wanglab/gogpt-training-data huggingface dataset:
Protein: Retinoic acid receptor, alpha (A0A0G2JW78)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU004334}.
Interaction partners:
- Retinoic acid receptor RXR-alpha
- Protein PML
- Promyelocytic leukemia zinc finger protein
- Retinoic acid receptor RXR-beta
- Nuclear receptor corepressor 1
- Nuclear receptor corepressor 2
- Transcription factor PU.1
- Nuclear receptor coactivator
- Retinoic acid receptor beta
- Nuclear receptor coactivator 2
Sequence:
MASNSSSCPTPGGGHLNGYPVPPYAFFFPPMLGGLSPPGALTSLQHQLPVSGYSTPSPATIETQSSSSEEIVPSPPSPPPLPRIYKPCFVCQDKSSGYHYGVSACEGCKGFFRRSIQKNMVYTCHRDKNCIINKVTRNRCQYCRLQKCFEVGMSKESVRNDRNKKKKETPKPECSESYTLTPEVGELIEKVRKAHQETFPALCQLGKYTTNNSSEQRVSLDIDLWDKFSELSTKCIIKTVEFAKQLPGFTTLTIADQITLLKAACLDILILRICTRYTPEQDTMTFSDGLTLNRTQMHNAGFGPLTDLVFAFANQLLPLEMDDAETGLLSAICLICGDRQDLEQPDKVDMLQEPLLEALKVYVRKRRPSRPHMFPKMLMKITDLRSISAKGAERVITLKMEIPGSMPPLIQEMLENSEGLDTLSGQSGGGTRDGGGLAPPPGSCSPSLSPSSHRSSPATQSP
Protein: Neuronal acetylcholine receptor subunit alpha-3 (P09481)
Organism: Gallus gallus (Chicken)
Function: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Subcellular location: Synaptic cell membrane {ECO:0000250|UniProtKB:P04757}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:P32297}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P04757}. Golgi apparatus {ECO:0000250|UniProtKB:P04757}. Note=Interaction with UBXN2A/UBXD4 promotes translocation to the plasma membrane. {ECO:0000250|UniProtKB:P04757}.
Interaction partners:
- Neuronal acetylcholine receptor subunit beta-4
- Neuronal acetylcholine receptor subunit alpha-5
- Neuronal acetylcholine receptor subunit beta-2
- Acetylcholine receptor subunit alpha
Sequence:
MQSIHALLLTAAVCILFQGCGGSEPEHRLYAALFKNYNQFVRPVKNASDPVIIQFEVSMSQLVKVDEVNQIMETNLWLKHIWNDYKLRWNPVDYGGAEFIRVPSGQIWKPDIVLYNNAVGDFQVDDKTKALLKYTGDVTWIPPAIFKSSCKIDVTYFPFDYQNCTMKFGSWSYDKAKIDLVLIGSTMNLKDYWESGEWAIIKAPGYKHDIKYNCCEEIYTDITYSLYIRRLPLFYTINMIIPCLLISFLTVLVFYLPSDCGEKVTLCISVLLSLTVFLLVITETIPSTSLVIPLIGEYLLFTMIFVTLSIVITVFVLNVHYRTPKTHTMPVWVRTIFLNLLPRIMFMTRPTSDEENNQKPKPFYTSEFSNLNCFNSSEIKCCKDGFVCQDMACSCCQYQRMKFSDFSGNLTRSSSSESVDPLFSFSVLSPEMRDAIESVKYIAENMKMQNEAKEIQDDWKYVAMVIDRIFLWVFILVCILGTAGLFLQPLMTGDDM
Protein: Cyclin-dependent kinase 14 (EC 2.7.11.22) (Cell division protein kinase 14) (Serine/threonine-protein kinase PFTAIRE-1) (O35495)
Organism: Mus musculus (Mouse)
Function: Serine/threonine-protein kinase involved in the control of the eukaryotic cell cycle, whose activity is controlled by an associated cyclin. Acts as a cell-cycle regulator of Wnt signaling pathway during G2/M phase by mediating the phosphorylation of LRP6 at 'Ser-1490', leading to the activation of the Wnt signaling pathway. Acts as a regulator of cell cycle progression and cell proliferation via its interaction with CCDN3. Phosphorylates RB1 in vitro, however the relevance of such result remains to be confirmed in vivo. May also play a role in meiosis, neuron differentiation and may indirectly act as a negative regulator of insulin-responsive glucose transport (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasm. Nucleus. Note=Recruited to the cell membrane by CCNY. {ECO:0000250}.
Interaction partners:
- Cyclin-Y
- G1/S-specific cyclin-D3
Sequence:
MCDLIEPQPAEKIGKMKKLRRTLSESFSRIALKKEDTTFDEICVTKMSTRNCQGTDSVIKHLDTIPEDKKVRVQRTQSTFDPFEKPANQVKRVHSENNACINFKSSSAGKESPKVRRHSSPSSPTSPKFGKADSYEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTPFTAIREASLLKGLKHANIVLLHDIIHTKETLTLVFEYVHTDLCQYMDKHPGGLHPDNVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLARAKSVPSHTYSNEVVTLWYRPPDVLLGSTEYSTCLDMWGVGCIFVEMIQGVAAFPGMKDIQDQLERIFLVLGTPNEDTWPGVHSLPHFKPERFTVYSSKSLRQAWNKLSYVNHAEDLASKLLQCSPKNRLSAQAALSHEYFSDLPPRLWELTDMSSIFTVPNVRLQPEAGESMRAFGKNNSYGKSLSNSKH
Protein: Protein-L-isoaspartate O-methyltransferase (EC 2.1.1.77) (G8JY24)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MAWRSSGSTNSELIDNLRNNRVFASQRAYDAMKSVDRGDFAPRAPYEDAPQRIGYNATHAAALDYLQNHLVAGAKALDVGSGSGYLTVCMAMMVGRNGTVVGIEHMPQLVELSEKNIRKHHSEQLERGNVIIIEGDGRQGFAEKAPYNAIHVGAASKGVPKALTDQLAEGGRMMIPVEQVDGNQVFMQIDKINGKIEQKIVEHVIYVPLTSREEQWNRN
Protein: Metalloprotease PmbA (EC 3.4.-.-) (Protein TldE) (P0AFK0)
Organism: Escherichia coli (strain K12)
Function: Metalloprotease involved in CcdA degradation. Suppresses the inhibitory activity of the carbon storage regulator (CsrA).
Subcellular location: Cytoplasm.
Interaction partners:
- Metalloprotease TldD
- Uncharacterized protein McbA
- UDP-N-acetylmuramate--L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptandioate ligase
Sequence:
MALAMKVISQVEAQRKILEEAVSTALELASGKSDGAEVAVSKTTGISVSTRYGEVENVEFNSDGALGITVYHQNRKGSASSTDLSPQAIARTVQAALDIARYTSPDPCAGVADKELLAFDAPDLDLFHPAEVSPDEAIELAARAEQAALQADKRITNTEGGSFNSHYGVKVFGNSHGMLQGYCSTRHSLSSCVIAEENGDMERDYAYTIGRAMSDLQTPEWVGADCARRTLSRLSPRKLSTMKAPVIFANEVATGLFGHLVGAIAGGSVYRKSTFLLDSLGKQILPDWLTIEEHPHLLKGLASTPFDSEGVRTERRDIIKDGILTQWLLTSYSARKLGLKSTGHAGGIHNWRIAGQGLSFEQMLKEMGTGLVVTELMGQGVSAITGDYSRGAAGFWVENGEIQYPVSEITIAGNLKDMWRNIVTVGNDIETRSNIQCGSVLLPEMKIAGQ
Protein: Zinc finger protein RP-8, isoform A (Zinc finger protein RP-8, isoform B) (Q9W1A3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Small ribosomal subunit protein uS5
- Protein BCCIP homolog
- Protein LTV1 homolog
- Nufip
Sequence:
MEIDLGFAEKSDNGAWLSNRYFPSKLGGQPAWLELEALPPTSQLQCSKCRAPKSFLAQLYAPFEDEYNFHRSIYVFLCRNSDCQEAQNASNFTVLRSQLPRKNKFFSEEEPSDVGQPLPAVPCLKKLCAACGCHAPHACSKCKAIHYCSPEHQRAHWPQHKPNCGAPEVATEKPLTQIVFPEFEIVMDSNPVESGEEDKDDEARLAEFQELESSGKTGDLSNVSEAEMDKYFGNSAAADDKTFRQFKKQTAAEPDQIVRYKRGGQPLWITNTVKTVEDQLNKLPNCIACGGERQFEFQIMPQALTLLEDENLDWGVLAVYTCAKSCPIDGYVEELLIKQDIVAEDQS
Protein: NAD-dependent protein deacylase sirtuin-5, mitochondrial (EC 2.3.1.-) (Regulatory protein SIR2 homolog 5) (SIR2-like protein 5) (Q68FX9)
Organism: Rattus norvegicus (Rat)
Function: NAD-dependent lysine demalonylase, desuccinylase and deglutarylase that specifically removes malonyl, succinyl and glutaryl groups on target proteins. Activates CPS1 and contributes to the regulation of blood ammonia levels during prolonged fasting: acts by mediating desuccinylation and deglutarylation of CPS1, thereby increasing CPS1 activity in response to elevated NAD levels during fasting. Activates SOD1 by mediating its desuccinylation, leading to reduced reactive oxygen species. Activates SHMT2 by mediating its desuccinylation. Modulates ketogenesis through the desuccinylation and activation of HMGCS2. Has weak NAD-dependent protein deacetylase activity; however this activity may not be physiologically relevant in vivo. Can deacetylate cytochrome c (CYCS) and a number of other proteins in vitro such as UOX.
Subcellular location: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03160}. Cytoplasm, cytosol {ECO:0000255|HAMAP-Rule:MF_03160}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03160}. Note=Mainly mitochondrial. Also present extramitochondrially, with a fraction present in the cytosol and very small amounts also detected in the nucleus. {ECO:0000255|HAMAP-Rule:MF_03160}.
Interaction partners:
- Sirtuin 6 6
- NAD-dependent protein deacetylase
- NAD-dependent protein deacetylase sirtuin-2
- NAD-dependent protein deacetylase sirtuin-7
- NAD-dependent protein lipoamidase sirtuin-4, mitochondrial
- Nicotinamide phosphoribosyltransferase
- Nicotinamide-nucleotide adenylyltransferase
- Glutamine-dependent NAD
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2
- NAD-dependent protein deacetylase sirtuin-1
Sequence:
MRPLPVAPGRLFSQLCCGPKPSASPQSKICLTMARPSSNMADFRKCFANAKHIVIISGAGVSAESGVPTFRGTGGYWRKWQAQHLATPLAFAHNPSQVWEFYHYRREVMRNKEPNPGHLAIAQCEARLRDQGRRVVVITQNIDELHRKAGTKNLLEIHGTLFKTRCTSCGNVAENYKSPICPALLGKGAPEPDTQESRIPVHKLPRCEEAGCGGLLRPHVVWFGENLDPAILKEVDRELARCDLCLVVGTSSVVYPAAMFAPQVASRGVPVAEFNMETTPATNRFRFHFPGPCGVTLPEALAPHETERIS
Protein: Profilin-2 (Q20025)
Organism: Caenorhabditis elegans
Function: Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- Actin
- Actin-depolymerizing factor 2, isoform c
- Gelsolin-like protein 1
- Actin-related protein 2
- WAPL domain-containing protein
- Ras-like GTP-binding protein rhoA
- FH2 domain-containing protein
- Actin
- Actin-related protein 10
- Cell division control protein 42 homolog
Sequence:
MSGWDDYIKLLFGKSPAIKRAAIIGSDGSVWARSGDANAFRATEVELKRFAALFNDINSVPGTGADLEEIHYIVPRVEEKLIFGKKEQTGFFAAKTNQAIVIAMYEGDNAQSASVRAGVEYIAQYLASSGY
Protein: Major sperm protein (O44782)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004211}; Single-pass type IV membrane protein {ECO:0000256|ARBA:ARBA00004211}.
Interaction partners:
- Ephrin receptor 1
- Oxysterol-binding protein
- Tar DNA-binding protein homolog 1
- Phosphofurin acidic cluster sorting protein 2
- Receptor-type tyrosine-protein phosphatase
- Major sperm protein
- START domain-containing protein
- Charged multivesicular body protein 2b
- Endoplasmic reticulum transmembrane protein
Sequence:
MSEKHSLLQVTPNRELVFTGPFSDVVTSHMTLKNTSTNPVCFKVKTTAPKQYCVRPNSGLLKSGDSKQITVMLQPLEGIPSDAGRHKFMVQSCVAPSEDLPDLESVWKIIDPAELTYSKLMVTFVDKRDPASGDDTKTFAVRNEDSFASSGQAQELGSSYSGTPSHDGTVNSLRKSLKSTVDEKEELQKKVHGLEQEIEVMLKKNRKLQQSHSDGALVDGAYPTLQIFLIAVAALLIGLIVGRLF
Protein: Sarcomere length short, isoform E (A0A0B4K633)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGLDFLDEWFLSQVPAPPPLPSLVPKAPPPPPPPLAPGEKRVLSSTQKETLEKLRTRPRRRPDWSEMMKEVESGKKLRHVACNDRSQPILTCKSITKLDDKFIYETEKGNSHNKLLKQIQGGIKLKPTKTNDRSKPVLDGLRKFRRQMTIEEQLQKSQSKINMLSEAPSSHALGPGSATALGAGGSRPSIVSAMSIDEESPDELDDIDKIRDDLQSTKQMLALELRNREAQDRENKKLLAKIRTLETELEREKSREKNLEYGSNVIVATMDPTPTAEQTYVNSLKREVEDARKVSKEVEQNYQSTAEQLVEAKTEIEEQRRQIQLLERKLAAALQGGGSLDGSRRPSDANFGRDSSPELEPEVSESDPDEPEEKKVERRERRSGKELKILRSKLTKLKVKEEAAKKEKDALKQAMKKNQSILKEENKKFKKLEKEVQKMAASMKLDEDDVDGEEKDEDEEEAEEEHASEEEEESDDESEESESEESEAETGSESEPEDSPNSAKKANVEPRVKKHESRFAAMKKCNVLLQANVDNLQDQIVQVRSRATNLQDELDAVIADLGF
Protein: Carnitine O-Acetyl-Transferase, isoform E (EC 2.3.-.-, EC 2.3.1.7) (A0A126GUQ4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKFRGNGKLLWNLTKNSLAQQSPNGIAKKVLPASSYSTVQKTIPLEQPNLLKYHVLPLEETLNRFMTTVEPLLTPEEFQRQKGITSEFLKKQGRELQLLLEETGSKEKNWLAHRWLKAAYLTYRDPVTVFVSPGMTFPKQNFRDSRAFVDYTARVIYGLGEFNDMVHANKIPIVKMGKNELDNSQFGKVFGTCRIPRRGTDEIVYNPDSDYVVVIYKNHFYQLKIYSKEGKLIAAPCLAAQLENIVLKETQVGVPYGILTTDSRDNWAEAYEYLVETPGNRDALKTIQGALFTVSLDEGTILKEGEETDELILSLIHGSGSKINSGNRWMDKTIQLVVNPNGNVGFTYEHSPAEGQPIAMMMDYVVQKMKEDPSFGQSGSQDFAPAQKIQFSSSNKSLEKSLNVAQENVDKLADALQMKVLKFNGFGKDFIKKQRLGPDSFVQMALQLAFYKMHSEPPAQYESAHLRIFDGGRTETIRSCSNESLAFSRAMQDPNVTDQERAAKLREAVVSHQTYAKLALQGKGVDRHLLGLKLMALEHSKPIPEFFKSPGFVKSSHFRMSTSQVATKYDAFMGYGPATDDGYACCYNPRDNDIILAISAWRHCPITDHLKFVKTLEQSFFEMKNVLEKNPPETKSKL
Protein: 26S proteasome regulatory subunit 8 (O18413)
Organism: Drosophila melanogaster (Fruit fly)
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 complex subunit p50
- Probable 26S proteasome non-ATPase regulatory subunit 3
- 26S proteasome non-ATPase regulatory subunit 1
- 26S proteasome regulatory subunit 7
- 26S proteasome non-ATPase regulatory subunit 4
- 26S proteasome non-ATPase regulatory subunit 11
- 26S proteasome non-ATPase regulatory subunit 7
- Proteasomal ubiquitin receptor ADRM1 homolog
- GH11341p
- 26S proteasome regulatory subunit 4
Sequence:
MTVTNRMEIESAYHKGEGFRSYYIQKIEELQLVVAEKHQNLRRLQAQRNELNAKVRMLREELQLLQEQGSYVGEVVKPMDKKKVLVKVHPEGKFVVDLDKNIDINDVTPNCRVALRNESYTLHKILPNKVDPLVSLMMVEKVPDSTYEMVGGLDKQIKEIKEVIELPVKHPELFDALGIAQPKGVLLYGPPGTGKTLLARAVAHHTECTFIRVSGSELVQKFIGEGSRMVRELFVMAREHAPSIIFMDEIDSIGSSRIESGSGGDSEVQRTMLELLNQLDGFEATKNIKVIMATNRIDILDPALLRPGRIDRKIEFPPPNEEARLDILKIHSRKMNLTRGINLRKIAELMPGASGAEVKGVCTEAGMYALRERRVHVTQEDFEMAVAKVMQKDSEKNMSIKKLWK
Protein: Nucleolar protein 6 (Q95XY4)
Organism: Caenorhabditis elegans
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}. Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604, ECO:0000256|RuleBase:RU364032}.
Interaction partners:
- Periodic tryptophan protein 2 homolog
- Nucleolar protein 14
- U3 small nucleolar RNA-associated protein 13 C-terminal domain-containing protein
- WD_REPEATS_REGION domain-containing protein
- NUC153 domain-containing protein
- HEAT repeat-containing protein 1 homolog
- WD_REPEATS_REGION domain-containing protein
- Ribosomal RNA-processing protein 7 homolog
- Small-subunit processome Utp12 domain-containing protein
- WD repeat-containing protein 46
Sequence:
METDGDVLPMSNAFKLLCEDTAPKSNKKLIEKQRQIAQKIKNVLETSKNGPKIQYKNLDFWTEFDVKHPLHHLQKAVDATSSSIPEFQWTPPKSIVITEKGQQIFIEIPPKALGNRDFLNLTYAAKRGHFACHVARLLSGKFEKVEFTAGGAHRDDPIFADILVDGVRIGFYCPELAKTKRFAPNIGNLRPATIFEDLFKETEIATPKFNQRMLWSILELEIAQEMEKELKAQKTARLAIFLLGNFFENRHLQHAITPIILTARVVRLVKNGKITENQEILTVLRVIFEDFITWSADDVEFVDSVEDDVDVEEYSQLFDVNLVWKNLNLASNLTKNYMERMKKELTICYPLLGQVYAFDPIFIEKLPVFAHYDHVARLHINISQLAEHLVEFGIDSIDNRDVIHKFVLSFEHKIEQTMSERYDFVGIHDISSNAEKSTWSLSEYPEKYRQKTYLIGFRSTSGWKNPLTVGPPAQTNDAKEFRELWKETSELRKFADTRICECVVWSEKPSEKVPRAVLQFVLQKMFSLPATCFSWRALTSSSTSAEADQQHEKKSQEAVFKAYTDLSTVLRGLKGLPLMITNVHGISGYLRGSEPAYPSVFAATSSTNKSSEDQHYVLPEIGKIPLFTPTVTVHIKLEYSGKWGNDVEAIRRLTSSFYVKIAERLREQHKLTAVPTIDQLFILKSGIVFKIVVVNDRILTILEEDVQKLKDSGASRIESSIQGMRLSMWKKKFISEPLLQLSLQSFSTSHKFFGSTVQLFKKWLGSKFLSGHHLNDHIIELLVVAAIGKKGQVPPQSTWSSFCRLLSLISTHPWSARPLIVDFGTKGFSEDERSKLEEKFIKMRPILPPMVVIYEEDHLGSKFTRENPQGIVLNRLVAVAREALKMMEKQAFGEKSIEMETSLLTENLSPYDAIINLEPCAVVRKKALMERKPPAETSKFRQKIPVVELDPVDELVYQLNNSFQQVAMFFYNKYGGHHIGVMFKPQEDEVPAKISRCSLHKSVSDSTLRLNRDEILENIQILGQGIVSDVQLKKQ
Protein: Proteasome subunit beta (A2ACR1)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU004203}. Nucleus {ECO:0000256|RuleBase:RU004203}.
Interaction partners:
Sequence:
MAVEFDGGVVMGSDSRVSAGEAVVNRVFDKLSPLHERIYCALSGSAADAQAVADMAAYQLELHGIELEEPPLVLAAANVVRNISYKYREDLSAHLMVAGWDQREGGQVYGTLGGMLTRQPFAIGGSGSTFIYGYVDAAYKPGMSPEECRRFTTDAIALAMSRDGSSGGVIYLVTITAAGVDHRVILGNELPKFYDE
Protein: Signal peptidase complex subunit 2 (F4JGB4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU368033}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU368033}.
Interaction partners:
- Signal peptidase complex subunit 2
Sequence:
MEEKKTESATKNVKKVNLLDHIAIKHLLDESVSDIVTSRGYKEDVRLSNVKFLLGGIIIVVALVAQFYNKKCGICLLLDFGKYVVLTAVMQLILYIKEKNAILFTYPLEGSFTSTGLVVSSKLPRFSDQYTLTIDSADPQSISAGKSVQFTKSVTQWLTKDGVLVEGLFWKDVEALVKEYTEAGEPKKKR
Protein: GH04080p (Prophenoloxidase 1 (EC 1.10.3.1, EC 1.14.18.1)) (Q7K2W6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Phenoloxidase 2
- Aromatic-L-amino-acid decarboxylase
- Aspartate aminotransferase, cytoplasmic
- Aspartate aminotransferase
- Tyrosine 3-monooxygenase
- Tyrosine aminotransferase
- Phenoloxidase 3
- MIP05841p)
- 3,4-dihydroxyphenylacetaldehyde synthase
- Serine protease inhibitor 27A
Sequence:
MTNTDLKALELMFQRPLEPAFTTRDSGKTVLELPDSFYTDRYRNDTEEVGNRFSKDVDLKIPIQELSNVPSLEFTKKIGLKNQFSLFNNRHREIASELITLFMSAPNLRQFVSLSVYTKDRVNPVLFQYAYAVAVAHRPDTREVPITNISQIFPSNFVEPSAFRDARQEASVIGESGARVHVDIPQNYTASDREDEQRLAYFREDIGVNSHHWHWHLVYPTTGPTEVVNKDRRGELFYYMHHQILARYNVERFCNNLKKVQPLNNLRVEVPEGYFPKILSSTNNRTYPARVTNQKLRDVDRHDGRVEISDVERWRDRVLAAIDQGYVEDSSGNRIPLDEVRGIDILGNMIEASPVLSINYNFYGNLHNEGHNIISFAHDPDYRHLEEFGVMGDVTTAMRDPIFYRWHGFIDTVFNKFKTRLNPYNAGELNFDGITVDYIEAKIGKSNTKANTLLTYWQKSSADLAAGLDFGPTTDRNIFASFTHLQNAPFTYTFNVTNNGARRTGTCRIFICPKVDERNQALNLEEQRLLAIEMDKFTVDLVPGENTIRRQSTESSVAIPFERSFRPVGADYQPKAADELARFKFCGCGWPQHLLLPKGNAQGMVFDLFVMISDYSQDSVEQPKTPNDACSTAYSFCGLKDKLYPDRRTMGYPFDRRLPNANLTELVGAFGNMAKTDLRIVFNDRVIDKA
Protein: Membrane-anchored lipid-binding protein YSP2 (Lipid transfer at contact site protein 4) (Lipid transfer protein anchored at membrane contact sites 3) (Yeast suicide protein 2) (Q06681)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in induction of programmed cell death in response to reactive oxygen species (ROS). May be involved in sterol transfer between intracellular membranes.
Subcellular location: Mitochondrion membrane {ECO:0000269|PubMed:16962064}; Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:26001273}; Single-pass membrane protein {ECO:0000255}. Note=Localizes to puncta in the cell periphery representing cortical endoplasmic reticulum (cER)-plasma membrane (PM) membrane contact sites. {ECO:0000269|PubMed:26001273}.
Interaction partners:
- Membrane-anchored lipid-binding protein LAM1
- Membrane-anchored lipid-binding protein SIP3
- Calcium-channel protein CCH1
- Protein PRY1
- Serine/threonine-protein kinase YPK1
Sequence:
MRDEATRKKRSFSDGHFFKKLKLMSRKKQPVMERSKTTRTRKESTNSAAKSSLSLRRANNGRKTIAKRRVLTDIGSTNEGVAGNSGSNSPAQYSHTPHFSDSIPPLPLELPDIVSIRSSRSHISNKSNKNKHGIDLTFIPRRSLQNSKAGLKKPNTSPQGYFNIPVTIDRASEKVKHTDTKNTFNSSSSENERPVLSILQKDDSQSSSHPAIDSMSAPNNINNNNDIENSSNSLFDTILSIAHSAISHVPKISALNTEIQREFSHSGESHTGSTRHPYFHIHHAQQQHPLSQQQGPLPVSENANQNPNDTVLIHSPSANTAHRSSSFLRHLDYLLSPTSGPASDKHTQVEEGDDEEELSPLSKAFLSPSTQLVPTNTSTTPLSGSLTPNNRNVNANSNSETENDNDRDDRSNVGKVKFQPLKVHEPAISTFGKGNLTLEAVAGSSDIDNTTIDLDENNTNNNPNASSTNLSHISKSNVNNNLGPKELNTSYRNSTYIDMARFENSQSNLSSHRARSKTLPANKALENAVGDEGNSKRNSRYSSYSNDMAFDDADERKFRSMSKKFLNRRSFSPSNLGNKVIPGINLRNSFNKNRNSSSDFFSTNQGQQMPRTSTAGSGNIHAIMGLDSGNDDFKLEGIEYASEKKNSEFHTLFKDCDINPNEKLIVDHSCALSRDILLQGRMYISDAHIGFFSNILGWVSTVFIPFKEIVQIEKKTTAGIFPNGIVIDTLHTKYIFASFMSRDATFDLITDVWNQIILGKKYRNGFGNNDDGTISDSSSAFFDDSDDNDDDGDLDDDDPDINSTDMTSSDDIDADVFNESNDLGKNQKSTNYLLGPNKHSPTTADFKPSNNDHLVIEANINAPLGKVVNLLYGEDVSYYERILKAQKNFEISPIPNNFLTKKIRDYAYTKPLSGSIGPSKTKCLITDTLEHYDLEDYVKVLSITKNPDVPSGNIFSVKTVFLFSWDKNNSTKLTVYNSVDWTGKSWIKSMIEKGTFDGVADTTKIMISEIKKILSDEDSNINSKHQASNNESEEEIINLPTIGPPVHDPTEPDFQKGKDDTVIDEKINIPVPLGTVFSLLYGDDTSYIKKIIENQNNFNVCDIPKFVNNAREITYTKKLNNSFGPKQTKCIVTETIEHMDLNSFFMVKQIVRSPDVPYGSSFSVHTRFFYSWGDHNTTNMKVVTNVVWTGKSMLKGTIEKGSIDGQRSSTKQLVDDLKKIISNASSTKKKSRRRGKTVNKRKSSPSTIKNEKNEENFEDTSTKNSFFSAFSMLQQVNITSVQGIMTIISFFICLIFFFRLLFHSKNTSNIQIITPGTILINGNEYNYVPNFKTLYHVYEDNIIKDARRKDSNKNNIVTDTEGLIWDWLIDRGNGTVQNSVLSNHIKESNNKKVKLVNGVSDHKIQQLVESIKITELQLQEMKELLAQTDNTSATNQLL
Protein: Trimeric intracellular cation channel type B (TRIC-B) (TRICB) (Transmembrane protein 38B) (Q9NVV0)
Organism: Homo sapiens (Human)
Function: Monovalent cation channel required for maintenance of rapid intracellular calcium release. May act as a potassium counter-ion channel that functions in synchronization with calcium release from intracellular stores.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9DAV9}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9DAV9}.
Interaction partners:
- Cartilage-associated protein
- Peptidyl-prolyl cis-trans isomerase FKBP10
- Prolyl 3-hydroxylase 1
- Interferon-induced transmembrane protein 5
- Protein transport protein Sec24D
- Cyclic AMP-responsive element-binding protein 3-like protein 1
- Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2
- Membrane-bound transcription factor site-2 protease
- Pigment epithelium-derived factor
Sequence:
MDSPWDELALAFSRTSMFPFFDIAHYLVSVMAVKRQPGAAALAWKNPISSWFTAMLHCFGGGILSCLLLAEPPLKFLANHTNILLASSIWYITFFCPHDLVSQGYSYLPVQLLASGMKEVTRTWKIVGGVTHANSYYKNGWIVMIAIGWARGAGGTIITNFERLVKGDWKPEGDEWLKMSYPAKVTLLGSVIFTFQHTQHLAISKHNLMFLYTIFIVATKITMMTTQTSTMTFAPFEDTLSWMLFGWQQPFSSCEKKSEAKSPSNGVGSLASKPVDVASDNVKKKHTKKNE
Protein: At2g03200 (Eukaryotic aspartyl protease family protein) (Putative chloroplast nucleoid DNA binding protein) (Q84M99)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MASSSSSSLLFPFFLILFSCLISVSSSRRSLIDRTLPKNLPRSGFRLSLRHVDSGKNLTKIQKIQRGINRGFHRLNRLGAVAVLAVASKPDDTNNIKAPTHGGSGEFLMELSIGNPAVKYSAIVDTGSDLIWTQCKPCTECFDQPTPIFDPEKSSSYSKVGCSSGLCNALPRSNCNEDKDACEYLYTYGDYSSTRGLLATETFTFEDENSISGIGFGCGVENEGDGFSQGSGLVGLGRGPLSLISQLKETKFSYCLTSIEDSEASSSLFIGSLASGIVNKTGASLDGEVTKTMSLLRNPDQPSFYYLELQGITVGAKRLSVEKSTFELAEDGTGGMIIDSGTTITYLEETAFKVLKEEFTSRMSLPVDDSGSTGLDLCFKLPDAAKNIAVPKMIFHFKGADLELPGENYMVADSSTGVLCLAMGSSNGMSIFGNVQQQNFNVLHDLEKETVSFVPTECGKL
Protein: General odorant-binding protein 99a (Q9VAJ4)
Organism: Drosophila melanogaster (Fruit fly)
Function: Present in the aqueous fluid surrounding olfactory sensory dendrites and are thought to aid in the capture and transport of hydrophobic odorants into and through this fluid.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- GEO11742p1
Sequence:
MKVFVAICVLIGLASADYVVKNRHDMLAYRDECVKELAVPVDLVEKYQKWEYPNDAKTQCYIKCVFTKWGLFDVQSGFNVENIHQQLVGNHADHNEAFHASLAACVDKNEQGSNACEWAYRGATCLLKENLAQIQKSLAPKA
Protein: 3-oxopimeloyl-[acyl-carrier-protein] synthase (3-oxopimeloyl-[ACP] synthase) (EC 2.3.1.-) (Q9EYU2)
Organism: Rhizobium loti (Mesorhizobium loti)
Function: Involved in the formation of the biotin precursor pimeloyl-ACP (Probable). Catalyzes the condensation of glutaryl-CoA, an intermediate in lysine degradation, with malonyl-ACP to produce 3-oxopimeloyl-ACP (By similarity).
Interaction partners:
Sequence:
MSRSSRVLGFGHHAPSRKVENPEIENRLGLEPGWIERRTGIRSRFWATDQDTLSGLATQAGDMALANAGIDRSDIGLLLLATSTPDHLLPPSAPLVAHKLGLGRAGAVDLTGACAGFIYALMFADGFTRLHGKASLVIAANILSRRINPAERASSVLFADAAGALVIGACEDPDLGILGASVDSDGSRYGLIQIPAGGSSIPFHDDLDLGQTRMTMTDGREVFAKAVEMMTDCSTSALAVAGVRPQDIDRFVPHQANARIFDAVGRNLGIADEAIVKTIAEYGNSSAATIPLSLSLAHRAAPFRPGEKVLLAAAGAGLSGGAIVVGI
Protein: Transcription factor MYB83 (Myb-related protein 83) (AtMYB83) (Q9C6U1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor that acts as molecular switch in the NAC012/SND1-mediated transcriptional network regulating secondary wall biosynthesis. Is directly activated by NAC012/SND1 and its close homologs, including NAC043/NST1, NAC066/NST2, NAC101/VND6 and NAC030/VND7. Is required for functional expression of a number of secondary wall-associated transcription factors and secondary wall biosynthetic genes involved in cellulose, xylan and lignin synthesis. Functions redundantly with MYB46 in the transcriptional regulatory cascade leading to secondary wall formation in fibers and vessels. Transcription activator that binds to the DNA consensus sequence 5'-ACC[AT]A[AC][TC]-3', designated as the secondary wall MYB-responsive element (SMRE). Regulates directly numerous transcription factors and a number of genes involved in secondary wall biosynthesis that contain SMRE elements in their promoters.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:19808805}.
Interaction partners:
- NAC domain-containing protein 30
- NAC domain-containing protein 43
- NAC domain-containing protein 12
- NAC domain-containing protein 73
- NAC domain-containing protein 66
- NAC domain-containing protein 10
- Homeobox protein knotted-1-like 7
- NAC domain-containing protein 7
- Cellulose synthase A catalytic subunit 8
- Cellulose synthase A catalytic subunit 7
Sequence:
MMMRKPDITTIRDKGKPNHACGGNNNKPKLRKGLWSPDEDEKLIRYMLTNGQGCWSDIARNAGLLRCGKSCRLRWINYLRPDLKRGSFSPQEEDLIFHLHSILGNRWSQIATRLPGRTDNEIKNFWNSTLKKRLKNNSNNNTSSGSSPNNSNSNSLDPRDQHVDMGGNSTSLMDDYHHDENMMTVGNTMRMDSSSPFNVGPMVNSVGLNQLYDPLMISVPDNGYHQMGNTVNVFSVNGLGDYGNTILDPISKRVSVEGDDWFIPPSENTNVIACSTSNNLNLQALDPCFNSKNLCHSESFKVGNVLGIENGSWEIENPKIGDWDLDGLIDNNSSFPFLDFQVD
Protein: Elongation of very long chain fatty acids protein (EC 2.3.1.199) (Very-long-chain 3-oxoacyl-CoA synthase) (A0A0A0MTI6)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}.
Interaction partners:
Sequence:
MEHFDASLSTYFKALLGPRDTRVKGWFLLDNYIPTFICSVIYLLIVWLGPKYMRNKQPFSCRGILVVYNLGLTLLSLYMFCELVTGVWEGKYNFFCQGTRTAGESDMKIIRVLWWYYFSKLIEFMDTFFFILRKNNHQITVLHVYHHASMLNIWWFVMNWVPCGHSSVCADNHPDQLRGHLAVHIPSWLVVFPDWIHDFPDCSLHKLLHSDLQQERGLPKERPPEGPPEWVHGCCEWTHQQLFTPGKQCEAKEAAEGLKSKN