTGSIVVSYHITHFNWRQLDPQCHFCNFMGMSMVFYGLCPLLLGAAMAVERFVGINRPFARSSMSNTRVCWTVALVWVTAGSISLLPLVGLGHYHLQVPGSWCFLNISSAPLDITFGLIFSLVGLASLAVSFLLNTVSVVTLLRVCCGADSTQRRRDYEVEMMVQLILIMVIASICWCPLLVFIAQTVLSGSELDVRYLLLWLRFATGNQVLDPWVYILFRRAILKRVAPKMDWSRGSIVSLYPTLSTSFRKLTRASLGGTLDRLDHIRPNPCIARQEDTPLPVLDTSATSV