wanglab/gogpt-training-data huggingface dataset:
Protein: U3 small nucleolar RNA-associated protein 25 (Q57UR4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
- Nrap protein domain-containing protein
- Sas10 C-terminal domain-containing protein
- Small-subunit processome Utp21 domain-containing protein
- U3 small nucleolar ribonucleoprotein protein MPP10, putative
- U3 small nuclear ribonucleoprotein
- Nop14-like protein
- RRM domain-containing protein
- rRNA biogenesis protein, putative
- BING4 C-terminal domain-containing protein
- PIN domain-containing protein
Sequence:
MGKPGGFFKRLKNKQKRLATHRRRGTKGASKEERRLKHNELVDYYAAKREAEELAAISSSSSSESEAASTDSELEARKEEKSLLALRRVLGIADGGRAVKRGRNNSHNGNDNNNGNNSKRKGVENQRDNDLSNVDTTAVNGTVPSDGGDDDWRTFLPQDEEEDEEEELEELEEENSYAIESDGQEVGTEDGSLEEDDAEDVMSMEESEEDEEGEDSGKEDAYEDDEEGDGDQQKFEEEKVQLLPQFHLGTAKLEALQRVVREDDPWFTKYHIDKHGSIDRSPMKLLKQKYHTEYGQIAVSASAHAMEHLIHEPFRVGWQGTASAPQKLDKRPPYMHETLWNKWLDYRAAKSRGPMTAEQRGLLDLLQGYPDVMDCCRSAENAEARREVFLLHALNHWYKARAVMVLHEAFLHEKKRQKRKNSKKKVKGSSAVSSKNLDDSDGEDGEYELRDRGFGKTRLLIMLPMRNIAHEYVTTLIELLRAIPEDCPRLATFDEDFTELAEAMDPTFSRRPRDYQRQFAGNIDDSFCVGLRIEPSRVRVYTHPLNSDMIICSPLGLRRRLERNGDASVSLSSIEVCLIDEAHVLLMQNWQHVMEVLGLLNKRPRDTTYGLSDLRRVYAWALAGQSGRHRQTIISSNVTNAVLLSTFRTFVNNSGRVSLHRREETGVLQQIMVPVRQHFLRFDPGSSVESCDDARFDFFTREVLPTKILPPVSRDVRTIIFVPSYFDYVRIRNYMIREHRDSFAAICEYTSLRQQRKSLGQFTDLERPLLLVTERFYFFRRYFVKHAEIIVFYSPPVFSSFYVSLVGRLVATSPNAFSLTLFCRYDSHELNRLVGTARARQLVEREAEAYSFVTN
Protein: mRNA export protein 33 (Q9USV4)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope. Involved in the export of mRNA from the nucleus to the cytoplasm. May play a role in mitotic spindle formation and/or function.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15116432, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Uncharacterized GTP-binding protein C9.07c
- GTP-binding protein 1
- Elongation factor 3
- mRNA export factor elf1
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein RACK1
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein uS3
- RWD domain-containing protein C1393.09c
Sequence:
MPPKKAAKGKGDPGKAAKKDPTKKAADATFGLKNKNRSTKVQAKIRQIEQNAAASGSKDAKRQEALRKRREEEKRAAEAAKAEVAALFNAIPKKQTPQNFLTRKEEVKESQKIDLYSDVRDQQTDLPLEKRPWINTDIVCKFFLEACETGKYGWLWQCPNGNMTCIYKHALPYGYVLSRDKKKDDTKEEISLEAFIEIERHRLGPNLTPVTEENFKKWSDGRRDRILKQAEERRSNRAVGRSNLSGREYFESNKDKTHEVVGDEEDWDFSALRRETEALAKAQDATAPIVSV
Protein: BAG family molecular chaperone regulator 7 (Bcl-2-associated athanogene 7) (Q9LVA0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Co-chaperone that regulates diverse cellular pathways, such as programmed cell death and stress responses. Necessary for the proper maintenance of the unfolded protein response (UPR) during heat and cold tolerance.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:20231441}.
Interaction partners:
- Probable WRKY transcription factor 29
- Heat shock 70 kDa protein BIP2
- BAG family molecular chaperone regulator 5, mitochondrial
- BAG family molecular chaperone regulator 4
- Bax inhibitor 1
- bZIP transcription factor 28
- BAG family molecular chaperone regulator 3
- NAC domain containing protein 103
- Bax inhibitor-1 family protein
- bZIP transcription factor 60
Sequence:
MTLFHRLDLIDPYTCTPLIVRETSIVEPSSLFLGFPSFIDEDIEDLFEFSSPNPLDLFETVTDLVKIKKSPSSCKYKVIRRRLEPEYPLKYLCDRVSDLESKFDRLVSPKSDRKYTLTKEIKGSGERKYKWEAEIQGPLERKYKLEAEIEGSGERKYRWTTEIKGGKKDEEGLKLAALKKEKAKAKAIAAAEAEKKKNKNKKKSYNWTTEVKSERENGEVSHTYIIKATTGGEKKKKHEEKEKKEKIETKSKKKEKTRVVVIEEEEEEDDESSEHGAIVLRKAFSRRNGAVRTKKGKNKEMPPEYAAVMIQRAFKAYLIRRSKSLRALRDLAIAKTKLKELRASFHNFSYRRLIARDGEERQKFSEKIIVLLLTVDAIEGVDVMVRGAKRSMVDELEAMLDVVDPQPQGKSLSMRRRTFDMPDSLIRKEIAEGVTQIVQMLETEEE
Protein: G protein-coupled receptor kinase (EC 2.7.11.-) (A9JRC5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MEIETMAANCALLKARDAGNAYRKGRSRKWKEILHFPHINQCKELENSIERDYYSLCVNQPIGKQLFKLFCATEPKLQHLIDLLEEMAKYEVTTDDLKKTSRDKLINKFKTSQSSMVREMVHKEMQNGNLNMENFISSCHSALHEYLSGAPFSEYQNSMYFDRFLQWKMVERRPVTQDNFREYRILGKGGFGEVCACQSRASGKMYACKKLVKKRVKRQGGEKMVLKEKQILERVNSRFVVSLAYTYETKDSLCLVLTVMDGGDLGFHIYKMGNQKLDKNRVQFYAAEVLCGLDHLHKHNVVYRDLKPENILLDYEGHIRISDLGLAEILPENKLVKGRVGTAGYMAPEVVAGTSYGVSVDWWGLGCLIYEMTAKKPPFRNHKEQISKKDLEQRILEKVELYDKMFDEETQNICQKLLAKNPKERLGCRSGQGAEVIKSH
Protein: Terminal nucleotidyltransferase 4B (Non-canonical poly(A) RNA polymerase PAPD5) (EC 2.7.7.19) (PAP-associated domain-containing protein 5) (Terminal guanylyltransferase) (EC 2.7.7.-) (Terminal uridylyltransferase 3) (TUTase 3) (Topoisomerase-related function protein 4-2) (TRF4-2) (Q8NDF8)
Organism: Homo sapiens (Human)
Function: Terminal nucleotidyltransferase that catalyzes preferentially the transfert of ATP and GTP on RNA 3' poly(A) tail creating a heterogeneous 3' poly(A) tail leading to mRNAs stabilization by protecting mRNAs from active deadenylation. Also functions as a catalytic subunit of a TRAMP-like complex which has a poly(A) RNA polymerase activity and is involved in a post-transcriptional quality control mechanism. Polyadenylation with short oligo(A) tails is required for the degradative activity of the exosome on several of its nuclear RNA substrates. Doesn't need a cofactor for polyadenylation activity (in vitro). Required for cytoplasmic polyadenylation of mRNAs involved in carbohydrate metabolism, including the glucose transporter SLC2A1/GLUT1. Plays a role in replication-dependent histone mRNA degradation, probably through terminal uridylation of mature histone mRNAs. May play a role in sister chromatid cohesion. Mediates 3' adenylation of the microRNA MIR21 followed by its 3'-to-5' trimming by the exoribonuclease PARN leading to degradation. Mediates 3' adenylation of H/ACA box snoRNAs (small nucleolar RNAs) followed by its 3'-to-5' trimming by the exoribonuclease PARN which enhances snoRNA stability and maturation.
Subcellular location: Nucleus {ECO:0000269|PubMed:18172165, ECO:0000269|PubMed:21788334}. Nucleus, nucleolus {ECO:0000269|PubMed:21855801, ECO:0000269|PubMed:23376078}. Cytoplasm {ECO:0000269|PubMed:18172165, ECO:0000269|PubMed:28383716}. Note=Predominantly expressed in the cytoplasm (PubMed:18172165).
Interaction partners:
- Zinc finger CCHC domain-containing protein 7
- Exosome RNA helicase MTR4
- Zinc finger CCHC domain-containing protein 8
- Exosome complex component 10
- Zinc finger CCHC domain-containing protein 14
- Poly
- Poly
- Poly
- Poly
- CCR4-NOT transcription complex subunit 9
Sequence:
MYRSGERLLGSHALPAEQRDFLPLETTNNNNNHHQPGAWARRAGSSASSPPSASSSPHPSAAVPAADPADSASGSSNKRKRDNKASGGRAAGGGRADGGGVVYSGTPWKRRNYNQGVVGLHEEISDFYEYMSPRPEEEKMRMEVVNRIESVIKELWPSADVQIFGSFKTGLYLPTSDIDLVVFGKWENLPLWTLEEALRKHKVADEDSVKVLDKATVPIIKLTDSFTEVKVDISFNVQNGVRAADLIKDFTKKYPVLPYLVLVLKQFLLQRDLNEVFTGGIGSYSLFLMAVSFLQLHPREDACIPNTNYGVLLIEFFELYGRHFNYLKTGIRIKDGGSYVAKDEVQKNMLDGYRPSMLYIEDPLQPGNDVGRSSYGAMQVKQAFDYAYVVLSHAVSPIAKYYPNNETESILGRIIRVTDEVATYRDWISKQWGLKNRPEPSCNGPVSSSSATQSSSSDVDSDATPCKTPKQLLCRPSTGNRVGSQDVSLESSQAVGKMQSTQTTNTSNSTNKSQHGSARLFRSSSKGFQGTTQTSHGSLMTNKQHQGKSNNQYYHGKKRKHKRDAPLSDLCR
Protein: Expansin (O49194)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Subcellular location: Secreted, cell wall {ECO:0000256|RuleBase:RU365023}. Membrane {ECO:0000256|RuleBase:RU365023}; Peripheral membrane protein {ECO:0000256|RuleBase:RU365023}.
Interaction partners:
Sequence:
MATKTMMLQIFPLFFFLFSVCNSIFLGANGDDNGGWQTAHATFYGGADATGTMGGACGYGNLYSQGYGTSTAALSTALFNNGLSCGACYELRCNNDPQWCISRTITVTATNFCPPNYALSSDNGGWCNPPREHFDLAEPRFLRIAEYRAGIVPVMFRRVSCVKKGGIRYTMNGHSYFNMVLITKLGGAGDITSVSIKGSRTGWLPMSRNWGQNWQSNAYLNGQSLSFKVTASDGRTITAYNVVPAGWQFGQTFEGGQF
Protein: DNA-directed RNA polymerase (EC 2.7.7.6) (P07659)
Organism: Enterobacteria phage T3 (Bacteriophage T3)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Interaction partners:
Sequence:
MNIIENIEKNDFSEIELAAIPFNTLADHYGSALAKEQLALEHESYELGERRFLKMLERQAKAGEIADNAAAKPLLATLLPKLTTRIVEWLEEYASKKGRKPSAYAPLQLLKPEASAFITLKVILASLTSTNMTTIQAAAGMLGKAIEDEARFGRIRDLEAKHFKKHVEEQLNKRHGQVYKKAFMQVVEADMIGRGLLGGEAWSSWDKETTMHVGIRLIEMLIESTGLVELQRHNAGNAGSDHEALQLAQEYVDVLAKRAGALAGISPMFQPCVVPPKPWVAITGGGYWANGRRPLALVRTHSKKGLMRYEDVYMPEVYKAVNLAQNTAWKINKKVLAVVNEIVNWKNCPVADIPSLERQELPPKPDDIDTNEAALKEWKKAAAGIYRLDKARVSRRISLEFMLEQANKFASKKAIWFPYNMDWRGRVYAVPMFNPQGNDMTKGLLTLAKGKPIGEEGFYWLKIHGANCAGVDKVPFPERIAFIEKHVDDILACAKDPINNTWWAEQDSPFCFLAFCFEYAGVTHHGLSYNCSLPLAFDGSCSGIQHFSAMLRDEVGGRAVNLLPSETVQDIYGIVAQKVNEILKQDAINGTPNEMITVTDKDTGEISEKLKLGTSTLAQQWLAYGVTRSVTKRSVMTLAYGSKEFGFRQQVLDDTIQPAIDSGKGLMFTQPNQAAGYMAKLIWDAVSVTVVAAVEAMNWLKSAAKLLAAEVKDKKTKEILRHRCAVHWTTPDGFPVWQEYRKPLQKRLDMIFLGQFRLQPTINTLKDSGIDAHKQESGIAPNFVHSQDGSHLRMTVVYAHEKYGIESFALIHDSFGTIPADAGKLFKAVRETMVITYENNDVLADFYSQFADQLHETQLDKMPPLPKKGNLNLQDILKSDFAFA
Protein: Activating transcription factor 7-interacting protein 1 (ATF-interacting protein) (ATF-IP) (ATF7-interacting protein) (ATFa-associated modulator) (hAM) (MBD1-containing chromatin-associated factor 1) (P621) (Q6VMQ6)
Organism: Homo sapiens (Human)
Function: Recruiter that couples transcriptional factors to general transcription apparatus and thereby modulates transcription regulation and chromatin formation. Can both act as an activator or a repressor depending on the context. Required for HUSH-mediated heterochromatin formation and gene silencing. Mediates MBD1-dependent transcriptional repression, probably by recruiting complexes containing SETDB1. Stabilizes SETDB1, is required to stimulate histone methyltransferase activity of SETDB1 and facilitates the conversion of dimethylated to trimethylated H3 'Lys-9' (H3K9me3). The complex formed with MBD1 and SETDB1 represses transcription and couples DNA methylation and histone H3 'Lys-9' trimethylation (H3K9me3). Facilitates telomerase TERT and TERC gene expression by SP1 in cancer cells.
Subcellular location: Nucleus {ECO:0000269|PubMed:19106100, ECO:0000269|PubMed:27732843}.
Interaction partners:
- Histone-lysine N-methyltransferase SETDB1
- Small ubiquitin-related modifier 2
- ARL14 effector protein
- Methyl-CpG-binding domain protein 1
- Histone H3.2
- Histone H3.1
- Cyclic AMP-dependent transcription factor ATF-7
- Transcription factor Sp1
- Doublesex- and mab-3-related transcription factor 1
- Activating transcription factor 7-interacting protein 2
Sequence:
MDSLEEPQKKVFKARKTMRVSDRQQLEAVYKVKEELLKTDVKLLNGNHENGDLDPTSPLENMDYIKDKEEVNGIEEICFDPEGSKAEWKETPCILSVNVKNKQDDDLNCEPLSPHNITPEPVSKLPAEPVSGDPAPGDLDAGDPASGVLASGDSTSGDPTSSEPSSSDAASGDATSGDAPSGDVSPGDATSGDATADDLSSGDPTSSDPIPGEPVPVEPISGDCAADDIASSEITSVDLASGAPASTDPASDDLASGDLSSSELASDDLATGELASDELTSESTFDRTFEPKSVPVCEPVPEIDNIEPSSNKDDDFLEKNGADEKLEQIQSKDSLDEKNKADNNIDANEETLETDDTTICSDRPPENEKKVEEDIITELALGEDAISSSMEIDQGEKNEDETSADLVETINENVIEDNKSENILENTDSMETDEIIPILEKLAPSEDELTCFSKTSLLPIDETNPDLEEKMESSFGSPSKQESSESLPKEAFLVLSDEEDISGEKDESEVISQNETCSPAEVESNEKDNKPEEEEQVIHEDDERPSEKNEFSRRKRSKSEDMDNVQSKRRRYMEEEYEAEFQVKITAKGDINQKLQKVIQWLLEEKLCALQCAVFDKTLAELKTRVEKIECNKRHKTVLTELQAKIARLTKRFEAAKEDLKKRHEHPPNPPVSPGKTVNDVNSNNNMSYRNAGTVRQMLESKRNVSESAPPSFQTPVNTVSSTNLVTPPAVVSSQPKLQTPVTSGSLTATSVLPAPNTATVVATTQVPSGNPQPTISLQPLPVILHVPVAVSSQPQLLQSHPGTLVTNQPSGNVEFISVQSPPTVSGLTKNPVSLPSLPNPTKPNNVPSVPSPSIQRNPTASAAPLGTTLAVQAVPTAHSIVQATRTSLPTVGPSGLYSPSTNRGPIQMKIPISAFSTSSAAEQNSNTTPRIENQTNKTIDASVSKKAADSTSQCGKATGSDSSGVIDLTMDDEESGASQDPKKLNHTPVSTMSSSQPVSRPLQPIQPAPPLQPSGVPTSGPSQTTIHLLPTAPTTVNVTHRPVTQVTTRLPVPRAPANHQVVYTTLPAPPAQAPLRGTVMQAPAVRQVNPQNSVTVRVPQTTTYVVNNGLTLGSTGPQLTVHHRPPQVHTEPPRPVHPAPLPEAPQPQRLPPEAASTSLPQKPHLKLARVQSQNGIVLSWSVLEVDRSCATVDSYHLYAYHEEPSATVPSQWKKIGEVKALPLPMACTLTQFVSGSKYYFAVRAKDIYGRFGPFCDPQSTDVISSTQSS
Protein: A disintegrin and metalloproteinase with thrombospondin motifs 5 (ADAM-TS 5) (ADAM-TS5) (ADAMTS-5) (EC 3.4.24.-) (ADMP-2) (Aggrecanase-2) (Implantin) (Q9R001)
Organism: Mus musculus (Mouse)
Function: Metalloproteinase that plays an important role in connective tissue organization, development, inflammation and cell migration. Extracellular matrix (ECM) degrading enzyme that shows proteolytic activity toward the hyalectan group of chondroitin sulfate proteoglycans (CSPGs) including ACAN, VCAN, BCAN and NCAN. Cleavage within the hyalectans occurs at Glu-Xaa recognition motifs. Plays a role in embryonic development, including limb and cardiac morphogenesis, and skeletal muscle development through its VCAN remodeling properties. Cleaves VCAN in the pericellular matrix surrounding myoblasts, facilitating myoblast contact and fusion which is required for skeletal muscle development and regeneration. Participates in the development of brown adipose tissue and browning of white adipose tissue. Plays an important role for T-lymphocyte migration from draining lymph nodes following viral infection.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q9UNA0}.
Interaction partners:
- Brevican core protein
- Aggrecan core protein
- Collagenase 3
- Metalloproteinase inhibitor 3
- Stromelysin-1
- Collagen alpha-1
- Syndecan-4
- Metalloproteinase inhibitor 1
- Interleukin-1 beta
Sequence:
MRLEWAPLLLLLLLLSASCLSLAADSPAAAPAQDKTRQPQAAAAAAEPDQPQGEETRERGHLQPLAGQRRSGGLVQNIDQLYSGGGKVGYLVYAGGRRFLLDLERDDTVGAAGSIVTAGGGLSASSGHRGHCFYRGTVDGSPRSLAVFDLCGGLDGFFAVKHARYTLKPLLRGSWAEYERIYGDGSSRILHVYNREGFSFEALPPRASCETPASPSGPQESPSVHSRSRRRSALAPQLLDHSAFSPSGNAGPQTWWRRRRRSISRARQVELLLVADSSMARMYGRGLQHYLLTLASIANRLYSHASIENHIRLAVVKVVVLTDKDTSLEVSKNAATTLKNFCKWQHQHNQLGDDHEEHYDAAILFTREDLCGHHSCDTLGMADVGTICSPERSCAVIEDDGLHAAFTVAHEIGHLLGLSHDDSKFCEENFGTTEDKRLMSSILTSIDASKPWSKCTSATITEFLDDGHGNCLLDLPRKQILGPEELPGQTYDATQQCNLTFGPEYSVCPGMDVCARLWCAVVRQGQMVCLTKKLPAVEGTPCGKGRVCLQGKCVDKTKKKYYSTSSHGNWGSWGPWGQCSRSCGGGVQFAYRHCNNPAPRNSGRYCTGKRAIYRSCSVTPCPPNGKSFRHEQCEAKNGYQSDAKGVKTFVEWVPKYAGVLPADVCKLTCRAKGTGYYVVFSPKVTDGTECRPYSNSVCVRGRCVRTGCDGIIGSKLQYDKCGVCGGDNSSCTKIIGTFNKKSKGYTDVVRIPEGATHIKVRQFKAKDQTRFTAYLALKKKTGEYLINGKYMISTSETIIDINGTVMNYSGWSHRDDFLHGMGYSATKEILIVQILATDPTKALDVRYSFFVPKKTTQKVNSVISHGSNKVGPHSTQLQWVTGPWLACSRTCDTGWHTRTVQCQDGNRKLAKGCLLSQRPSAFKQCLLKKC
Protein: ATP-sensitive inward rectifier potassium channel 1 (ATP-regulated potassium channel ROM-K) (Inward rectifier K(+) channel Kir1.1) (KAB-1) (Potassium channel, inwardly rectifying subfamily J member 1) (P35560)
Organism: Rattus norvegicus (Rat)
Function: In the kidney, probably plays a major role in potassium homeostasis. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. This channel is activated by internal ATP and can be blocked by external barium.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P48048}; Multi-pass membrane protein {ECO:0000255}. Note=Phosphorylation at Ser-44 by SGK1 is necessary for its expression at the cell membrane. {ECO:0000250|UniProtKB:P48048}.
Interaction partners:
- Serine/threonine-protein kinase Sgk1
- Solute carrier family 12 member 1-chloride cotransporter 1)
- Solute carrier family 12 member 3
- Serine/threonine-protein kinase WNK4
- Chloride channel protein ClC-Kb
- Barttin
- Epithelial sodium channel subunit alpha
- Cystic fibrosis transmembrane conductance regulator
- Serine/threonine-protein kinase WNK1
- Claudin-16
Sequence:
MGASERSVFRVLIRALTERMFKHLRRWFITHIFGRSRQRARLVSKEGRCNIEFGNVDAQSRFIFFVDIWTTVLDLKWRYKMTVFITAFLGSWFLFGLLWYVVAYVHKDLPEFYPPDNRTPCVENINGMTSAFLFSLETQVTIGYGFRFVTEQCATAIFLLIFQSILGVIINSFMCGAILAKISRPKKRAKTITFSKNAVISKRGGKLCLLIRVANLRKSLLIGSHIYGKLLKTTITPEGETIILDQTNINFVVDAGNENLFFISPLTIYHIIDHNSPFFHMAAETLSQQDFELVVFLDGTVESTSATCQVRTSYVPEEVLWGYRFVPIVSKTKEGKYRVDFHNFGKTVEVETPHCAMCLYNEKDARARMKRGYDNPNFVLSEVDETDDTQM
Protein: Periplasmic protein TorT (Q87ID2)
Organism: Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)
Subcellular location: Cell envelope {ECO:0000256|ARBA:ARBA00004196}.
Interaction partners:
Sequence:
MVINQRSIRTIFKHSVLAASLCASLPSVAAEKICAIYPHLKDSYWLSVNYGMVSEAEKQGVNLRVLEAGGYPNKSRQEQQLALCTQWGANAIILGTVDPHAYEHNLKSWVGNTPVFATVNQLDLDEEQSTLLKGEVGVDWYWMGYEAGKYLAERHPKGSGKTNIALLLGPRTRGGTKPVTTGFYEAIKNSDIHIVDSFWADNDKELQRNLVQRVIDMGNIDYIVGSAVAIEAAISELRSADKTHDIGLVSVYLSHGVYRGLLRNKVLFAPTDKMVQQGRLSVMQAAHYLRHQPYEKQASPIIKPLTPKTLHDDTIEESLSPSEYRPTFSIKAVD
Protein: DH domain-containing protein (Q7JNG4)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MPCANLMPRCKQEFRRIFANSSKERAAAANSSSSNNNSPATRQSTSTSSPVTANGHTTESSTSAPIGVLSSGEPTSSNSIPSSSTPTHTVPSSVPATVIPIVVAEDEKAEDCLPPPMENITINNSIDEKDMNEDSVAASDAVEPEVALPAKVEKTPEETARFKRSYVLMELVETEQDYVKDLTSVVEGYIGNLNKMDLPADLVGKDKIIFANIVNILEFHKTNFLKEIEKCSENYEAAGAAFVKYERRLHTLYVTYCQNKPKSDYLLAQDDFEAFFADTKAKLGHKVALCDLLIKPVQRIMKYQLLLKDILKFTERAKDKTDTLKKALQVMHVVPKACDDMMQVGRLQNFDKSLSAQGKLIHQGTLQISESIAGNVQKPKDRRIFLFEQSAIIADHIPPKKEFGNPTYIFKSQFMVNKMVFEPNVPDDPLRFVIKSSDPTQPTSFIANAQSQEEKDEWNRKMSELLDQQKRLLAALVDPRRYNDMSSGMGDLSLGAPGGDRRGAPSSANRSAASSSKKPAESPKKEGKSKSSLFSFGKKPAKSPTSPPPVGK
Protein: SIN3 transcription regulator family member A (H3BQL7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKRRLDDQESPVYAAQQRRIPGSTEAFPHQHRVLAPAPPVYEAVSETMQSATGIQYSVTPSYQVSAMPQSSGSHGPAIAAVHSSHHHPTAVQPHGGQVVQSHAHPAPPVAPVQGQQQFQRLKVVFSSFSWVKKFIFSRKYWLQLVGCGGTTSNLRY
Protein: Isoaspartyl peptidase/L-asparaginase 1 (EC 3.4.19.5) (L-asparagine amidohydrolase 1) [Cleaved into: Isoaspartyl peptidase/L-asparaginase 1 subunit alpha; Isoaspartyl peptidase/L-asparaginase 1 subunit beta] (P50287)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts in asparagine catabolism but also in the final steps of protein and degradation via hydrolysis of a range of isoaspartyl dipeptides. The affinity for Asn and at least 4 isoaspartyl dipeptides (L-beta-Asp-Ala, L-beta-Asp-Gly, L-beta-Asp-Leu, L-beta-Asp-Phe) is quite low, KM being greater than 4.0 mM. The enzyme is inactive on alpha-aspartyl dipeptides.
Interaction partners:
- Asparagine synthetase 2
- Asparagine synthetase 1
- Asparagine synthetase 3
- Aspartate aminotransferase, cytoplasmic isozyme 1
- Aspartate aminotransferase 3, chloroplastic
- Aspartate aminotransferase, cytoplasmic isozyme 2
- Aspartate carbamoyltransferase, chloroplastic
- Aspartate aminotransferase, mitochondrial
- Aspartate aminotransferase, chloroplastic
- Adenylosuccinate synthetase, chloroplastic
Sequence:
MVGWAIALHGGAGDIPIDLPDERRIPRESALRHCLDLGISALKSGKPPLDVAELVVRELENHPDFNAGKGSVLTAQGTVEMEASIMDGKTKRCGAVSGLTTVVNPISLARLVMEKTPHIYLAFDAAEAFARAHGVETVDSSHFITPENIARLKQAKEFNRVQLDYTVPSPKVPDNCGDSQIGTVGCVAVDSAGNLASATSTGGYVNKMVGRIGDTPVIGAGTYANHLCAISATGKGEDIIRGTVARDVAALMEYKGLSLTEAAAYVVDQSVPRGSCGLVAVSANGEVTMPFNTTGMFRACASEDGYSEIAIWPNN
Protein: Transcriptional activator SPT7 (P35177)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Functions as component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and SLIK. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA an altered form of SAGA, may be involved in positive transcriptional regulation. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus. SPT7 is transcriptional activator of TY elements and other genes.
Subcellular location: Nucleus.
Interaction partners:
- Histone acetyltransferase GCN5
- SAGA complex subunit NGG1
- SAGA complex subunit SPT20
- SAGA complex subunit ADA2
- SAGA complex/NuA4 acetyltransferase complex subunit TRA1
- SAGA complex subunit SGF11
- Ubiquitin carboxyl-terminal hydrolase 8
- SAGA complex subunit SPT3
- SAGA complex/transcription factor TFIID complex subunit TAF9
- SAGA complex/transcription factor TFIID complex subunit TAF10
Sequence:
MTERIPIKNYQRTNAKALLKLTEKLFNKNFFDLYLTSQQLVVLEYLLSISSEEDKLKAWDYFLKGNIALNVEKSFPLTQEEEHHGAVSPAVDTRSDDVSSQTIKDNNNTNTNTSISNENHVENEIEDKGDNAIANEDNFVNNDESDNVEEDLFKLDLEDLKQQISGTRFIGNLSLKIRYVLWQCAIDYIYCDRNEFGDENDTEYTLLDVEEKEEEEIGKNEKPQNKEGISKFAEDEDYDDEDENYDEDSTDVKNVDDPPKNLDSISSSNIEIDDERRLVLNISISKETLSKLKTNNVEEIMGNWNKIYHSFEYDKETMIKRLKLEESDKMIEKGKKKRSRSDLEAATDEQDRENTNDEPDTNQKLPTPEGSTFSDTGNKRPKQSNLDLTVNLGIENLSLKHLLSSIQQKKSQLGISDYELKHLIMDVRKNRSKWTSDERIGQEELYEACEKVVLELRNYTEHSTPFLNKVSKREAPNYHQIIKKSMDLNTVLKKLKSFQYDSKQEFVDDIMLIWKNCLTYNSDPSHFLRGHAIAMQKKSLQLIRMIPNITIRNRADLEKEIEDMEKDKDYELDEEEEVAGSGRKGLNMGAHMLAKENGKVSEKDSSKTVKDEAPTNDDKLTSVIPEGEKEKDKTASSTVTVHENVNKNEIKENGKNEEQDMVEESSKTEDSSKDADAAKKDTEDGLQDKTAENKEAGENNEEEEDDDDEDEDEDMVDSQSYLLEKDDDRDDLEISVWKTVTAKVRAEICLKRTEYFKNGKLNSDSEAFLKNPQRMKRFDQLFLEYKEQKALESYRQKIEQNSIMKNGFGTVLKQEDDDQLQFHNDHSLNGNEAFEKQPNDIELDDTRFLQEYDISNAIPDIVYEGVNTKTLDKMEDASVDRMLQNGINKQSRFLANKDLGLTPKMNQNITLIQQIRHICHKISLIRMLQSPLSAQNSRSNPNAFLNNHIYNYTIIDDSLDIDPVSQLPTHDYKNNRELIWKFMHKNISKVAMANGFETAHPSAINMLTEIAGDYLSNLIKTLKLHHETNSLNRGTNVEMLQTTLLENGINRPDDLFSYVESEFGKKTKKLQDIKQKLESFLRALLRPTLQELSERNFEDESQSFFTGDFASELTGEDFFGFRELGLEKEFGVLSSSVPLQLLTTQFQTVDGETKVQAKKIQPEESDSIVYKKITKGMLDAGSFWNTLLPLLQKDYERSKAYIAKQSKSSANDKTSMTSTEDNSFALLEEDQFVSKKTATKARLPPTGKISTTYKKKPIASAFILPEEDLENDVKADPTTTVNAKVGAENDGDSSLFLRTPQPLDPLDMDDAFDDTNMGSNSSFSLSLPRLNQ