wanglab/gogpt-training-data huggingface dataset:
Protein: FAD-binding monooxygenase VdtE (EC 1.14.13.-) (Viriditoxin biosynthesis cluster protein E) (A0A443HK11)
Organism: Byssochlamys spectabilis (Paecilomyces variotii)
Function: FAD-binding monooxygenase; part of the gene cluster that mediates the biosynthesis of viriditoxin, one of the 'classical' secondary metabolites produced by fungi and that has antibacterial activity. The first step is performed by the polyketide synthase VdtA which condenses one acetyl-CoA and 6 malonyl-CoA units to form the heptaketide monomer backbone of viriditoxin. The product of VdtA is then O-methylated on C7 by the O-methyltransferase VdtC. The O-methyl group is important for the stereoselective coupling of the monomers at the final step of viriditoxin biosynthesis. The short-chain dehydrogenase/reductase VdtF then acts as a stereospecific reductase converting the pyrone to dihydropyrone via the reduction of the C3-C4 double bond. The FAD-binding monooxygenase VdtE then converts the ketone group into a methyl-ester group to yield semi-viriditoxin. Finally, the laccase VdtB is involved in dimerization of 2 semi-viriditoxin molecules to yield the final viriditoxin. VdtB is responsible for the regioselective 6,6'-coupling of semi-viriditoxin, which yields (M)-viriditoxin and (P)-viriditoxin at a ratio of 1:2. The non-catalytic carboxylesterase-like protein VdtD affects the stereochemistical outcome of the coupling. The highly reducing polyketide synthase VdtX is not involved in viriditoxin synthesis, but might possibly play a role in the production of additional metabolites not identified yet.
Interaction partners:
- Putative lipase
- Putative esterase
Sequence:
MASMQEVDALVVGAGFGGLWMTNRLKEAGLNVLCVEKAPQAGGVWYWNCYPGARVDSRYPVYQYSDESLCKDWNWSELFPGYEEIRKYLSYAVDKWQLNSHIRYNTTVTGARFDESDHKWTVEGINGSHGTIRIRCRWYILALGFASKPYIPDFEGLNRFQGPCFHSSAWPQEGIDLKGRRVAVVGTGASAVQIIQTISKEVGHLTVYQRTPCTAMPMRQQSLTPEYQDNFKASGEMAATMRRTKYERFGGQDVQFVSRRWHEDTPEQRRAVFEQAWQKGGFHLLLSTYFEVFDDVEVNHAAWRFWAEKSRERIHNTKYKDILAPLEAVHAFGGKRTPFEQDYFEAFNRRNVDLIDMKASPILSFAEKGIITQNEGLQEFDVIILATGFDTNTGALTSIHIQDTDGILLKDRWSYDGVMTTFGMSTSKFPNMFFFYGPQAPTAFSNGPSCIELQGEFVEELILDMIGKGVTRVDTTSEAEKRWKESTLSLWNQFVFSSTKGFYTGENIPGKKAEPLNWFGGFPRYRKALTECRDGGYKEYSLRSLPKVPDPEHRGLIDKVAVVTSAQPVGA
Protein: Mismatch repair endonuclease PMS2 (G5EFG5)
Organism: Caenorhabditis elegans
Interaction partners:
- DNA mismatch repair protein S5 domain-containing protein
- DNA mismatch repair protein
- DNA mismatch repair proteins mutS family domain-containing protein
- Exonuclease 1
- Fanconi-associated nuclease 1 homolog
- Helicase ATP-binding domain-containing protein
- MutS protein homolog 5
- MutS protein homolog him-14
- XPA C-terminal domain-containing protein
- Proliferating cell nuclear antigen
Sequence:
MSQNKIERISKEVAERLTTAQVVVSLSSAIRQLIDNSIDAGSTIIDIRVKNNGFESIEVQDNGSGIEARNFDALCKPHSTSKLTQFSDFDKLATLGFRGEALNALCTVSSVSIFTRASDTEIGTRLTYDHSGNIICRQSAARELGTTIIVNKLFETLPVRRKELERSQKREFVKLLSTVQSFALLCPHIKILCTNNINGKKTNLICTPGGTTSIQDVVANLFGIARKIENSKIGSGLIPIQQNQPDVEIMTIHSVPMEEMHFFDLFKIRGFVSSCEHGCGRGTSDRQFVYINNRPVEYSRVCSVINDVYKQFNKKQYPIIVLFIDVPPEKIDVNVTPDKKTVMLEKERHLLAVVRASMMKTYLKIVGSHSTVRSSVEDRRIMNLSQQSFSNASFMSSKSSTPDDFNNTTLNSTYPEDSLLNTSDLLKQRKENRSPPAKKSCPMIRRTEPFHSVPSTSNSRTQRLENFSFTMEPKRVEVSKKIPSKSDKKLTDEELRSAVIEENPLKKAGEIDDIEILEQSQESQDVNESQCSQDSQTSQNSRVSYFTLRPQQKIKFSMKLLREAYSPKTDETDDNTEEAEVSAEKDVLNEITTKINKEENDDAERQLSRSLTKDDFSKMKIIGQFNHGFIICRLRGHLFIVDQHASDEKYNFERLQSSAKLTKQPLFMPTALGFGAVQELIIRENLPIFHANGFDFEFSENDGCIKTFLTARPELLNQQLTNSDLEEILAVVSQYPNQMYRPVRIRKIFASKACRKSVMIGKPLNQREMTQIIRHLAKLDQPWNCPHGRPTIRHLASLPDRAEFE
Protein: DnaJ heat shock protein family (Hsp40) member C7 (A0A6I8PRZ0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MCPKNASYYGNRAATLMMLGRFREALGDAQQSVRLDDSFVRGHLREGKCHLSLGNAMAACRSFQRALELDHKNAQAQQEFKNANAVMEYEKIAETDFEKRDFRKVVFCMDRALEFAPACHRFKILKAECLAMLGRYPEAQSVASDILRMDSTNADALYVRGLCLYYEDCIEKAVQFFVQALRMAPDHEKACIACRNAKALKAKKEDGNKAFKEGNYKLAYELYTEALGIDPNNIKTNAKLYCNRGTVNSKLRKLDDAIEDCTNAVKLDDTYIKAYLRRAQCYMDTEQYEEAVRDYEKVYQTEKTKEHKQLLKNAQLELKKSKRKDYYKILGVDKNASEDEIKKAYRKRALMHHPDRHSGASAEVQKEEEKKFKEVGEAFTILSDPKKKTRYDSGQDLDEEGMNMGDFDPNNIFKAFFGGPGGFSFEASGPGNFFFQ
Protein: Small ribosomal subunit protein uS12 (40S ribosomal protein S23) (P62268)
Organism: Rattus norvegicus (Rat)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. Plays an important role in translational accuracy.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P62266}. Cytoplasm {ECO:0000250|UniProtKB:P62266}. Rough endoplasmic reticulum {ECO:0000250|UniProtKB:Q6SA96}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P62266}. Note=Detected on cytosolic polysomes (By similarity). Detected in ribosomes that are associated with the rough endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:P62266, ECO:0000250|UniProtKB:Q6SA96}.
Interaction partners:
- Small ribosomal subunit protein eS8
- Small ribosomal subunit protein eS7
- Small ribosomal subunit protein uS9
- Small ribosomal subunit protein uS7
- Ubiquitin-like protein FUBI
- Small ribosomal subunit protein uS15
- Large ribosomal subunit protein eL18
- Small ribosomal subunit protein uS4
- Small ribosomal subunit protein eS1
- Small ribosomal subunit protein uS14
Sequence:
MGKCRGLRTARKLRSHRRDQKWHDKQYKKAHLGTALKANPFGGASHAKGIVLEKVGVEAKQPNSAIRKCVRVQLIKNGKKITAFVPNDGCLNFIEENDEVLVAGFGRKGHAVGDIPGVRFKVVKVANVSLLALYKGKKERPRS
Protein: Nucleoside diphosphate kinase (EC 2.7.4.6) (Q9U9K9)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MPSERTFIAVKPDGVQRNLVGEIIKRFENKGYKLVGLKLLQPTEEQAKQHYIDLASKPFYSGLVSYFSSGPIVGMVWEGLGVVKGGRVLLGATNPADSLPGTIRGDFAVDVGRNVCHGSDSVESAKREIAFWFKAEELVSWTSHSVKQIYGRA
Protein: Translation initiation factor eIF2B subunit epsilon (eIF2B GDP-GTP exchange factor subunit epsilon) (Q64350)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the exchange of eukaryotic initiation factor 2-bound GDP for GTP.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P56287}.
Interaction partners:
- Translation initiation factor eIF2B subunit alpha
- Translation initiation factor eIF2B subunit beta
- Translation initiation factor eIF2B subunit delta
- Translation initiation factor eIF2B subunit gamma
- Eukaryotic translation initiation factor 2 subunit 1
- Eukaryotic translation initiation factor 2, subunit 2
- Eukaryotic translation initiation factor 2 subunit 3, X-linked
- Eukaryotic translation initiation factor 2 subunit 3, Y-linked
- tRNA
- dTDP-D-glucose 4,6-dehydratase
Sequence:
MAATAAVPSAVGGRANKRGGGSGGGGTQGAEEEPPPPLQAVLVADSFDRRFFPISKDQPRVLLPLANVALIDYTLEFLTATGVQETFVFCCWKAAQIKEHLQKSKWCHPTSLNVVRIITSDLYRSLGDVLRDVDAKALVRSDFLLIYGDVVSNINISKALEEHRLRRKLEKNVSVMTMVFKESSPSHPTRCHEDNVVLAVDSTTNRILHFQKTQGLRHFSFPLGLFQGSLDGVEIRYDLLDCHISICSPQVAQLFTDNFDYQTRDDFVRGLLVNEEILGNQIHLHVTSREYGARVSNLHMYSAVCADVIRRWVYPLTPEVNFTDSSTQSYTHSRHNIYRGPEVSLGHGSVLEENVLLGAGTVVGSNCSITNSVIGPNCHIGDNVVLDQAYLWQGVRVAAGAQIHQSLLCDRAEVKERVILKPHCVLTSQVVVGPDIILPEGSVISLHPPDAEEDEDDGQFSDDSGADQEKEKVKLKGYNPAEVGPEGQGYLWKAEDVDEKEDEELRQSLWGLMINMEEESETESERSVDPEELDSRAGSPQLDDIRVFQNEVLGTLQRGREENISCDNLVLEINSLKYAYNISLKEVMQVLSHVVLEFPLQQVDGVLDPNRYCALLLPLLKAWSPVFRNYIKRAADHLEALAAIEDFFLEHETLVPSLAKVLMAFYQLEILAEETILSWFSQRDITDKGQQLRKNQQLQRFIQWLREAEEESSDDD
Protein: Putative diacyglycerol O-acyltransferase Rv3087 (EC 2.3.1.20) (Putative triacylglycerol synthase Rv3087) (P9WKB1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Required for maintaining the appropriate mycolic acid composition and permeability of the envelope on its exposure to acidic pH. Upon expression in E.coli functions weakly as a triacylglycerol synthase, making triacylglycerol (TG) from diolein and long-chain fatty acyl-CoA. Has no wax synthase activity.
Interaction partners:
- Long-chain-fatty-acid--CoA ligase FadD13
- Probable diacyglycerol O-acyltransferase Tgs4
- Putative FAD-containing monooxygenase MymA
- Putative alcohol dehydrogenase D
- Putative acetyl-hydrolase LipR
- Putative oxidoreductase SadH
- Triacylglycerol lipase
- Diacylglycerol kinase
- Possible multi-functional enzyme with acyl-CoA-reductase activity AcrA1
- Possible triacylglycerol synthase
Sequence:
MRRLNGVDALMLYLDGGSAYNHTLKISVLDPSTDPDGWSWPKARQMFEERAHLLPVFRLRYLPTPLGLHHPIWVEDPEFDLDAHVRRVVCPAPGGMAEFCALVEQIYAHPLDRDRPLWQTWVVEGLDGGRVALVTLLHHAYSDGVGVLDMLAAFYNDTPDEAPVVAPPWEPPPLPSTRQRLGWALRDLPSRLGKIAPTVRAVRDRVRIEREFAKDGDRRVPPTFDRSAPPGPFQRGLSRSRRFSCESFPLAEVREVSKTLGVTINDVFLACVAGAVRRYLERCGSPPTDAMVATMPLAVTPAAERAHPGNYSSVDYVWLRADIADPLERLHATHLAAEATKQHFAQTKDADVGAVVELLPERLISGLARANARTKGRFDTFKNVVVSNVPGPREPRYLGRWRVDQWFSTGQISHGATLNMTVWSYCDQFNLCVMADAVAVRNTWELLGGFRASHEELLAAARAQATPKEMAT
Protein: E3 ubiquitin-protein ligase SINAT3 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase SINAT3) (Seven in absentia homolog 3) (Q84JL3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. It probably triggers the ubiquitin-mediated degradation of different substrates. Modulates directly the ubiquitination and proteasomal-dependent degradation of FREE1, a component of the ESCRT-I complex. Modulates directly the ubiquitination and proteasomal-dependent degradation of ELC/VPS23A, a component of the ESCRT-I complex.
Subcellular location: Endosome, multivesicular body {ECO:0000269|PubMed:32753431, ECO:0000269|PubMed:32786047}. Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:32753431}.
Interaction partners:
- Probable receptor-like protein kinase At3g17420
- Protein ELC
- At3g20340
- Probable protein phosphatase 2C 36
- Protein FREE1
Sequence:
MDLDSMDCTSTMDVTDDEEIHQDRHSYASVSKHHHTNNNTTNVNAAASGLLPTTTSVHELLECPVCTNSMYPPIHQCHNGHTLCSTCKARVHNRCPTCRQELGDIRCLALEKVAESLELPCKHMSLGCPEIFPYYSKLKHETVCNFRPYSCPYAGSECSVTGDIPFLVAHLRDDHKVDMHSGCTFNHRYVKSNPREVENATWMLTVFHCFGQYFCLHFEAFQLGMAPVYMAFLRFMGDETEARNYNYSLEVGGYGRKLIWEGTPRSVRDSHRKVRDSHDGLIIQRNMALFFSGGDRKELKLRVTGRIWKEQQQSGEGGGACIPNLS
Protein: Transmembrane emp24 domain-containing protein 2 (Membrane protein p24A) (p24) (p24 family protein beta-1) (p24beta1) (Q15363)
Organism: Homo sapiens (Human)
Function: Involved in vesicular protein trafficking. Mainly functions in the early secretory pathway but also in post-Golgi membranes. Thought to act as cargo receptor at the lumenal side for incorporation of secretory cargo molecules into transport vesicles and to be involved in vesicle coat formation at the cytoplasmic side. In COPII vesicle-mediated anterograde transport involved in the transport of GPI-anchored proteins and proposed to act together with TMED10 as their cargo receptor; the function specifically implies SEC24C and SEC24D of the COPII vesicle coat and lipid raft-like microdomains of the ER. Recognizes GPI anchors structural remodeled in the ER by PGAP1 and MPPE1. In COPI vesicle-mediated retrograde transport inhibits the GTPase-activating activity of ARFGAP1 towards ARF1 thus preventing immature uncoating and allowing cargo selection to take place. Involved in trafficking of G protein-coupled receptors (GPCRs). Regulates F2RL1, OPRM1 and P2RY4 exocytic trafficking from the Golgi to the plasma membrane thus contributing to receptor resensitization. Facilitates CASR maturation and stabilization in the early secretory pathway and increases CASR plasma membrane targeting. Proposed to be involved in organization of intracellular membranes such as the maintenance of the Golgi apparatus. May also play a role in the biosynthesis of secreted cargo such as eventual processing.
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000269|PubMed:9472029}; Single-pass type I membrane protein {ECO:0000255}. Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:10852829, ECO:0000269|PubMed:12237308}; Single-pass type I membrane protein {ECO:0000255}. Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:10852829, ECO:0000269|PubMed:12237308}; Single-pass type I membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:10852829, ECO:0000269|PubMed:12237308}; Single-pass type I membrane protein {ECO:0000255}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000269|PubMed:12237308}; Single-pass type I membrane protein {ECO:0000255}. Note=Cycles between compartments of the early secretatory pathway. {ECO:0000269|PubMed:12237308}.
Interaction partners:
- Transmembrane emp24 domain-containing protein 10
- Transmembrane emp24 domain-containing protein 9
- Transmembrane emp24 domain-containing protein 4
- Transmembrane emp24 domain-containing protein 7
- Transmembrane emp24 domain-containing protein 3
- Transmembrane emp24 domain-containing protein 5
- Surfeit locus protein 4
- Vesicular integral-membrane protein VIP36
- Protein ERGIC-53
- Ras-related protein Rab-1A
Sequence:
MVTLAELLVLLAALLATVSGYFVSIDAHAEECFFERVTSGTKMGLIFEVAEGGFLDIDVEITGPDNKGIYKGDRESSGKYTFAAHMDGTYKFCFSNRMSTMTPKIVMFTIDIGEAPKGQDMETEAHQNKLEEMINELAVAMTAVKHEQEYMEVRERIHRAINDNTNSRVVLWSFFEALVLVAMTLGQIYYLKRFFEVRRVV
Protein: Probable pseudouridine-5'-phosphatase (EC 3.1.3.96) (GS1-like protein) (Pseudouridine-5'-monophosphatase) (5'-PsiMPase) (Q94529)
Organism: Drosophila melanogaster (Fruit fly)
Function: Dephosphorylates pseudouridine 5'-phosphate, a potential intermediate in rRNA degradation.
Interaction partners:
- Putative riboflavin kinase
Sequence:
MANKVLRKVTHCVFDMDGLLLDTERLYTVATEMILEPYGKTYPFEIKEQVMGLQTEPLARFMVEHYELPMSWEEYARQQRANTEILMRNAQLMPGAERLLRHLHANKVPFCLATSSGADMVELKTAQHRELFSLFNHKVCGSSDKEVVNGKPAPDIFLVAAGRFGVPPKPSDCLVFEDSPNGVTAANSAGMQVVMVPDPRLSQEKTSHATQVLASLADFKPEQFGLPAFTD
Protein: TYMS opposite strand protein (Q8TAI1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTPASGATASLGRLRARPRSRWDAAYLPAVAAVCVARASHVPNGTLRFGVCKARRTMRPLPRRIEVRTKRGPQRPAAPERSPQPRLPPSRHPSRRGPRRHLSGCSAPACRIPTGCRCPCGRPS
Protein: Axin-1 (Axis inhibition protein 1) (hAxin) (O15169)
Organism: Homo sapiens (Human)
Function: Component of the beta-catenin destruction complex required for regulating CTNNB1 levels through phosphorylation and ubiquitination, and modulating Wnt-signaling. Controls dorsoventral patterning via two opposing effects; down-regulates CTNNB1 to inhibit the Wnt signaling pathway and ventralize embryos, but also dorsalizes embryos by activating a Wnt-independent JNK signaling pathway. In Wnt signaling, probably facilitates the phosphorylation of CTNNB1 and APC by GSK3B. Likely to function as a tumor suppressor. Enhances TGF-beta signaling by recruiting the RNF111 E3 ubiquitin ligase and promoting the degradation of inhibitory SMAD7. Also a component of the AXIN1-HIPK2-TP53 complex which controls cell growth, apoptosis and development. Facilitates the phosphorylation of TP53 by HIPK2 upon ultraviolet irradiation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16601693}. Nucleus {ECO:0000269|PubMed:17210684}. Membrane {ECO:0000250|UniProtKB:O35625}. Cell membrane {ECO:0000250|UniProtKB:O35625}. Note=MACF1 is required for its translocation to cell membrane (By similarity). On UV irradiation, translocates to the nucleus and colocalizes with DAAX (PubMed:17210684). {ECO:0000250|UniProtKB:O35625, ECO:0000269|PubMed:17210684}.
Interaction partners:
- F-box/WD repeat-containing protein 1A
- Glycogen synthase kinase-3 alpha
- Catenin beta-1
- Segment polarity protein dishevelled homolog DVL-1
- Axin-2
- Low-density lipoprotein receptor-related protein 6
- Adenomatous polyposis coli protein
- Casein kinase I isoform alpha
- Glycogen synthase kinase-3 beta
- Segment polarity protein dishevelled homolog DVL-2
Sequence:
MNIQEQGFPLDLGASFTEDAPRPPVPGEEGELVSTDPRPASYSFCSGKGVGIKGETSTATPRRSDLDLGYEPEGSASPTPPYLKWAESLHSLLDDQDGISLFRTFLKQEGCADLLDFWFACTGFRKLEPCDSNEEKRLKLARAIYRKYILDNNGIVSRQTKPATKSFIKGCIMKQLIDPAMFDQAQTEIQATMEENTYPSFLKSDIYLEYTRTGSESPKVCSDQSSGSGTGKGISGYLPTLNEDEEWKCDQDMDEDDGRDAAPPGRLPQKLLLETAAPRVSSSRRYSEGREFRYGSWREPVNPYYVNAGYALAPATSANDSEQQSLSSDADTLSLTDSSVDGIPPYRIRKQHRREMQESVQVNGRVPLPHIPRTYRVPKEVRVEPQKFAEELIHRLEAVQRTREAEEKLEERLKRVRMEEEGEDGDPSSGPPGPCHKLPPAPAWHHFPPRCVDMGCAGLRDAHEENPESILDEHVQRVLRTPGRQSPGPGHRSPDSGHVAKMPVALGGAASGHGKHVPKSGAKLDAAGLHHHRHVHHHVHHSTARPKEQVEAEATRRAQSSFAWGLEPHSHGARSRGYSESVGAAPNASDGLAHSGKVGVACKRNAKKAESGKSASTEVPGASEDAEKNQKIMQWIIEGEKEISRHRRTGHGSSGTRKPQPHENSRPLSLEHPWAGPQLRTSVQPSHLFIQDPTMPPHPAPNPLTQLEEARRRLEEEEKRASRAPSKQRYVQEVMRRGRACVRPACAPVLHVVPAVSDMELSETETRSQRKVGGGSAQPCDSIVVAYYFCGEPIPYRTLVRGRAVTLGQFKELLTKKGSYRYYFKKVSDEFDCGVVFEEVREDEAVLPVFEEKIIGKVEKVD
Protein: Uncharacterized protein YdeI (P31130)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Protein YdeJ
Sequence:
MKFQAIVLASFLVMPYALADDQGGLKQDAAPPPPHAIEDGYRGTDDAKKMTVDFAKTMHDGASVSLRGNLISHKGEDRYVFRDKSGEINVVIPAAVFDGREVQPDQMINISGSLDKKSAPAVVRVTHLQK
Protein: Zinc finger protein 143 (SPH-binding factor) (Selenocysteine tRNA gene transcription-activating factor) (hStaf) (P52747)
Organism: Homo sapiens (Human)
Function: Transcriptional activator. Activates the gene for selenocysteine tRNA (tRNAsec). Binds to the SPH motif of small nuclear RNA (snRNA) gene promoters. Participates in efficient U6 RNA polymerase III transcription via its interaction with CHD8.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Homeobox protein SIX5
- T-complex protein 11 homolog
- POU domain, class 2, transcription factor 1
- Chromodomain-helicase-DNA-binding protein 8
- THAP domain-containing protein 11
- Transcription factor Sp1
- Double-strand-break repair protein rad21 homolog
- Transcriptional repressor CTCF
- Structural maintenance of chromosomes protein 3
- TATA-box-binding protein
Sequence:
MLLAQINRDSQGMTEFPGGGMEAQHVTLCLTEAVTVADGDNLENMEGVSLQAVTLADGSTAYIQHNSKDAKLIDGQVIQLEDGSAAYVQHVPIPKSTGDSLRLEDGQAVQLEDGTTAFIHHTSKDSYDQSALQAVQLEDGTTAYIHHAVQVPQSDTILAIQADGTVAGLHTGDATIDPDTISALEQYAAKVSIDGSESVAGTGMIGENEQEKKMQIVLQGHATRVTAKSQQSGEKAFRCEYDGCGKLYTTAHHLKVHERSHTGDRPYQCEHAGCGKAFATGYGLKSHVRTHTGEKPYRCSEDNCTKSFKTSGDLQKHIRTHTGERPFKCPFEGCGRSFTTSNIRKVHVRTHTGERPYYCTEPGCGRAFASATNYKNHVRIHTGEKPYVCTVPGCDKRFTEYSSLYKHHVVHTHSKPYNCNHCGKTYKQISTLAMHKRTAHNDTEPIEEEQEAFFEPPPGQGEDVLKGSQITYVTGVEGDDVVSTQVATVTQSGLSQQVTLISQDGTQHVNISQADMQAIGNTITMVTQDGTPITVPAHDAVISSAGTHSVAMVTAEGTEGEQVAIVAQDLAAFHTASSEMGHQQHSHHLVTTETRPLTLVATSNGTQIAVQLGEQPSLEEAIRIASRIQQGETPGLDD
Protein: Stellate supressor protein (Q24541)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MIHARYIRSERGVNDMHRKYMRGDFESCPNISCNRKNTLPVGLRSTAHAVKTTSILKLIHSHVRAQLSGHLLNAAAELETAPGQPTSLCFRLHQKALMPLKSPKSSPKNIKYSSS
Protein: Histone-binding protein RBBP4 N-terminal domain-containing protein (Q385S1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Histone deacetylase 2
- Histone deacetylase
- Histone H4
- Histone H4
- Histone H3 variant
- Histone H3, putative
- Histone H2A
- Chromatin assembly factor 1 subunit B, putative
- DNA damage-binding protein 1
Sequence:
MRKALVEPHEGGEALPIKESSPSSSVAATGVGEGSYQETKRYRTWRKHTRDLYQRLTHIDLVWESPAVRLMPFSTSKPGLLTRTLLCCTRACNGDQSYLQLLSVTTPSCAESLDATYSTYCEATGEVGGYGMAPSAVGLRIERSILHDGEPLTARYMHANPLIIASGSKDGNAYVFDWSRISLNKFPNDPPRPRAPLPPNEPSEGDTGEERALYNKRMSALQAVVREQDRWDKRHGEGQHLLTLTGGNGPCGALDWSTTTDGTVAAGSLGRICVWQIANMSKDDPRVVSCVQKYTIENESRVNEVSFSWMEPTSFVASVESGAVLRGDIRDPQLSQLFRLEVPATSSSVSPLDGTSLLVGSEEGEAFYYDLRYTLHPVMTVELHEGAISSAQWCPHSRHLFCTGGEGDAMCCVYNVTANRLLFKHAGHVENVTDVSWDWQEGCEGQLVSADAWSVMLWRPRDIFYTS
Protein: Kinesin-II 95 kDa subunit (KRP-85/95 95 kDa subunit) (P46871)
Organism: Strongylocentrotus purpuratus (Purple sea urchin)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305}.
Interaction partners:
- Kinesin-associated protein 3
- Uncharacterized protein.
- Uncharacterized protein.
- Kinesin light chain
- WD_REPEATS_REGION domain-containing protein.
- Kinesin heavy chain
- Kinesin-II 85 kDa subunit
Sequence:
MSKKSAETVKVVVRCRPMNSKEISQGHKRIVEMDNKRGLVEVTNPKGPPGEPNKSFTFDTVYDWNSKQIDLYDETFRSLVESVLQGFNGTIFAYGQTGTGKTFTMEGVRSNPELRGVIPNSFEHIFTHIARTQNQQFLVRASYLEIYQEEIRDLLAKDQKKRLDLKERPDTGVYVKDLSSFVTKSVKEIEHVMTVGNNNRSVGSTNMNEHSSRSHAIFIITIECSELGVDGENHIRVGKLNLVDLAGSERQAKTGATGDRLKEATKINLSLSALGNVISALVDGKSSHIPYRDSKLTRLLQDSLGGNAKTVMVANMGPASYNFDETITTLRYANRAKNIKNKPKINEDPKDALLREFQEEISRLKQALDKKGPSDGRKKGKKRKPGEQGGDDDIEDETEEEGDEMDEEEMYKESQQKLEEEKEKIMANQSMIAEEKQKLLSEVQKRQGEIKKEHQQKEMLEGKIKAMESKLLVGGKSIVDHTNEQQRKIEEQRLLLAEEKNRERDMERKLKEQDDKTVEIEGTFSSLQQEVEVKTKKLKKLFAKLQSYKSDIQDLQDEHARERQELEQTQNELIRELKLKKVIADNFIPVEERTKITTRAVFDEETEEWLLTPLAKAEGPSQMAKRPVSAVGNRRPIADYARMAAQMGGNPRYKAENILSVDLDMPNRTTRDYEGPSVAPRVQAALDAALQDEDDLDLEVQPEVFKAKTKLKKDKVRSKHKAVAKPGSNSQLYPQARGLIQK
Protein: Sisters on the loose, isoform B (A0A0S0WFC5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSDDWDDEPIVDTRGARGGDWSDDEDTAKSFSGEAEGDGVGGSGGEGGGYQGGNRDVFGRIGGGRGGGAGGYRGGNRDGGGFHGGRREGERDFRGGEGGFRGGQGGSRGGQGGSRGGQGGFRGGEGGFRGRLYENEDAKELPPIPSSCDKDEVGAFIDQLDLSKYTTSLALIRKLRDYLLTAFKALVNQAWASLEKLAQEKRAQKAHQIRETTDMMNRLMEDMGRLIREGEHEEANGIGMGFQSIDADCRADLSQWRNLQQVVMPQSSEIRDGQTNRTSGTEGGRSGGLTDGDDLTEIQSAAYAVYHQVLDRGYQTGRRLYDDNQGALREDSIPTEDREHPENNQVDGSTYGVTRFLHWLSENFVTRHEIRAVRFGSPHMVFQSYDWPESPKQHISTVHQKGIFYSQPLIRTRIIATVASEPNNSSSGQLSSMVNLARHQRSQNQETPDGIYVSRYNATGDEETPCSATGVPGRVVALRASSTPNEHRSDPGLSFIPNLTYEDGTIPSLAAGGAASTPLAPSLPAEHSLGLEMDSNTLVVPADADETRLVGHPGSTVVRSRLGGPPASTPLLSFRPRLPVIDEEHHLRFTRVSRELQMSVAFPPEETTLSEQREWGSIFRPRDEMVNYAEGPPPRQTQRARRRSRTRRRRNRIASAASPQLTPERIVRREEAFQSSRHIAATFMSSLLQNAAGEVTTSSGLAVTRSVKEITTSVHITRNVLQEEVPPTTEATTTSLEVAQATGYSDSGACMQSAAFSQDLPVVAPLEISGNASSDQASFDQALALLPPINSTPIGQHPIAVFGPKTEIEIKPQKMDISNMMNTSVPPMPMEVDEVPLEVSNTLANMSDHAYVTDIQILPSLQLNSLNLVSTNITDNAVNIAPSTSTNDLQTPSDRRTSMQNQLYRVSMNDLAYISQHANVVRLMVDRQEELGAQVSSLGPFKENSQGALNFSTMPAVKVYDPRIIQNIQKDKMRVVHGLFGALIRQSQVDMHNAPFIRNRKDALMAYRFLLELKTANIISLSSDGRFFGLL
Protein: Iron-sulfur cluster biogenesis chaperone, mitochondrial (EC 3.6.4.10) (Heat shock 70 kDa protein) (Q5B0C0)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Required for the assembly of iron-sulfur (Fe/S) clusters in mitochondria (By similarity). Assisted by the DnaJ-like co-chaperone jac1 and the nucleotide exchange factor mge1, it mediates ATP-dependent Fe-S cluster transfer from the scaffold proteins isu1/isu2 to grx5 (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P0CS90}.
Interaction partners:
- Heat shock protein 60
- GrpE protein homolog
- DnaJ homolog 1
- Mitochondrial import inner membrane translocase subunit TIM44
- Nucleoporin NSP1
- Mitochondrial import inner membrane translocase subunit tim14
- Mitochondrial import inner membrane translocase subunit tim-17
- Cytochrome c oxidase subunit 4, mitochondrial
- Mitochondrial import inner membrane translocase subunit TIM23, putative
- Heat shock protein
Sequence:
MLSSRLSRALPRTAPFARAPAFRLPSTAARRWNSTEEKVKGQVIGIDLGTTNSAVAVMEGKTPKIIENAEGARTTPSVVAFAQDGERLVGIAAKRQAVVNPENTLFATKRLIGRKFTDAEVQRDIKEVPYKIVQHTNGDAWVEARGEKYSPAQIGGFVLGKMKETAENYLSKPVKNAVVTVPAYFNDSQRQATKDAGQIAGLNVLRVVNEPTAAALAYGLEKEADRVVAVYDLGGGTFDISVLEIQKGVFEVKSTNGDTHLGGEDFDISLVRHIVQQFKKESGLDLSNDRMAIQRIREAAEKAKIELSSSLQTEINLPFITADASGAKHINLKMTRAQLESLVEPLISRTVDPVRKALKDANLQSSEVQDIILVGGMTRMPKVTESVKSLFGREPAKSVNPDEAVAIGAAIQGAVLAGEVTDVLLLDVTPLSLGIETLGGVFTRLINRNTTIPTKKSQTFSTAADFQTAVEIKVFQGERELVKDNKLLGNFQLVGIPPAHRGVPQIEVTFDIDADSIVHVHAKDKSTNKDQSITIASGSGLSDAEIQSMVEDAEKYGAQDKERKAAIEAANRADSVLNDTEKALKEFEDRLDKAEAEQIREKINTLREFVAKNQSGEVAATAEELKQKTDELQTASLTLFDKMHKAQSEQQQQPNQGETGQGENKP