wanglab/gogpt-training-data huggingface dataset:
Protein: Ubiquitin-like protein NEDD8 (Neddylin) (F1QMF9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- E3 ubiquitin-protein ligase RBX1
- NEDD8-activating enzyme E1 catalytic subunit
- NEDD8-activating enzyme E1 regulatory subunit
- Cullin 2
- SUMO peptidase family member, NEDD8-specific
- Cullin-1
- NEDD8-conjugating enzyme UBC12
- COP9 signalosome complex subunit 5
- Cullin-5
- NEDD8-conjugating enzyme UBE2F
Sequence:
MLIKVKTLTGKEIEIDIEPTDKVERIKERVEEKEGIPPQQQRLIYSGKQMNDEKTAADYKIQGGSVLHLVLALRGGQIHQKPDRLLLNM
Protein: Histone acetyltransferase (EC 2.3.1.48) (A0A3F2YNX6)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU361211}.
Interaction partners:
Sequence:
MVKLANPLYTEWILEAIKKVKKQKQRPSEERICNAVSSSHGLDRKTVLEQLELSVKDGTILKVSNKGLNSYKDPDNPGRIALPKPRNHGKLDNKQNVDWNKLIKRAVEGLAESGGSTLKSIERFLKGQKDVSALFGGSAASGFHQQLRLAIKRAIGHGRLLKDGPLYRLNTKATNVDGKESCESLSCLPPVSLLPHEKDKPVAEPIPICSFCLGTKEQNREKKPEELISCADCGNSGHPSCLKFSPELTVRVKALRWQCIECKTCSSCRDQGKNADNMLFCDSCDRGFHMECCDPPLTRMPKGMWICQICRPRKKGRKLLQKKAAQIKRRYTNPIGRPKNRLKKQNTVSKGPFSKVRTGPGRGRKRKITLSSQSASSSSEEGYLERIDGLDFCRDSNVSLKFNKKTKGLIDGLTKFFTPSPDGRKARGEVVDYSEQYRIRKRGNRKSSTSDWPTDNQDGWDGKQENEERLFGSQEIMTEKDMELFRDIQEQALQKVGVTGPPDPQVRCPSVIEFGKYEIHTWYSSPYPQEYSRLPKLYLCEFCLKYMKSRTILQQHMKKCGWFHPPANEIYRKNNISVFEVDGNVSTIYCQNLCLLAKLFLDHKTLYYDVEPFLFYVLTQNDVKGCHLVGYFSKEKHCQQKYNVSCIMILPQYQRKGYGRFLIDFSYLLSKREGQAGSPEKPLSDLGRLSYMAYWKSVILECLYHQNDKQISIKKLSKLTGICPQDITSTLHHLRMLDFRSDQFVIIRREKLIQDHMAKLQLNLRPVDVDPECLRWTPVIVSNSVVSEEEEEEAEEGENEEPQCQERELEISVRVGKSVSHENKEQDSYSVESEKKPEVMAPVSSTRLSKQVLPHDSLPANSQPSRRGRWGRKNRKTQERFGDKDSKLLLEETSSAPQEQYGECGEKSEATQEQYTESEEQLVASEEQPSQDGKPDLPKRRLSEGVEPWRGQLKKSPEALKCRLTEGSERLPRRYSEGDRAVLRGFSESSEEEEEPESPRSSSPPILTKPTLKRKKPFLHRRRRVRKRKHHNSSVVTETISETTEVLDEPFEDSDSERPMPRLEPTFEIDEEEEEEDENELFPREYFRRLSSQDVLRCQSSSKRKSKDEEEDEESDDADDTPILKPVSLLRKRDVKNSPLEPDTSTPLKKKKGWPKGKSRKPIHWKKRPGRKPGFKLSREIMPVSTQACVIEPIVSIPKAGRKPKIQESEETVEPKEDMPLPEERKEEEEMQAEAEEAEEGEEEDAASSEVPAASPADSSNSPETETKEPEVEEEEEKPRVSEEQRQSEEEQQELEEPEPEEEEDAAAETAQNDDHDADDEDDGHLESTKKKELEEQPTREDVKEEPGVQESFLDANMQKSREKIKDKEETELDSEEEQPSHDTSVVSEQMAGSEDDHEEDSHTKEELIELKEEEEIPHSELDLETVQAVQSLTQEESSEHEGAYQDCEETLAACQTLQSYTQADEDPQMSMVEDCHASEHNSPISSVQSHPSQSVRSVSSPNVPALESGYTQISPEQGSLSAPSMQNMETSPMMDVPSVSDHSQQVVDSGFSDLGSIESTTENYENPSSYDSTMGGSICGNSSSQSSCSYGGLSSSSSLTQSSCVVTQQMASMGSSCSMMQQSSVQPAANCSIKSPQSCVVERPPSNQQQQPPPPPPQQPQPPPPQPQPAPQPPPPQQQPQQQPQPQPQQPPPPPPPQQQPPLSQCSMNNSFTPAPMIMEIPESGSTGNISIYERIPGDFGAGSYSQPSATFSLAKLQQLTNTIMDPHAMPYSHSPAVTSYATSVSLSNTGLAQLAPSHPLAGTPQAQATMTPPPNLASTTMNLTSPLLQCNMSATNIGIPHTQRLQGQMPVKGHISIRSKSAPLPSAAAHQQQLYGRSPSAVAMQAGPRALAVQRGMNMGVNLMPTPAYNVNSMNMNTLNAMNSYRMTQPMMNSSYHSNPAYMNQTAQYPMQMQMGMMGSQAYTQQPMQPNPHGNMMYTGPSHHSYMNAAGVPKQSLNGPYMRR
Protein: RNA-binding suppressor of PAS kinase protein 1 (Q05672)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- DNA-directed RNA polymerase III subunit RPC2
- Cytochrome b-c1 complex subunit 1, mitochondrial
- DNA-directed RNA polymerases I and III subunit RPAC2
- Cytochrome b-c1 complex subunit 2, mitochondrial
- DNA-directed RNA polymerases I and III subunit RPAC1
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
Sequence:
MTALDSRNWGLTPAMETGLFQKPQDRIFIIELENSIVSFINSNTESFQLRPMNSYYRLLSHQIAEYHNLNHVLARTQDSCVILFKGENFQKIEGKPLLQELQLNKKPEECASSSESIEKSNNNRIFRILKRKEVGNECDYKIDGNTRTPNSNLTANSNKDQKIEIDDKSSTDLEQERIEKERLYEQRKQEIFDKLNKSEDDVKSTNSSGSSDSDNEWSDWLNGDDSNTQTSNGSVSSSSPFNSSVTTIQVNKPQQQFYDSRRGRGGRRRGTNNYKDAYRGQSRRNKENGGYQSGYSSPYLVYPPPQMGGNSLPTYPLMYNPAGPAPGPAPSPMVMGNNTVFMNPYMYNMNPQGSCSFGTPIPMYPPYQYQYQYQYNTQYHSGPYSNTPSYNSNNYTRSSANKYHHFQGKNSYSGAIPKRSDDSNSNKNEGIRRASVEGSPSSRDTDSVEMKFDKLNI
Protein: Protein byr4 (Q10951)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has an essential role in ensuring cytokinesis and septation occur only once during mitosis. It does so by interacting with the ras1 signaling pathways, thereby suppressing them.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Cell division control protein 16
- Septum-promoting GTP-binding protein 1
- Cell division control protein 7
- Septation initiation network scaffold protein cdc11
- Septation initiation protein sid4
- Serine/threonine-protein kinase sid1
- Maintenance of ploidy protein mob1
- Serine/threonine-protein kinase plo1
- Probable E3 ubiquitin-protein ligase dma1
- Serine/threonine-protein kinase sid2
Sequence:
MTEVECWDDDPDFASDVDNASLFTQSIATTSASTSVDDGFSFDDSISRLNSLSISDVPSAHSRVEQWNQQVHNLNHELSSNKNRISSNVEGYEDDFSFDEEGEEGNNEFNTLRPNKYQDADVDEFNTIRASETASQRPPIPFSSDTLKKTYLSSENDARYPSVSDSPYCESEGFSSFEDDFEIDPDTDLNSILHRKQNRMDPKASFSSVEQSSLRTPSSAHNDDGFWDDFDIDFNNETESIFRKKIRSPNTINQKHPYISSTISYQPNVHQDAKYYPLCKDIFPSLANENPHSDNPNLKYSSKTLSKRDTSSHYPETLKASSKHSSPVKGNSSISSTWTPSNLKIYHSKNSMGLMDLDALKTVASNSKYRTKPKNCKTYGDGTELDTLDELPVDYEFELKLRKKQTTKVSGTPKSKHAGSTQEWHSHTTPRSTSKHENNLNNITNSAKNEHIRSQRQHKTHAAPSKELTKESLSNDQLSVKEKRRHHKKAPTLIQNLNSPRTPKIVGKMRYNPTKHCWEGNDYAIRDFDTPISPSRPALISNISTKKGIQVVGNMVYDPTRLRWIDNSISGQEAEDPFSGFDDLEDTDSTSQYLNENSGSFNGSINSIINFPDMSEIYDVGPEFEKKQFSEDIQWRKRIDGWFFSFKNDDRSRLWELYNILNAEQ
Protein: CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase 1, chloroplastic/mitochondrial (EC 2.7.8.5) (Phosphatidylglycerophosphate synthase 1) (PGP synthase 1) (Protein JOVTENKY) (O80952)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the committed step to the synthesis of the acidic phospholipids. Transfers specifically a phosphatidyl group from CDP-diacylglycerol to glycerol-3-phosphate to form phosphatidylglycerophosphate. Cannot catalyze the phosphatidyl group transfer to inositol, serine, choline or phosphatidylglycerol. Possesses high activity with CDP-dipalmitoylglycerol and low activity with CDP-dioleoylglycerol.
Subcellular location: Plastid, chloroplast membrane {ECO:0000269|PubMed:12609031}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000269|PubMed:12609031, ECO:0000305|PubMed:11741606}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Phosphatidylglycerophosphate phosphatase 1, chloroplastic/mitochondrial
- Phosphatidate cytidylyltransferase 1
- Probable CDP-diacylglycerol--inositol 3-phosphatidyltransferase 2
- Phosphatidate cytidylyltransferase 5, chloroplastic
- Phosphatidate cytidylyltransferase 4, chloroplastic
- Phosphatidate cytidylyltransferase 3
- Phosphatidate cytidylyltransferase 2
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase 1
- Phosphatidylserine decarboxylase proenzyme 1, mitochondrial
- Cardiolipin synthase
Sequence:
MLRSGLASLIVDVNLRRTLRPSPTFSFPAHLSRCIITSRYSSRTSLRFPIQISRHQHRLSYFSSSSSSEQSRPTSSSRNSFSGHGQLDSDDNSSPPPSQSSSKVLTLPTVLTLGRVAAVPLLVATFYVDSWWGTTATTSIFIAAAITDWLDGYLARKMRLGSAFGAFLDPVADKLMVAATLILLCTKPIQVAELGPLPWLLTVPSIAIIGREITMSAVREWAASQNGKLLEAVAVNNLGKWKTATQMTALTILLASRDSNVGWLVASGAGLLYVSAGLSVWSLAVYMRKIWKVLMK
Protein: Oxidoreductase-like protein SRL4 (Suppressor of RAD53 and LCD1 4) (Suppressor of RAD53 null lethality 4) (Q03085)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May be involved in the regulation of dNTP production. Induces the SOS system when expressed in E.coli, therefore, it may play a role in DNA metabolism and/or in genome stability.
Interaction partners:
- Protein BOP2
- Cell wall protein PIR5
Sequence:
MKKTIYKVLVSFYQYVGLGKKFHPSHDTVLIIGGSSNELGIELCETFIEDYHTKVINIDTIDSINGKNARRSEKLYTFISCKDFSDIKCLEESMLYLQNLEIIPTVLINNMQEGIESTLLKEDKFLRLDEESLNEFEKIVRYNLQSVILITKFCLSNIFPKVQAEAQEKAKGFYIVNISSVLTLKPCKSGTHFITSKCGINSFHDGITSELKLKDSNLNVKTLIAYLPSFESEAHWKRLSPSISKHLVHCLLEGRYGDTILESKRSIGDILLITGFKSSFT
Protein: Uncharacterized protein (Q583F6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- GTP-binding nuclear protein
- RNA binding protein, putative
Sequence:
MTSSWGPQQHEALVQFLRNVTSSDMNVQRDNILQLQRFAFSGGAAIFLLEVLCSGNESYEASIRHSAGLILKQIVQINPTIIDCLNADIVGPPLLRALADTIPSVNVAASLVVASIVRGEGLLQRWPQLLETLKNESSLTFLRCQQATDMEGFFTVSRTVQGLATCTRIVCEECNEELRELIEADSSACECLGELFSYMLQAVAFMLRSGGDVASAMQLVLSAATSCFVEKVFFLSDNPDESFDDSTPEASLDVSTAPDHTLHYAKQLHEQVCALVAELCTAPFNQHVLVATTEYLSEALRWDTESSASTINATVLFLPHVLYRIRSHESEEESIVIRCLTLLGDIAETHATVLSGIAREVAETLFYNAVHLTDIFPNTSEEETTSAPDDEATVRPVVLNRRNVEAGDAEDHSDENKSDINSCGATDRSDGQESDAECATTKKQVFTHILDVMSCTCPGDLLAHLIPLITSALTREANSVESLKEQQAALFILAEVVDELFDDLHDDFLGHVSANCWGALGPNSTAPHHLRYQAVRCVARMSTGWAASARRPAHLQGLISPPPVLHLLIGVTASEVSKQVQLEAINSITKVTLYSLDDCRIDGETRAVASALSTVIRGLVSALPSMQYAARTATYRCLSEVLSVASGNEQRQQEPLIDDITTMHTITALGKQGQQLASLLHHGENKKKSGTNAVELISLMNAMVEVVSAASKGTLEDVVSPLTEFALVVLNCSADTEGNSSSIMEVYGSDIATLVFDMLDGCCSALMNEEELLCMIDSSLRTAVLLKNVMVGYGTGAANNVVSVCAQILEERQRRQQFGEVELARSCVAFLSTAMHFHRDPHMVATICRLCLTEVACEMPAVKAISNVFLCLGLIFYNLLFDHNADPVPILHVVVPSQSLNNLTETLRSYLTSSTAQDRGYVKMNAFICAVALAALHQVGRLHLDVAEPLLFAVIHASPSFIPRVKNHIGEAYRLLLMLSLLLAADQSNWAPVVPTIVKAIDSFTSTAPTVLSAEVRRRYLPLVGANGQ
Protein: INO80 complex subunit E (H3BNM4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MNGPADGEVDYKKKYRNLKRKLKFLIYEHECFQEELRKAQRKLLKVSRDKSFLLDRLLQYENVDEDSSDSDATASSDNSETEGTPKLSDTPAPKRKRSPPLGGAPSPSSLSLPPSTGFPLQASGVPSPYLSSLPEPSPLRPKREKRPRLPRKLKMAVGPPDCPVGGPLTFPGRGSGAGVGTTLTPLPPPKMPPPTILSTVPRQMFSDAGSGDDALDGDDDLVIDIPE
Protein: Protein AATF (Apoptosis-antagonizing transcription factor) (Rb-binding protein Che-1) (Traube protein) (Q9JKX4)
Organism: Mus musculus (Mouse)
Function: May function as a general inhibitor of the histone deacetylase HDAC1. Binding to the pocket region of RB1 may displace HDAC1 from RB1/E2F complexes, leading to activation of E2F target genes and cell cycle progression. Conversely, displacement of HDAC1 from SP1 bound to the CDKN1A promoter leads to increased expression of this CDK inhibitor and blocks cell cycle progression (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:11071758}.
Interaction partners:
- Neuroguidin
- Nucleolar protein 10
- RNA cytidine acetyltransferase
- Nucleolar protein 14
- WD repeat-containing protein 43
- U3 small nucleolar RNA-associated protein 18 homolog
- DDB1- and CUL4-associated factor 13
- WD repeat-containing protein 3
- BMS1 homolog, ribosome assembly protein
- Nucleolar protein 58
Sequence:
MAAPQPLALQLEQLLNPRPREADPEADPEEATRARVIDRFDEGEEEKDDLAVSSIRKLAPVSLLDTDKRYSGKTTSRKAWKEDHWEQALPSSSDNEASDEGGSEDGDSEGLGLEEISEDVDEDLEDNKISDEGGSEDGDSEGLGLEEFSEDVEEDLEGEDEEDREEDRNSEDDGVVAAFSSVKVSEEVEKGRAVKNQIALWDQLLEGRIKLQKALLTTNQLPQPDVFPVFKDKGGPEFASALKNSHKALKALLRSLVDLQEELLFQYPDTRHIVNGAKPNTESEEISSEDDELVGEKKKQRKAPPKRKLEMEDYPSFMAKRFADFTIYRNHTLQKWHDKTKLASGKLGKGFGAFERSILTQIDHIMMDKERLLRRTQTKRSAYRVLGKPEPVPEPVAETLPGEPETLPQGPANAHLRDLDEEIFDDDDFYHQLLRELIERKTSSLDPNDQVAMGRQWLAIQKLRSKIRKKVDRKASKGRKLRFHVLSKLLSFMAPIDHTAMSDDARTELFRSLFGQLNPPDADRGK
Protein: Pentatricopeptide repeat-containing protein At1g18485 (Q0WN60)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Prolamin-like protein
- Polyribonucleotide nucleotidyltransferase 2, mitochondrial
- U4/U6 small nuclear ribonucleoprotein PRP4-like protein
- Protein PLASTID REDOX INSENSITIVE 2
- Anaphase-promoting complex subunit 11
Sequence:
MASVLLPLPQVFVLFDYRRSRKESSFPRAVYNSNSISSNSTNANHFLRRISNFCETGDLDKSFRTVQEFVGDDESSSDAFLLVREALGLLLQASGKRKDIEMGRKIHQLVSGSTRLRNDDVLCTRIITMYAMCGSPDDSRFVFDALRSKNLFQWNAVISSYSRNELYDEVLETFIEMISTTDLLPDHFTYPCVIKACAGMSDVGIGLAVHGLVVKTGLVEDVFVGNALVSFYGTHGFVTDALQLFDIMPERNLVSWNSMIRVFSDNGFSEESFLLLGEMMEENGDGAFMPDVATLVTVLPVCAREREIGLGKGVHGWAVKLRLDKELVLNNALMDMYSKCGCITNAQMIFKMNNNKNVVSWNTMVGGFSAEGDTHGTFDVLRQMLAGGEDVKADEVTILNAVPVCFHESFLPSLKELHCYSLKQEFVYNELVANAFVASYAKCGSLSYAQRVFHGIRSKTVNSWNALIGGHAQSNDPRLSLDAHLQMKISGLLPDSFTVCSLLSACSKLKSLRLGKEVHGFIIRNWLERDLFVYLSVLSLYIHCGELCTVQALFDAMEDKSLVSWNTVITGYLQNGFPDRALGVFRQMVLYGIQLCGISMMPVFGACSLLPSLRLGREAHAYALKHLLEDDAFIACSLIDMYAKNGSITQSSKVFNGLKEKSTASWNAMIMGYGIHGLAKEAIKLFEEMQRTGHNPDDLTFLGVLTACNHSGLIHEGLRYLDQMKSSFGLKPNLKHYACVIDMLGRAGQLDKALRVVAEEMSEEADVGIWKSLLSSCRIHQNLEMGEKVAAKLFELEPEKPENYVLLSNLYAGLGKWEDVRKVRQRMNEMSLRKDAGCSWIELNRKVFSFVVGERFLDGFEEIKSLWSILEMKISKMGYRPDTMSVQHDLSEEEKIEQLRGHSEKLALTYGLIKTSEGTTIRVYKNLRICVDCHNAAKLISKVMEREIVVRDNKRFHHFKNGVCSCGDYW
Protein: DsRNA activated Z-DNA binding protein kinase (Protein kinase containing Z-DNA binding domains) (Q0H740)
Organism: Salmo salar (Atlantic salmon)
Interaction partners:
Sequence:
MSCDNRQGDQLDLKERICTFLKVKKEGSTALQIAKAVGLKTAKDVNSVLYTLNRAGLLNATPDKPPVWSVEKPGAASVSVSVPESDRVPSPSETPGITVEELRRVLTSKSDGRGMSAQEIARELGQSRKCVNKHLYDLQSSGKAEKLGEKVWKMNDEASCGGELIEYQSDYQDISIRLTESSRFSKDFKLLSVLGAGGFGCVIKAQHKLDGETYAVKIVKNMGEANREVKALATLEHSSIVRYYTTWPEDANWVDGGYSTESSVLSEISEDSDNYSDQGDGSTHVTKQSDLDLSETASEDQANHSMTDSSSRNGDWPCLFIQMEFCDGGTLKDWISINKGRTKDKALGIFQQLVCGVEYIHSEGLIHRDLKPENILFGSDGMVKIGDFGLVTTITTLSGASMYRTVNKGTPFYMSPEQTGGKYDEKTDIFSLGLIWFELLWYMSTVSEKSKVFESLQTRTFPCDFREKFIFEHKLISKMLSELPANRQNAKEIAALLKSNLFGNQAGIPQKTV
Protein: FERM domain-containing protein 8 (iRhom tail-associated protein) (iTAP) (Q3UFK8)
Organism: Mus musculus (Mouse)
Function: Promotes the cell surface stability of iRhom1/RHBDF1 and iRhom2/RHBDF2 and prevents their degradation via the endolysosomal pathway. By acting on iRhoms, involved in ADAM17-mediated shedding of TNF, amphiregulin/AREG, HBEGF and TGFA from the cell surface (By similarity). Negatively regulates Wnt signaling, possibly by antagonizing the recruitment of AXIN1 to LRP6 (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9BZ67}. Cell membrane {ECO:0000250|UniProtKB:Q9BZ67}.
Interaction partners:
- Inactive rhomboid protein 2
- Tigger transposable element-derived protein 3
Sequence:
MEGAEGNAGQPGPAERSHRSSVSSVGARAADVLVYLADDTVVPLAVENLSSISAHELHRAVREVLQLPDVALEAFALWLVSPLLEVQLKPKHQPYKLGRQWPELLLRFTNASDDDVAMDEPSLQFRRNVFFPRRRELQIHDEEVLRLLYEEAKGNVLTARYPCDLEDCEVLGGLVCRVQLGPYQPGQPAACTLREKLDSFLPAHLCKRGHGLFAAFRGRGAKTGPGEQGLLNAYRQVKEVTGNNSEREATLGSHYRAYLLKCHELPFYGCAFFHGEVDKPAQGFLHRGGRKPVTVAISLEGVHVIDNREKHVLLGLRFQELSWDHTSPEEEEPVLWLEFDGDSEGTPVNKLLRIYSKQAELMSGLIEYCIELSQAAEPTLSQESASGPHEAPSPSPPPTQRPKLRRQGSVVCSRIQHLSTIDYVEDGKGIKRVKPKRTTSFFSRQLSSSQGSYTVVQPTDDSLEQS
Protein: Actin-related protein 2 (Actin-like protein 2) (Q9UUJ1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Functions as ATP-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the pointed end of the daughter actin filament (By similarity). During cytokinesis it colocalizes to the cortical actin patches until spetation is complete. Has a role in the mobility of these patches. Essential for viability.
Subcellular location: Cytoplasm, cytoskeleton, actin patch {ECO:0000269|PubMed:10588653}.
Interaction partners:
- Actin-related protein 2/3 complex subunit 5
- Actin-related protein 2/3 complex subunit 3
- Actin-related protein 2/3 complex subunit 2
- Actin-related protein 2/3 complex subunit 1
- Actin-related protein 2/3 complex subunit 4
- Actin-related protein 3
- Actin-binding protein wsp1
- Actin
- Actin-depolymerizing factor gmf1
- Profilin
Sequence:
MESAPIVLDNGTGFVKVGYAKDNFPRFQFPSIVGRPILRAEEKTGNVQIKDVMVGDEAEAVRSLLQVKYPMENGIIRDFEEMNQLWDYTFFEKLKIDPRGRKILLTEPPMNPVANREKMCETMFERYGFGGVYVAIQAVLSLYAQGLSSGVVVDSGDGVTHIVPVYESVVLNHLVGRLDVAGRDATRYLISLLLRKGYAFNRTADFETVREMKEKLCYVSYDLELDHKLSEETTVLMRNYTLPDGRVIKVGSERYECPECLFQPHLVGSEQPGLSEFIFDTIQAADVDIRKYLYRAIVLSGGSSMYAGLPSRLEKEIKQLWFERVLHGDPARLPNFKVKIEDAPRRRHAVFIGGAVLADIMAQNDHMWVSKAEWEEYGVRALDKLGPRTT
Protein: Abscisic acid receptor PYL9 (ABI1-binding protein 4) (PYR1-like protein 9) (Regulatory components of ABA receptor 1) (Q84MC7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Receptor for abscisic acid (ABA) required for ABA-mediated responses such as stomatal closure and germination inhibition. Inhibits the activity of group-A protein phosphatases type 2C (PP2Cs) in an ABA-independent manner but more efficiently when activated by ABA. Confers enhanced sensitivity to ABA. Can be activated only by (+)-ABA but not by (-)-ABA.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9FLB1}. Nucleus {ECO:0000250|UniProtKB:O49686}. Cell membrane {ECO:0000250|UniProtKB:O49686}. Note=Localizes at the plasma membrane in the presence of a CAR protein. {ECO:0000250|UniProtKB:O80920}.
Interaction partners:
- Protein phosphatase 2C 56
- Protein phosphatase 2C 16
- Protein phosphatase 2C 77
- Transcription factor MYB44
- Protein phosphatase 2C 37
- DET1- and DDB1-associated protein 1
- Probable protein phosphatase 2C 78
- Protein phosphatase 2C 7
- Probable protein phosphatase 2C 24
- Protein phosphatase 2C 3
Sequence:
MMDGVEGGTAMYGGLETVQYVRTHHQHLCRENQCTSALVKHIKAPLHLVWSLVRRFDQPQKYKPFVSRCTVIGDPEIGSLREVNVKSGLPATTSTERLELLDDEEHILGIKIIGGDHRLKNYSSILTVHPEIIEGRAGTMVIESFVVDVPQGNTKDETCYFVEALIRCNLKSLADVSERLASQDITQ
Protein: Endoplasmic reticulum membrane adapter protein XK (Membrane transport protein XK) (XK homolog) (XK-related protein 1) (Q9QXY7)
Organism: Mus musculus (Mouse)
Function: Recruits the lipid transfer protein VPS13A from lipid droplets to the endoplasmic reticulum (ER) membrane.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305|PubMed:25231987}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P51811}.
Interaction partners:
- Kell blood group glycoprotein homolog
- Endothelin-3
- Intermembrane lipid transfer protein VPS13A
Sequence:
MKFPASVIASVFLFVAETAAALYLSSTYRSAGDRMWQVLTLLFSLMPCALVQFTLLFVHRDLSRDRPLALLMHLLQLGPLYRCCEVFCIYCQSDQNEEPYVSITKKRQMPKDGLSEEVEKEVGQAEGKLITHRSAFSRASVIQAFLGSAPQLTLQLYITVLEQNITTGRCFIMTLSLLSIVYGALRCNILAIKIKYDEYEVKVKPLAYVCIFLWRSFEIATRVIVLVLFTSVLKIWVVAVILVNFFSFFLYPWIVFWCSGSPFPENIEKALSRVGTTIVLCFLTLLYAGINMFCWSAVQLKIDNPELISKSQNWYRLLIYYMTRFIENSVLLLLWYFFKTDIYMYVCAPLLILQLLIGYCTGILFMLVFYQFFHPCKKLFSSSVSESFRALLRCACWSSLRRKSSEPVGRIDTDLKACTEQDVMPTTSKVIPEATDIWTAVDLCSA
Protein: DNA-directed RNA polymerase 3, chloroplastic (EC 2.7.7.6) (NsRpoT-C) (T7 bacteriophage-type single subunit RNA polymerase 3) (P69242)
Organism: Nicotiana sylvestris (Wood tobacco) (South American tobacco)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:12061895, ECO:0000269|PubMed:12435389}.
Interaction partners:
- rRNA adenine N
- Protein TPLATE
- rRNA adenine N
- rRNA adenine N
Sequence:
MASTASYSPSPTSQWRTQKLPKRFNFYVIHNQEFGKLSQSSSLPTSSFPKTLKLPVIQMPINNNIQSQTTVCVSTDENLEELVNLQKIANGVLTKESNKRVFIQDPPWVSSLFMNSLFVRAKQVQGVRREFREIERRRRYAMLRRRQIKAETEAWEQMVEEYRELEREMCEKKLAPNLPYVKKLLLGWFEPLRQAIEKEQNAETTVKHRAAFAPHIDSLPADKMAVIVMHKLMGLLMMGGKEERCVQVVQAAVQIGMAVENEVRIHNFLEKTKKLQKHMTGAQSQEDMSRETMILRKRVKSLIKRNRVVEVRKLMKSEEPESWGRDTQAKLGCRLLELLTETAYVQPPVDQSADTPPDIRPAFRHVFRIATRDPGKSIVKKYGVIECDPLVVAGVDRTVKQMMIPYVPMLVPPKKWRGYDKGGYLFLPSYLMRTHGSRRQQDAVRSVPTKQMQQVYEALDTLGSTKWRVNKRILSVVESIWAGGGNIAGLVDRKDVPIPELHSDDIMEVKKWKWRVRKSKKINQELHSQRCDTELKLSVARKLKDEEGFYYPHNLDFRGRAYPMHPHLNHLSSDLCRGILEFAEGRPLGKSGLRWLKIHLASLYAGGIEKLCYDARLAFVENHIDDILDSANNPLNGNRWWLNAEDPFQCLAACINLSEALKSSSPHTVFSHLPIHQDGSCNGLQHYAALGRDSMEAAAVNLVAGDKPADVYTEIALRVDHIIRGDSIKDPATDPNALLAKLLIDQVDRKLVKQTVMTSVYGVTYVGAREQIKRRLEEKGLIDDDRLLFTASCYAAKVTLAALGELFQAARGTMTWLGDCAKVIASENQPVRWTTPLGLPVVQPYFKTQRHVIRTSLQVLALQREGDTVEVRKQRTAFPPNFVHSLDGSHMMMTAVACRDAGLQFAGVHDSFWTHACDVDQMNRILREKFVELYSMPILEDLLESFQNSYPALTFPPLPKRGDFDLVEVLESPYFFN
Protein: Uncharacterized protein (Q582N6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- fumarate reductase
Sequence:
MADNEEVPPSGPRMTREETDELVRRLYDQQMERAARREEERQRQLARPFCSSRRIKKDEEENLVRRIYDVQRERFQQSKEERERRLTLELQSKDKKLPESEIQDQVDRIYNQEVAKSKARREELQKRYLPEVPPKTIGKKQLKESVERLFRVDYVKRDEELFKKHVYPYDPPTTKISRTDVEAMANRLSRRGS
Protein: DNA-binding protein inhibitor ID-1 (Inhibitor of DNA binding 1) (Inhibitor of differentiation 1) (P20067)
Organism: Mus musculus (Mouse)
Function: Transcriptional regulator (lacking a basic DNA binding domain) which negatively regulates the basic helix-loop-helix (bHLH) transcription factors by forming heterodimers and inhibiting their DNA binding and transcriptional activity. Implicated in regulating a variety of cellular processes, including cellular growth, senescence, differentiation, apoptosis, angiogenesis, and neoplastic transformation. Inhibits skeletal muscle and cardiac myocyte differentiation. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-BMAL1 heterodimer.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16516211}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:16516211}.
Interaction partners:
- Thrombospondin-1
- Protein C-ets-2
- Transcription factor E2-alpha
- Ras-related protein Rap-1b
- Ras-related protein Rap-1A
- Transcription factor 4
- Myoblast determination protein 1
- Forkhead box protein O3
- Transcription factor COE2
Sequence:
MKVASGSAAAAAGPSCSLKAGRTAGEVVLGLSEQSVAISRCAGTRLPALLDEQQVNVLLYDMNGCYSRLKELVPTLPQNRKVSKVEILQHVIDYIRDLQLELNSESEVGTTGGRGLPVRAPLSTLNGEISALAAEVRSESEYYIILQWETEATGGGCPPSLLFRRIAI
Protein: Sigma factor AlgU negative regulatory protein (P38107)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Negative regulator of the sigma factor AlgU. Plays a role in the differentiation of P.aeruginosa into the alginate-producing form. Inactivation of mucA causes a switch from the non-mucoid to mucoid state resulting in constitutive expression of alginate biosynthetic genes.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- RNA polymerase sigma-H factor
- Sigma factor AlgU regulatory protein MucB
- AlgW protein
- Probable periplasmic serine endoprotease DegP-like
- Positive regulator for alginate biosynthesis MucC
- Positive alginate biosynthesis regulatory protein
- Glycine zipper 2TM domain-containing protein
- GDP-mannose 6-dehydrogenase
- Alginate biosynthesis transcriptional regulatory protein AlgB
- RNA polymerase sigma-54 factor
Sequence:
MSREALQETLSAVMDNEADELELRRVLAACGEDAELRSTWSRYQLARSVMHREPTLPKLDIAAAVSAALADEAAPPKAEKGPWRMVGRLAVAASVTLAVLAGVRLYNQNDALPQMAQQGTTPQIALPQVKGPAVLAGYSEEQGAPQVITNSSSSDTRWHEQRLPIYLRQHVQQSAVSGTESALPYARAASLENR
Protein: D-amino acid dehydrogenase (EC 1.4.99.-) (D-alanine dehydrogenase) (P0A6J5)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the oxidative deamination of D-amino acids. Has broad substrate specificity; is mostly active on D-alanine, and to a lesser extent, on several other D-amino acids such as D-methionine, D-serine and D-proline, but not on L-alanine. Participates in the utilization of L-alanine and D-alanine as the sole source of carbon, nitrogen and energy for growth. Is also able to oxidize D-amino acid analogs such as 3,4-dehydro-D-proline, D-2-aminobutyrate, D-norvaline, D-norleucine, cis-4-hydroxy-D-proline, and DL-ethionine.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:13292, ECO:0000269|PubMed:15358424}; Peripheral membrane protein {ECO:0000269|PubMed:13292, ECO:0000269|PubMed:15358424}.
Interaction partners:
- Alanine racemase, catabolic
- Alanine racemase, biosynthetic
- Histidinol-phosphate aminotransferase
- Aspartate aminotransferase
- Aromatic-amino-acid aminotransferase
- Hydroxycarboxylate dehydrogenase B
- L-alanine exporter AlaE
Sequence:
MRVVILGSGVVGVASAWYLNQAGHEVTVIDREPGAALETSAANAGQISPGYAAPWAAPGVPLKAIKWMFQRHAPLAVRLDGTQFQLKWMWQMLRNCDTSHYMENKGRMVRLAEYSRDCLKALRAETNIQYEGRQGGTLQLFRTEQQYENATRDIAVLEDAGVPYQLLESSRLAEVEPALAEVAHKLTGGLQLPNDETGDCQLFTQNLARMAEQAGVKFRFNTPVDQLLCDGEQIYGVKCGDEVIKADAYVMAFGSYSTAMLKGIVDIPVYPLKGYSLTIPIAQEDGAPVSTILDETYKIAITRFDNRIRVGGMAEIVGFNTELLQPRRETLEMVVRDLYPRGGHVEQATFWTGLRPMTPDGTPVVGRTRFKNLWLNTGHGTLGWTMACGSGQLLSDLLSGRTPAIPYEDLSVARYSRGFTPSRPGHLHGAHS