wanglab/gogpt-training-data huggingface dataset:
Protein: Fas-binding factor 1 (FBF-1) (Protein albatross) (Q8TES7)
Organism: Homo sapiens (Human)
Function: Keratin-binding protein required for epithelial cell polarization. Involved in apical junction complex (AJC) assembly via its interaction with PARD3. Required for ciliogenesis.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Cytoplasm, cytoskeleton, spindle pole. Cell junction. Note=Localizes specifically to the distal appendage region of the centriole, which anchors the mother centriole to the plasma membrane. Localizes to the apical junction complex (AJC) in epithelial cells.
Interaction partners:
- Sodium channel and clathrin linker 1
- Centrosomal protein of 83 kDa
- Centrosomal protein of 164 kDa
- Centrosomal protein of 89 kDa
- TRAF3-interacting protein 1
- 5'-3' exoribonuclease 2
- Decapping and exoribonuclease protein
- DNA-directed RNA polymerase II subunit RPB1
- Ninein
- DNA-directed RNA polymerase II subunit RPB2
Sequence:
MAPKTKKGCKVTLPEKPVKLASHTRDTTGVSQMFPSSKARTKSLLGDDVFSTMAGLEEADAEVSGISEADPQALLQAMKDLDGMDADILGLKKSNSAPSKKAAKDPGKGELPNHPKPAGGAIPTKKSLPSPSSSGHQNRRFSSEDLEDPLRGLLSYDEGGITKQPPVTQSKTASDKSPSTVRDQGPSIPLTPGDTPIRKKEELLFDDGDDIMATLGFGDSPKAEKRQIGDQEGPRPARSTLDELLGRGMATKLLARPGTGEHREFKLDKKYQRPQDSEDMWGDEDFTFGAYQPTVVSSEGRQSRRQSVSRFFADSGADPKGEPGSKQSPPMASSPIQPRKGGADWLGLKDEDLDLFPASPTREAHRESSVPVTPSVPPPASQHSTPAGLPPSRAKPPTEGAGSPAKASQASKLRASKEEKEDWLSHALSRKKSQGLAREQHAGTSEGLHLAGTAGHPPSGSQPLTSTQGLEHAAAGGSSGTTARERPCVRPGVSGSPVTQNHAASALPTGSPKRGTAPGDLSATEPATCFPSTQKPTEPSVPVQPLLPESLARSLLPSTEYQKQLLAAQVQLQCSPAELQAELLHSQARLAELEAQVRKLELERAQHELLLGSLQQQHQADLELIESAHRSRIKVLETSYQQREERLRRENEELSARYLSQCQEAEQARAELTAQHQRRLAAIAQEKDQEMERLRELQRASILDMRRDHEEQLQRLKLLKDREVDAATSATSHTRSLNSIIHQMEKFSSSLHELSSRVEASHLTTSQERELGIRQRDEQLRALQERLGQQQRDMEEERSRQQEVIGKMEARLNEQSRLLEQERWRVTAEQSKAESMQRALEEQRKVTAQQMAMERAELERAKSALLEEQKSVMLKCGEERRRLAAEWAEFSAQQKLSKERAEREAERALQVDTQREGTLISLAKQAELKIRASELRAEEKQLAAERAALEQERQELRLEKERINATALRVKLRAEEVESMSKVASEKYEEGERALREAQQVQAEQQARLQAVQQQQERLRKQEQHMHQEHLSLAQQRLQLDRARQDLPSSLVGLFPRAQGPAASSQSALMPPAPTTRWCSQPPTGLDPSPLHLHARLALLRHMAEQDRDFLENEQFFLETLKKGSYNLTSHSA
Protein: ATP-dependent 6-phosphofructokinase 4, chloroplastic (ATP-PFK 4) (Phosphofructokinase 4) (EC 2.7.1.11) (Phosphohexokinase 4) (Q9FKG3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:17485088}.
Interaction partners:
- Glucose-6-phosphate isomerase 1, chloroplastic
- Glucose-6-phosphate isomerase, cytosolic
- Aldolase-type TIM barrel family protein
- transaldolase
- Transketolase-1, chloroplastic
- Transketolase-2, chloroplastic
- Hexokinase-like 1 protein
- Hexokinase-4
- Mannose-6-phosphate isomerase 1
- Mannose-6-phosphate isomerase 2
Sequence:
MEASISFLGSTKPNISLFNPSSNVLPRRDFPLPALKLKKVSVLPRILHQKRLIRAQCSDGFKPEEDDGFVLEDVPHLTKFLPDLPSYPNPLKESQAYAIVKRTFVSSEDVVAQNIVVQKGSKRGVHFRRAGPRERVYFRSDEVKACIVTCGGLCPGINTVIREIVCGLNNMYGVNNILGIQGGYRGFYSKNTMNLTPKVVNDIHKRGGTFLQTSRGGHDTAKIVDNIQDRGINQVYIIGGGGTQKGAEKIYEEVERRGLQVAVSGIPKTIDNDIAVIDKSFGFDTAVEEAQRAINAAHVEVESVENGVGIVKLMGRYSGFIAMIATLANRDVDCCLIPESPFFLEGKGGLFEFIEERLKENRHMVIVIAEGAGQDYVAQSMRASETKDASGNRLLLDVGLWLTQQIKDHFTNVRKMMINMKYIDPTYMIRAIPSNASDNVYCTLLAQSAVHGAMAGYSGFTVGPVNSRHAYIPISQVTEVTNTVKLTDRMWARLLASTNQPSFLTGEGALQNVIDMETQEKIDNMKISSI
Protein: Aspartyl beta-hydroxylase, isoform G (EC 1.14.11.16) (A4UZJ1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSGDVQPRKRKDKRRKRDDDESSHGVHITKMGNEDLHLHVHHDHGTGGHWCAKIIFFALMAVLLGLVGLIIMENRGLEDLDTPLSESRFSKVFDGWVDEHRDEHDGHDVQEPSGEALDDHDEHDDHDDHEDEDEEPLTEELEEELEEEEEPTEEDEPAADEEYEEDEDEENNAGENITAEDAEEEEEEEDNDDEGTVEATVEATTEATTEATGEYEAEEDDEDEAAADDDAVESTEAPLSKAEEQEDDEDEDEEEQEIEESVEPERSQYAAQSAPAKDNNDDDDDDDQDKNDADDGDDDEFESLAQQFENDPEDTVPAKAVESEEQDQDQADEEEPKEEGSSWLASLAVKFGVGVALALVSRLVLIRKSPNTTEDEPAPETIFRRRLTIATAEDHIPDDVEELPPLDDEYSEEEIEIEEEIEVEISDIEEEEEEVRHDNDDNVASMASYVPETFEQLSAMYKYAQEPTKDAKPEQKEKEPEKPVGHSDIYVEYEDGAIEDYEHDGVSDEEITDEEDEISDVDDADLMNRLEAKYGRLPVKEFESDPDSDDPSWTRNY
Protein: Cytochrome P450 93G1 (EC 1.14.19.76) (Flavone synthase II) (OsFNSII) (Q0JFI2)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Functions as flavone synthase II (FNSII) that catalyzes the direct conversion of flavanones to flavones. In vitro, can convert naringenin and eriodictyol to apigenin and luteolin, respectively. Acts as a key branch point enzyme that channels flavanones to the biosynthesis of soluble tricin O-linked conjugates.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Flavanone 4-reductase
- Flavanone 3-dioxygenase 1
- Chalcone--flavanone isomerase
- Flavonoid 3'-monooxygenase CYP75B3
- Flavonoid 3'-monooxygenase CYP75B4
- Chalcone-flavonone isomerase family protein
- Chalcone-flavonone isomerase family protein
- Probable 5'-adenylylsulfate reductase 1, chloroplastic
- Naringenin 7-O-methyltransferase
- Os03g0367101 protein
Sequence:
MASLMEVQVPLLGMGTTMGALALALVVVVVVHVAVNAFGRRRLPPSPASLPVIGHLHLLRPPVHRTFHELAARLGPLMHVRLGSTHCVVASSAEVAAELIRSHEAKISERPLTAVARQFAYESAGFAFAPYSPHWRFMKRLCMSELLGPRTVEQLRPVRRAGLVSLLRHVLSQPEAEAVDLTRELIRMSNTSIIRMAASTVPSSVTEEAQELVKVVAELVGAFNADDYIALCRGWDLQGLGRRAADVHKRFDALLEEMIRHKEEARMRKKTDTDVGSKDLLDILLDKAEDGAAEVKLTRDNIKAFIIDVVTAGSDTSAAMVEWMVAELMNHPEALRKVREEIEAVVGRDRIAGEGDLPRLPYLQAAYKETLRLRPAAPIAHRQSTEEIQIRGFRVPAQTAVFINVWAIGRDPAYWEEPLEFRPERFLAGGGGEGVEPRGQHFQFMPFGSGRRGCPGMGLALQSVPAVVAALLQCFDWQCMDNKLIDMEEADGLVCARKHRLLLHAHPRLHPFPPLL
Protein: Tyramine receptor Ser-2 (O02213)
Organism: Caenorhabditis elegans
Function: G-protein coupled receptor for tyramine, a known neurotransmitter and neuromodulator and direct precursor of octopamine. The rank order of potency is tyramine > octopamine > dopamine > serotonin > epinephrine = norepinephrine.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Tyramine receptor tyra-2
- Ligand-Gated ion Channel
- Tyramine beta-hydroxylase
- Guanine nucleotide-binding protein subunit beta-2
- Guanine nucleotide-binding protein subunit beta-1
- Tyrosine decarboxylase
- Serotonin-gated chloride channel mod-1
Sequence:
MFRNYTDSVQEMVLRAIDSIRDSVINASSAVSTTTLPPLDIPMTSMKPPSIIPTVELVLGTITYLVIIAMTVVGNTLVVVAVFSYRPLKKVQNYFLVSLAASDLAVAIFVMPLHVVTFLAGGKWLLGVTVCQFFTTADILLCTSSILNLCAIALDRYWAIHNPINYAQKRTTKFVCIVIVIVWILSMLISVPPIIGWNNWQENMMEDSCGLSTEKAFVVFSAAGSFFLPLLVMVVVYVKIFISARQRIRTNRGRSALMRIQNAEGDDDYRKMSIKRASVESARTSSRVGEKTPLVIADGQTTVTTLAAHSTDGGSLPKDETTKHMKYHNNGSCKVKVKDVKEDEGNPNPTAVLRKREKISVAKEKRAAKTIAVIIFVFSFCWLPFFVAYVIRPFCETCKLHAKVEQAFTWLGYINSSLNPFLYGILNLEFRRAFKKILCPKAVLEQRRRRMSAQP
Protein: Four and a half LIM domains protein 1 (FHL-1) (KyoT) (RBP-associated molecule 14-1) (RAM14-1) (Skeletal muscle LIM-protein 1) (SLIM) (SLIM-1) (P97447)
Organism: Mus musculus (Mouse)
Function: May have an involvement in muscle development or hypertrophy. Isoform 2 binds to RBP-J and plays a negative regulatory role in the RBP-J-mediated transcription in mammalian systems.
Subcellular location: [Isoform 1]: Cytoplasm.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus.
Interaction partners:
- Recombining binding protein suppressor of hairless
- Titin
Sequence:
MSEKFDCHYCRDPLQGKKYVQKDGRHCCLKCFDKFCANTCVDCRKPISADAKEVHYKNRYWHDNCFRCAKCLHPLASETFVSKDGKILCNKCATREDSPRCKGCFKAIVAGDQNVEYKGTVWHKDCFTCSNCKQVIGTGSFFPKGEDFYCVTCHETKFAKHCVKCNKAITSGGITYQDQPWHAECFVCVTCSKKLAGQRFTAVEDQYYCVDCYKNFVAKKCAGCKNPITGFGKGSSVVAYEGQSWHDYCFHCKKCSVNLANKRFVFHNEQVYCPDCAKKL
Protein: Uncharacterized protein (Q580E3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTCRSEETNWGLLFDIALSHGESLRRQRLTYVGFMTLLRSAGVVGPVTGIYQVLLGALWQHHGLQRSCNEGGKGGETKNALDLTMDIDGFITIMNVVCIRCYQAQRFSEMLEDDHPISEAVTLCAEEQGKIHSSVTYTMRRFFKPFISRSIVLKRMVVSLDSRKNSWTPYANRLITHILAASADSIVFPLFDRYAECGRIYRPSFEGMVDDIFPHFSPSQRNAALSVFTYDGFTGIHKLMKYVHPDVDKETRAALELHSFAEALLMLAIVAFSNESQHKHHRPFTAKVWAAFEDYYCKFLGVPMVSDPIKDNKFASITPSANLVFPAEVPLNKLSSFLISGWNLTVDDWPCDTPDPGKGYPPRILKFPEDGFDDIPLMDKQESAAKAPTSTTGMAAKLFEEELIRPTPAEYSLPIYGVQRCTVYVDEQRANAFQRAPNIVEVVIPKSMWNISIDGTKVEFVTYGDEGKLLLRPNKDVTISIRDVKGSTTFETKSVPLLESPFEQVILPPQMEVLRTAFSHHAANDLLPVERFDDACAELCIITSGTKDHCFLFAKSKLEGSEERIPLKGAETLESAQGISFSEFVSALATVLLRRHEARNTLPDIPYLLAVGSSRMKKSLPPLAEWKGENSGNPAQWLPLKLTQPHNARIDVPYDNALRKKSSFLRRYSGTEGLLKSLGKDHHMLRPLPAFPVEVKTVDVVSQYDDDEKGLFDKVAKTSSSLQESFLKEEMVVSRKGWTLE
Protein: Homeobox protein Hox-C11 (Homeobox protein Hox-3H) (O43248)
Organism: Homo sapiens (Human)
Function: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Binds to a promoter element of the lactase-phlorizin hydrolase gene.
Subcellular location: Nucleus.
Interaction partners:
- Homeobox protein Hox-C10
- T-box transcription factor TBX4
- T-box transcription factor TBX5
Sequence:
MFNSVNLGNFCSPSRKERGADFGERGSCASNLYLPSCTYYMPEFSTVSSFLPQAPSRQISYPYSAQVPPVREVSYGLEPSGKWHHRNSYSSCYAAADELMHRECLPPSTVTEILMKNEGSYGGHHHPSAPHATPAGFYSSVNKNSVLPQAFDRFFDNAYCGGGDPPAEPPCSGKGEAKGEPEAPPASGLASRAEAGAEAEAEEENTNPSSSGSAHSVAKEPAKGAAPNAPRTRKKRCPYSKFQIRELEREFFFNVYINKEKRLQLSRMLNLTDRQVKIWFQNRRMKEKKLSRDRLQYFSGNPLL
Protein: Proteasome subunit beta type-1 (EC 3.4.25.1) (Macropain subunit PRE3) (Multicatalytic endopeptidase complex subunit PRE3) (Proteasome component PRE3) (Proteinase YSCE subunit PRE3) (P38624)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity. PRE3 and PRE4 are necessary for the peptidyl-glutamyl-peptide-hydrolyzing activity.
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- Proteasome subunit beta type-6
- 26S proteasome regulatory subunit RPN6
- 26S proteasome regulatory subunit RPN12
- 26S proteasome regulatory subunit RPN1
- 26S proteasome regulatory subunit RPN10
- Proteasome subunit alpha type-3
- Ubiquitin carboxyl-terminal hydrolase RPN11
- 26S proteasome subunit RPT4
- Proteasome subunit alpha type-4
- 26S proteasome regulatory subunit RPN8
Sequence:
MNGIQVDINRLKKGEVSLGTSIMAVTFKDGVILGADSRTTTGAYIANRVTDKLTRVHDKIWCCRSGSAADTQAIADIVQYHLELYTSQYGTPSTETAASVFKELCYENKDNLTAGIIVAGYDDKNKGEVYTIPLGGSVHKLPYAIAGSGSTFIYGYCDKNFRENMSKEETVDFIKHSLSQAIKWDGSSGGVIRMVVLTAAGVERLIFYPDEYEQL
Protein: LD23835p (Q7KN56)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Chromosome, centromere, kinetochore {ECO:0000256|ARBA:ARBA00004629}.
Interaction partners:
Sequence:
SARSFCLTDTRQPKVSGHLLEENDMDFDNAKENIQPLASGRNVSLLQASLSQDSTHGQELLAQRKQMEEEVRTYKGADPLGAWYTFICWIEQSYPAGGSGSGLQTVLHQCLTKFEDDERYRQDKRLIKLFIKFMEKQKDKIEFYQQMYNNGIGTMLADFYIAWAYSYDLSGNMRKADEIFRLGLECRAEPLEDLKEAHHHFGYTVGQRMLYSTGEEANAVNQELNERRLALQSLHGRRQQISNSITVGSIRTGAAVKSGLPGVVQVEPSTTTSRRNVGRNVEVFNDENSEGNIPISNSETEVKSSLRSIIDSACSQENIKEPVAWNKANAKRHKHGKIFGSNASPDLGFDIHVDEQAMPPITNYERRLEQPFRFPTNFVAKNRPQEPWVTPVTIEDEPNASGLPCYNKCLLYPRPNIEFSPEEYRAYSFLKHRNPQHPFIHRNDDWWGTGRVIRGIRCYPNFARYSKPQDLDELDKFWKPPLVPGLQVVFDKIYNEVEQKEYQPEELLAAKWMEKRNVTVHGDFDMEETVCLPGNKMPRRKSFFPSSFRKSIMPRRVSSVQEEDEKKEDEATLIVKDIPSQVAPKIPESPCDQIDEPKIKIFEDSGSPRDNFAVPAVPVPKIEIYEDSEEPQPTPKTRPFYDGDETCSTQMFNMFIKSQAVSTPKGTQKQAPSRQFGTVLKELPLPEEAAHSVESPVETRSPTLRKQLSTILETSEHGTQSLATSGTTTKSTITSTSSPGSNAVSKLGSKIEENTPGQMRLQRVISAGVSAVLSEPEKPGGDNFLRRELWEPNAPSVPMLKSLRFQEDKTETIPRPLACFQEDKTETLPQMPIALPENSMDHGSLGAENCFSAPQLPTLEDESDLCGLFGKTPPKTNIFGSPKRNFDPTSQLFKSTQGDRRSFAVTGNKLEAAPSISNLQDSFMCDLSFVPETQPEAVAKSGAIQKFDIFLDDTQPKLTKSKPVALMVSSFDLDCTLPETQQVAIKEPGTQQENIGHSHMIASFMKDCTEIGSCPSQMPASVVKTNISSTSNKIKFSNDSMSESSRKAPVNENVGISKQPDEFFELNAATEMFATNISMIKNSTLLIPNAKVAEASELSIYYKTTPLTPKQSHRSWSQSDLETPPRENFVHPTSNGDQTVLNETLADANKNPFNVELISSLLESIDFSMYIEKLPHCQLVGHVKRLHPNTHLEVHNEKFEVSKMIGKGAYGSVYVGKHLKSGKKVALKQERPTNYWEFYICLEIHSRLTSEQMIPSYAHIDYALVGNNSSVYISEFSDYGSLIGVCNKVKSVTNRNMDEYVVMHLSCQMLDIVDHLHAMGIIHADIKPDNFLLMKPICADPNEVSLQLIDFGVSIDMKLFPDNQTFNYVHHDDLFKCIEMRTGRPWTYQLDLYGLVSVMHVLLFGRYMEVVQRSPSTIWMPKTNVPRYFQRTMWENIFRTLLNIRDCRTMPNLQQLRTQLKCALAEKEKYVAEAISKFNTILQK
Protein: Calmodulin-binding coil-coil protein (C8VIR1)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000256|ARBA:ARBA00004267}.
Interaction partners:
Sequence:
MAYPYIDTPRTEVDGNATYLTNGYRSVGRHNLSALDSVENSFQTPSKDEDVLKVLGDGRGRSFAGSKLNTPRATAGTKSTRSALNSRQLPTMGAKGEFTPMLKSAMKNNYMKNVSTTRGTGGPKTPSYARGGYRSNGNTPGLTVMEMTGIDEEDATADEPTPVPQVASSSVAGTPLPGLTSRDNGVLGDGSNMTLKEQEKIIDKLDKDNFGLKLKIHFLQEQLEKAGPAYNQAALHENTELKISKLTMQRDISRYKKSLQQAERDLEAYRQQFQDFKEKMRRKHTDETIQREMEDQRVKELQEQLREARDSRSEEIDKLRDDIEDLEASLREKDRTIEEREEEIEELKDRDSQEKDSLSELETELRRAKEQLEELQDSLDQAKSDAIEARTSERQALEEKERAEQNLQELHDEMSNKSISTKGLTRQLEEEVKELRQRNSTLKEELESKTQQMNDLEERLQNSRETTDSERERLLEELTQVRREREVARQERDDLNVQLQEAHDELQRKTDEKALLHTRHHALTDESSNLQNELAKAQSNIRELQESLDTVKQNAAENAENLRSQYMEDIERLQEEIESLHHEIEDKEGQFALEQDRWESLRRNLQVQKDRAEDQAAGFKRTIEKLEQVEHTLTGKESKLQEVIDSEKARHFNAEAVLSRQVKELNDDLSAKRDAIDELRHELLSVKEELRLARRAEATLKEKVQSLEDEVVVLQSSLEEEQEYTKAHTRKGPVEQESQVQKLLADKQKLRDQLANAHVELHDLKTVKAEIEAERDELQAQLEQVQNQVSDTRFDKEKTELRKASLRMETELKRLKEDKMSLLETKESLENQLNSEIERAALEENRLSAEIDQLQTKLQSASGGRDRELALTKSKLQRFERRIHELEERLEQQPPANQEQSATAADLSMLRHSLDEVRKREKALIQRETDQKASIRAYKTKIVELERELHDATIKKFETQSPSSSPANKLQQDVRTLRKQLSDAHRALRELKSKNHDLERAAMREEDQRDLHELLKQSTLEAESLALQVSEKEAQLNDAESRIRRVREERASYARKANAALKELDTLQDRYKQTMEKARAKGENKTKHEKEMLGLGKEILWLRARLKREEKFRRDLAWGKGLMELGERVRIACNEADLRMISDMGVIARDRSNLRSPKAKLKTAVSMVKAVVRMQKMSREWKKTTKLGEGLKRAKNEVMKRRELSKE
Protein: Cell wall synthesis protein KRE9 (O74683)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Function: Involved in cell wall beta(1->6) glucan synthesis.
Subcellular location: Secreted, cell wall {ECO:0000305}.
Interaction partners:
- Protein ROT1
- Protein BIG1
Sequence:
MLLLAILLSLFALIRADVNIVEPGPGDTFSGADGTVSINLKWVDNGAYPPLDKVAYYLFSLCYGPNTKIQCVYKPDTKITPDDLDKDDAGTYSYKFDIQSSVVGSGQFYVQVFAWVDGQGYTLHYTPRIELTNMGGPTTFELLTYTDTIQPVPQTSIRTGTDTNTQSFDASSVYSLPYTEQTLKTRVAPIQQQPGTKVTATTWSRRYPTSAVTFYSTFRSSLDQLSTLTPAWNYTVSSAVNYATPAAMPSDNGGWYNPIKRQSLSTRKLNVRYLSS
Protein: E3 ubiquitin-protein ligase PUB23 (EC 2.3.2.27) (Plant U-box protein 23) (RING-type E3 ubiquitin transferase PUB23) (U-box domain-containing protein 23) (Q84TG3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: E3 ubiquitin-protein ligase that negatively regulates water stress response. May control in coordination with PUB23 a drought signaling pathway by ubiquitinating cytosolic RPN12a. Acts as negative regulator of the immunity triggered by the pathogen-associated molecular patterns (PAMPs), in association with PUB22 and PUB24.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18664614}.
Interaction partners:
- 26S proteasome non-ATPase regulatory subunit 8 homolog A
- Exocyst complex component EXO70B2
- 26S proteasome non-ATPase regulatory subunit 11 homolog
- Squamosa promoter-binding-like protein 11
- Probable WRKY transcription factor 40
Sequence:
MSGGIMDEEIEIPPFFLCPISLEIMKDPVIVSTGITYDRDSIEKWLFAGKKNSCPVTKQDITDADLTPNHTLRRLIQSWCTLNASYGVERIPTPRPPICKSEIEKLIRDSASSHENQVKCLKRLRQIVSENATNKRCLEAAGVPEFLANIVSNDSENGSLTDEALNLLYHLETSETVLKNLLNNKKDNNIVKSLTKIMQRGMYESRVYATLLLKNILEVADPMQSMTLKPEVFTEVVQILDDRISQKATKAAMHILVNICPWGRNRHKAVEAGVISVIIELLMDESFTSERRGPEMAMVVLDLLCQCAEGRAEFLNHGAAIAVVCKKILRVSQTASDRAVRVLLSVGRFCATPALLHEMLQLGVVAKLCLVLQVSCGGKTKEKAKELLKLHARVWKDSPCLPKNMILAYPC
Protein: PITH domain-containing protein 1 (Q8BWR2)
Organism: Mus musculus (Mouse)
Function: Promotes megakaryocyte differentiation by up-regulating RUNX1 expression. Regulates RUNX1 expression by activating the proximal promoter of the RUNX1 gene and by enhancing the translation activity of an internal ribosome entry site (IRES) element in the RUNX1 gene (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9GZP4}.
Interaction partners:
Sequence:
MSHGHSHGGGGCRCAAEREEPPEQRGLAYGLYLRIDLERLQCLNESREGSGRGVFKPWEERTDRSKFVESDADEELLFNIPFTGNVKLKGVIIMGEDDDSHPSEMRLYKNIPQMSFDDTEREPEQTFSLNRDITGELEYATKISRFSNVYHLSIHISKNFGADTTKIFYIGLRGEWTELRRHEVTICNYEASANPADHRVHQVTPQTHFIS
Protein: Reticulon-like protein (E1JHT6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU363132}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU363132}.
Interaction partners:
- Vacuolar protein sorting-associated protein VTA1 homolog
- GTP cyclohydrolase 1
- Atlastin
- Kekkon 5, isoform A
- Receptor expression-enhancing protein
- RE14391p
- Spastin
- Receptor expression enhancing protein A, isoform I
- ADP-ribosylation factor-like protein 6-interacting protein 1
Sequence:
MDRNFDELKKEAAATNEDIFKQAQRAYEDSALGGDTGNVSGGAQDDNAHTEHYFANEQKKLDFGDAQEFVQRLAADAKDAKLDLDTKFAQKTDDFEDFLRDAGKEVKQGISGLTTDFMNAERGFSAPLAPFSETVAQAPVIPAQAPAVPDHAPAVPAPVAPAPAVPAPLPVEEDLLGSFTDQPSAPLQAFQPTAPSTANFYDDEEDDFLGKPTTAAPAAPVAPLTKANQDSDTESPSVSYTPSPAKKPIVDALKDQDNEKFISSEDLASDFKEEPRSAPTPAPAPAPILDAAPAVAPAPVAVPVSVPVAKPQPVPVAVPVTTALITDLDDEEVVFKPTVQEAPKAPTIAAPVVEPKPEPPKPKVEPAKPKVVPVAPVESTQPQPKIASVEEIFCKYGLDAWFKPERLHPQVESLIYWRDVKKSGIVFGAGLITLAAISSFSVISVFAYLSLLTLFGTVAFRIYKSVTQAVQKTNEGHPFKDYLELDLTLSHEKVQNIAGVAVAHINGFISELRRLFLVEDIIDSIKFGVILWVFTYVGAWFNGMTLVILAFVSLFTLPKVYENNKQSIDTHLDLVRSKLTEITDKIRVAIPIGNKKPEAAAESEKDK
Protein: MutL homolog 1 (H0Y818)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSFVAGVIRRLDETVVNRIAAGEVIQRPANAIKEMIENCLDAKSTSIQVIVKEGGLKLIQIQDNGTGIRKEDLDIVCERFTTSKLQSFEDLASISTYGFRGEALASISHVAHVTITTKTADGKCAYRASYSDGKLKAPPKPCAGNQGTQITVEDLFYNIATRRKALKNPSEEYGKILEVVGRYSVHNAGISFSVKKQGETVADVRTLPNASTVDNIRSIFGNAVSRELIEIGCEDKTLAFKMNGYISNANYSVKKCIFLLFINHRLVESTSLRKAIETVYAAYLPKNTHPFLYLSLEISPQNVDVNVHPTKHEVHFLHEESILERVQQHIESKLLGSNSSRMYFTQTLLPGLAGPSGEMVKSTTSLTSSSTSGSSDKVYAHQMVRTDSREQKLDAFLQPLSKPLSSQPQAIVTEDKTDISSGRARQQDEEMLELPAPAEVAAKNQSLEGDTTKGTSEMSEKRGPTSSNPRKRHREDSDVEMVEDDSRKEMTAACTPRRRIINLTSVLSLQEEINEQGHEVLREMLHNHSFVGCVNPQWALAQHQTKLYLLNTTKLSEELFYQILIYDFANFGVLRLSEPAPLFDLAMLALDSPESGWTEEDGPKEGLAEYIVEFLKKKAEMLADYFSLEIDESEVPGSIPNSWKWTVEHIVYKALRSHILPPKHFTEDGNILQLANLPDLYKVFERC
Protein: Protein DETOXIFICATION 1 (AtDTX1) (Multidrug and toxic compound extrusion protein 1) (MATE protein 1) (Q9SIA5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Efflux carrier for plant-derived alkaloids, antibiotics, heavy metal and other toxic compounds. Involved in cadmium detoxification. Requires probably a proton-motive force for the efflux.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11739388}; Multi-pass membrane protein {ECO:0000269|PubMed:11739388}.
Interaction partners:
- Protein DETOXIFICATION 43
- Protein DETOXIFICATION 42
- KIB1-4 beta-propeller domain-containing protein
- Expressed protein
- KIB1-4 beta-propeller domain-containing protein
- KIB1-4 beta-propeller domain-containing protein
- Protein DETOXIFICATION 44, chloroplastic
- Amino acid transporter AVT1E
- Calcium-binding site protein
- Protein DETOXIFICATION 46, chloroplastic
Sequence:
MEEPFLLRDELLVPSQVTWHTNPLTVELKRVSRLAAPMATVTIAQYLLPVISVMVAGHNGELQLSGVALANSFTNVTGFSIMCGLVGALETLCGQAYGAKQYEKIGTYAYSAIASNIPICFLISILWLYIEKILISLGQDPEISRIAGSYAFWLIPALFGQAIVIPLSRFLLTQGLVIPLLFTAVTTLLFHVLVCWTLVFLFGLGCNGPAMATSVSFWFYAVILSCYVRFSSSCEKTRGFVSRDFVSSIKQFFQYGIPSAAMICLEWWLFEILILCSGLLPNPKLETSVLSICLTIETLHYVISAGVAAAVSTRVSNNLGAGNPQVARVSVLAGLCLWIVESAFFSILLFTCRNIIGYAFSNSKEVLDYVADLTPLLCLSFILDGFTAVLNGVARGSGWQHIGAWNNTVSYYLVGAPVGIYLAFSRELNGKGLWCGVVVGSTVQATILAIVTASINWKEQAEKARKRIVSTENRLA
Protein: Alpha,alpha-trehalose-phosphate synthase [UDP-forming] (EC 2.4.1.15) (Trehalose-6-phosphate synthase) (UDP-glucose-glucosephosphate glucosyltransferase) (O94213)
Organism: Pichia angusta (Yeast) (Hansenula polymorpha)
Function: Synthase catalytic subunit of the trehalose synthase complex that catalyzes the production of trehalose from glucose-6-phosphate and UDP-alpha-D-glucose in a two step process.
Interaction partners:
Sequence:
MVKGNVIVVSNRIPVTIKKTEDDENGKSRYDYTMSSGGLVTALQGLKNPFRWFGWPGMSVDSEQGRQTVERDLKEKFNCYPIWLSDEIADLHYNGFSNSILWPLFHYHPGEMNFDEIAWAAYLEANKLFCQTILKEIKDGDVIWVHDYHLMLLPSLLRDQLNSKGLPNVKIGFFLHTPFPSSEIYRILPVRKEILEGVLSCDLIGFHTYDYVRHFLSSVERILKLRTSPQGVVYNDRQVTVSAYPIGIDVDKFLNGLKTDEVKSRIKQLETRFGKDCKLIIGVDRLDYIKGVPQKLHAFEIFLERHPEWIGKVVLIQVAVPSRGDVEEYQSLRAAVNELVGRINGRFGTVEFVPIHFLHKSVNFQELISVYAASDVCVVSSTRDGMNLVSYEYIACQQDRKGSLVLSEFAGAAQSLNGALVVNPWNTEELSEAIYEGLIMSEEKRRGNFQKMFKYIEKYTASYWGENFVKELTRV
Protein: Probable glucan endo-1,3-beta-glucosidase A6 (EC 3.2.1.39) ((1->3)-beta-glucan endohydrolase) ((1->3)-beta-glucanase) (Anther-specific protein A6) (Beta-1,3-endoglucanase) (Protein MATERNAL EFFECT EMBRYO ARREST 48) (Q06915)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable beta-1,3-glucanase that may be involved in the degradation of callose walls around the microspore tetrad during pollen development (Probable). May be required for pollen exine formation.
Interaction partners:
- Type III polyketide synthase B
- Cytochrome P450 703A2
- ATA20 protein
- Cytochrome P450 704B1
- Beta-glucosidase 20
- Polygalacturonase QRT3
- Non-specific lipid-transfer protein 12
- Type III polyketide synthase A
- Putative fasciclin-like arabinogalactan protein 20
- 4-coumarate--CoA ligase-like 1
Sequence:
MSLLAFFLFTILVFSSSCCSATRFQGHRYMQRKTMLDLASKIGINYGRRGNNLPSPYQSINFIKSIKAGHVKLYDADPESLTLLSQTNLYVTITVPNHQITALSSNQTIADEWVRTNILPYYPQTQIRFVLVGNEILSYNSGNVSVNLVPAMRKIVNSLRLHGIHNIKVGTPLAMDSLRSSFPPSNGTFREEITGPVMLPLLKFLNGTNSYFFLNVHPYFRWSRNPMNTSLDFALFQGHSTYTDPQTGLVYRNLLDQMLDSVLFAMTKLGYPHMRLAISETGWPNFGDIDETGANILNAATYNRNLIKKMSASPPIGTPSRPGLPIPTFVFSLFNENQKSGSGTQRHWGILHPDGSPIYDVDFTGQTPLTGFNPLPKPTNNVPYKGQVWCVPVEGANETELEETLRMACAQSNTTCAALAPGRECYEPVSIYWHASYALNSYWAQFRNQSIQCFFNGLAHETTTNPGNDRCKFPSVTL
Protein: RNA helicase (EC 3.6.4.13) (A0A2R8YF78)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSHVAVENALGLDQQFAGLDLNSSDNQSGGSTASKGRYIPPHLRNREATKGFYDKDSSGWSSSKDKDAYSSFGSRSDSRGKSSFFSDRGSGSRGRFDDRGRSDYDGIGSRGDRSGFGKFERGGNSRWCDKSDEDDWSKPLPPSERLEQELFSGGNTGINFEKYDDIPVEATGNNCPPHIESFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYSDGPGEALRAMKENGRYGRRKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPKGVRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQKVVWVEESDKRSFLLDLLNATGKDSLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNERNINITKDLLDLLVEAKQEVPSWLENMAYEHHYKGSSRGRSKSSRFSGGFGARDYRQSSGASSSSFSSSRASSSRSGGGGHGSSRGFGGGSVNL
Protein: Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B (Asp/Glu-ADT subunit B) (EC 6.3.5.-) (Q72AV5)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Interaction partners:
- Aspartyl/glutamyl-tRNA
- Glutamyl-tRNA
- Asparagine--tRNA ligase
- Aspartate--tRNA
- Glutamine--tRNA ligase
- GMP synthase
- Glutamate--tRNA ligase
- Glutamyl-Q tRNA
- DUF4254 domain-containing protein
- Phenylalanine--tRNA ligase beta subunit
Sequence:
MASYEAVIGLEVHAQLRTRSKLFCSCSTAFGADPNAHVCEVCAGMPGVLPVLNEKAVEFAARMGIAVGCTVNRTSVFARKNYFYPDLPKGYQISQYEQPICEHGHLDISVGDAVKRIGITRIHLEDDAGKNIHSAGENVSYVDLNRTGVPLIEIVSEPDLRSAEEAVAYLKALRAIVVHLGICDGNMEEGSFRCDANVSLRPRGAAEFGTRAELKNLNSFRHVQRAIEYEISRQADLLDDGDKVVQETRLYDSVKNITVSMRGKEEAHDYRYFPDPDLIPIHIDEARLAEWQATLPELPQARLERFMSSFGLSAQDAEVLTAERDHAEFFEAAVKLYDQPRKIANMMLGPLQRELNQRGTSLAVSAMRPEALAELVRIIDAGLISAKIGNDVFGELFENGAMPEAFVRERGLVQISDTSAIEQAVDEVIAENPAEVEAYRGGKTKLVSFFVGQVMRKTRGKANPALVNELLASKLG