wanglab/gogpt-training-data huggingface dataset:
Protein: ADP-ribosylhydrolase ARH3 (ADP-ribose glycohydrolase ARH3) (ADP-ribosylhydrolase 3) (O-acetyl-ADP-ribose deacetylase ARH3) (EC 3.5.1.-) (Poly(ADP-ribose) glycohydrolase ARH3) (EC 3.2.1.143) ([Protein ADP-ribosylarginine] hydrolase-like protein 2) ([Protein ADP-ribosylserine] hydrolase) (EC 3.2.2.-) (Q9NX46)
Organism: Homo sapiens (Human)
Function: ADP-ribosylhydrolase that preferentially hydrolyzes the scissile alpha-O-linkage attached to the anomeric C1'' position of ADP-ribose and acts on different substrates, such as proteins ADP-ribosylated on serine and threonine, free poly(ADP-ribose) and O-acetyl-ADP-D-ribose. Specifically acts as a serine mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to serine residues on proteins, thereby playing a key role in DNA damage response. Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage. Does not hydrolyze ADP-ribosyl-arginine, -cysteine, -diphthamide, or -asparagine bonds. Also able to degrade protein free poly(ADP-ribose), which is synthesized in response to DNA damage: free poly(ADP-ribose) acts as a potent cell death signal and its degradation by ADPRHL2 protects cells from poly(ADP-ribose)-dependent cell death, a process named parthanatos. Also hydrolyzes free poly(ADP-ribose) in mitochondria. Specifically digests O-acetyl-ADP-D-ribose, a product of deacetylation reactions catalyzed by sirtuins. Specifically degrades 1''-O-acetyl-ADP-D-ribose isomer, rather than 2''-O-acetyl-ADP-D-ribose or 3''-O-acetyl-ADP-D-ribose isomers.
Subcellular location: Nucleus {ECO:0000269|PubMed:17991898, ECO:0000269|PubMed:34479984}. Cytoplasm {ECO:0000269|PubMed:16278211, ECO:0000269|PubMed:34479984}. Chromosome {ECO:0000269|PubMed:30045870}. Mitochondrion matrix {ECO:0000269|PubMed:17991898, ECO:0000269|PubMed:34479984, ECO:0000305|PubMed:22433848}. Note=Recruited to DNA lesion regions following DNA damage; ADP-D-ribose-recognition is required for recruitment to DNA damage sites. {ECO:0000269|PubMed:30045870}.
Interaction partners:
- Poly
- Poly [ADP-ribose] polymerase 1
- ADP-ribose glycohydrolase MACROD1
- ADP-ribose glycohydrolase MACROD2
- ADP-ribose glycohydrolase OARD1
- Histone PARylation factor 1
- U8 snoRNA-decapping enzyme
Sequence:
MAAAAMAAAAGGGAGAARSLSRFRGCLAGALLGDCVGSFYEAHDTVDLTSVLRHVQSLEPDPGTPGSERTEALYYTDDTAMARALVQSLLAKEAFDEVDMAHRFAQEYKKDPDRGYGAGVVTVFKKLLNPKCRDVFEPARAQFNGKGSYGNGGAMRVAGISLAYSSVQDVQKFARLSAQLTHASSLGYNGAILQALAVHLALQGESSSEHFLKQLLGHMEDLEGDAQSVLDARELGMEERPYSSRLKKIGELLDQASVTREEVVSELGNGIAAFESVPTAIYCFLRCMEPDPEIPSAFNSLQRTLIYSISLGGDTDTIATMAGAIAGAYYGMDQVPESWQQSCEGYEETDILAQSLHRVFQKS
Protein: General transcription factor 3C polypeptide 4 (EC 2.3.1.48) (TF3C-delta) (Transcription factor IIIC 90 kDa subunit) (TFIIIC 90 kDa subunit) (TFIIIC90) (Transcription factor IIIC subunit delta) (Q9UKN8)
Organism: Homo sapiens (Human)
Function: Essential for RNA polymerase III to make a number of small nuclear and cytoplasmic RNAs, including 5S RNA, tRNA, and adenovirus-associated (VA) RNA of both cellular and viral origin. Has histone acetyltransferase activity (HAT) with unique specificity for free and nucleosomal H3. May cooperate with GTF3C5 in facilitating the recruitment of TFIIIB and RNA polymerase through direct interactions with BRF1, POLR3C and POLR3F. May be localized close to the A box.
Subcellular location: Nucleus.
Interaction partners:
- General transcription factor 3C polypeptide 5
- General transcription factor 3C polypeptide 1
- General transcription factor 3C polypeptide 3
- General transcription factor 3C polypeptide 6
- General transcription factor 3C polypeptide 2
- Transcription factor IIIB 90 kDa subunit
- DNA-directed RNA polymerase III subunit RPC3
- DNA-directed RNA polymerase III subunit RPC6
- DNA-directed RNA polymerase III subunit RPC1
- Transcription factor TFIIIB component B'' homolog
Sequence:
MNTADQARVGPADDGPAPSGEEEGEGGGEAGGKEPAADAAPGPSAAFRLMVTRREPAVKLQYAVSGLEPLAWSEDHRVSVSTARSIAVLELICDVHNPGQDLVIHRTSVPAPLNSCLLKVGSKTEVAECKEKFAASKDPTVSQTFMLDRVFNPEGKALPPMRGFKYTSWSPMGCDANGRCLLAALTMDNRLTIQANLNRLQWVQLVDLTEIYGERLYETSYRLSKNEAPEGNLGDFAEFQRRHSMQTPVRMEWSGICTTQQVKHNNECRDVGSVLLAVLFENGNIAVWQFQLPFVGKESISSCNTIESGITSPSVLFWWEYEHNNRKMSGLIVGSAFGPIKILPVNLKAVKGYFTLRQPVILWKEMDQLPVHSIKCVPLYHPYQKCSCSLVVAARGSYVFWCLLLISKAGLNVHNSHVTGLHSLPIVSMTADKQNGTVYTCSSDGKVRQLIPIFTDVALKFEHQLIKLSDVFGSVRTHGIAVSPCGAYLAIITTEGMINGLHPVNKNYQVQFVTLKTFEEAAAQLLESSVQNLFKQVDLIDLVRWKILKDKHIPQFLQEALEKKIESSGVTYFWRFKLFLLRILYQSMQKTPSEALWKPTHEDSKILLVDSPGMGNADDEQQEEGTSSKQVVKQGLQERSKEGDVEEPTDDSLPTTGDAGGREPMEEKLLEIQGKIEAVEMHLTREHMKRVLGEVYLHTWITENTSIPTRGLCNFLMSDEEYDDRTARVLIGHISKKMNKQTFPEHCSLCKEILPFTDRKQAVCSNGHIWLRCFLTYQSCQSLIYRRCLLHDSIARHPAPEDPDWIKRLLQSPCPFCDSPVF
Protein: Putative uncharacterized protein VPS61 (Q03913)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized protein VPS63
- Putative uncharacterized protein YOR041C
- Signal peptidase complex subunit 2
Sequence:
MYRFCAHAYLLLKYEKYHNQNQQLKKLWASFRCLFRLAAFALPRRYQSFFEAELILKNSTLETRLTLYRRLRSRLRLKNKNYTRSSSIMFNIQTTFPPHGEMKTFIVLREVDLLLLSLEFMNVSLARADLLVRNLHYFAIHSTLVMLHQYEYIYLMLTSGFCRYLGVCFFMIIQKYVTPGVMLGRWKVTA
Protein: (+)-3-carene synthase 2, chloroplastic (EC 4.2.3.107) (Terpene synthase (+)3car2) (PbTPS-(+)3car2) (R9QMR6)
Organism: Pinus banksiana (Jack pine) (Pinus divaricata)
Function: Monoterpene synthase (TPS) involved in the biosynthesis of monoterpene natural products included in conifer oleoresin secretions and volatile emissions; these compounds contribute to biotic and abiotic stress defense against herbivores and pathogens. Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) to (+)-3-carene.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
Sequence:
MSLISAVPLASSCVSKSLISSVREHTALRRAIATLQMSRRGKSVAASIRMSSATAGSDDGVKRRIGDYHSNLWDDNFIQSLSSPYGASSYGEHADRLIGEVKEIFNSFSIADGELISPVNDLLQQLWMVDNVERLGIDRHFQTEIKVALDYVYRYWSEEGIGCGRDSAFTDLNTTALAFRIFRLHGYTVSSDVFEHFKDQKGQFAASANDTELQTRSVFNLFRASLIAFPEEKVLEEAEKFAAAYLKAALQTLPVSGLSREIQYVFDYRWHSNLPRLEARSYIDILADNTISGTPDANTKKLLELAKLEFNIFHSVQQKELQCLWRWWKEWGCPELTFIRHRYVEFYTLVSGIDMVPEHATFRLSCVKTCHLITILDDMYDTFGTIDELRLFTAAVKRWDPSATECLPEYMKGVYMVLYETVNEMAKEAQKSQRRDTLGYVRQALEDYIGSYLKEAEWIATGYVPTFQEYFENGKLSSGHRIATLQPILTLSIPFPHHILQEIDFPSKFNDYAASILRLRGDTRCYKADSARGEEASCISCYMRDNPGSTQEDALNLINGMIEDMIKKLNWEFLRPDNNAPISSKKHAFNISRGLHHFYNYRDGYSVASKETKDLVIKTVLEPVLM
Protein: Probable 3',5'-cyclic-AMP phosphodiesterase pde-4 (EC 3.1.4.53) (Q22000)
Organism: Caenorhabditis elegans
Function: Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes (By similarity). Antagonizes dorsal D (DD) motor neuron respecification by reducing levels of cAMP.
Interaction partners:
- adenylate cyclase
- cAMP-dependent protein kinase catalytic subunit
- Adenosine kinase
- Probable 3',5'-cyclic phosphodiesterase pde-6
- Adenylate kinase
- AMP deaminase
- Adenine phosphoribosyltransferase
- Probable adenylate kinase isoenzyme ZK673.2
- cAMP-dependent protein kinase regulatory subunit
- Adenylate kinase isoenzyme 1
Sequence:
MPRRRGSSSSSSAAGGSGGGGGFGFSSLRRELHLHNFFRTSSPSASSTSRTPPAALPPRTSAVTIPGSNHKLTSSASSYHPPRELTVSTFSAGSATAADGLGGAHLTPSLSSSVHARRESFLYRASDDLREASSLRPVSRASSIASNEHGHGDDLIVTPFAQLLASLRNVRSNLISITNIQNSDDSRHANRSAKRPPLHNIELPDDVVHCAHDTLEELDWCLDQLETIQTHRSVSEMASSKFRKMLNKELSHFAESSKSGTQVSKFLITTYMDKEEDEPSIEIEVPTEVQGPSTSGPMTLSILKKAQTAAMNKISGVRKLRAPSHDGHVPEYGVNCAREIAVHMQRLDDWGPDVFKIDELSKNHSLTVVTFSLLRQRNLFKTFEIHQSTLVTYLLNLEHHYRNNHYHNFIHAADVAQSMHVLLMSPVLTEVFTDLEVLAAIFAGAVHDVDHPGFTNQYLINSNNELAIMYNDESVLEQHHLAVAFKLLQDSNCDFLANLSRKQRLQFRKIVIDMVLATDMSKHMSLLADLKTMVEAKKVAGNNVIVLDKYNDKIQVLQSMIHLADLSNPTKPIELYQQWNQRIMEEYWRQGDKEKELGLEISPMCDRGNVTIEKSQVGFIDYIVHPLYETWADLVYPDAQNILDQLEENREWYQSRIPEEPDTARTVTEDDEHK
Protein: Cellular retinoic acid-binding protein 1 (Cellular retinoic acid-binding protein I) (CRABP-I) (P62965)
Organism: Mus musculus (Mouse)
Function: Cytosolic CRABPs may regulate the access of retinoic acid to the nuclear retinoic acid receptors.
Subcellular location: Cytoplasm.
Interaction partners:
- Cytochrome P450 26A1
- Retinoic acid receptor beta
- Cytochrome P450 26B1
Sequence:
MPNFAGTWKMRSSENFDELLKALGVNAMLRKVAVAAASKPHVEIRQDGDQFYIKTSTTVRTTEINFKVGEGFEEETVDGRKCRSLPTWENENKIHCTQTLLEGDGPKTYWTRELANDELILTFGADDVVCTRIYVRE
Protein: Uncharacterized protein (Q2YKV5)
Organism: Brucella abortus (strain 2308)
Interaction partners:
- Secreted protein
Sequence:
MVRNDLNWMMETTLTSQQWLPVELLNIGLAAAVFFACLVHSLWKAVFDELNPVFWRRTAALLWAGVVIVALTGGMDTFNWPQALGWLLVAGGVCATVWRAGMGYYRQYCAHNSHGFHARRTRLSSGR
Protein: Translation machinery-associated protein 17 (ATPase-dedicated chaperone of 17 kDa) (ADC17) (Q12513)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: ATPase-dedicated chaperone that assists the formation of the RPT6-RPT3 ATPase pair, an early step in proteasome assembly. Plays a key role in maintaining homeostatic proteasome levels and adjusting proteasome assembly when demands increase, such as during proteasome stresses. Function overlaps with RPN14.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Fatty acid synthase subunit alpha reductase
- Fatty acid synthase subunit beta dehydratase; Enoyl-[acyl-carrier-protein] reductase; [Acyl-carrier-protein] acetyltransferase; [Acyl-carrier-protein] malonyltransferase; S-acyl fatty acid synthase thioesterase]
- S-formylglutathione hydrolase
- 26S proteasome regulatory subunit RPN14
- Probable 26S proteasome regulatory subunit p28
- DNA mismatch repair protein HSM3
- 26S proteasome regulatory subunit 6B homolog
- 26S proteasome regulatory subunit 8 homolog
- 26S proteasome subunit RPT4
- Probable 26S proteasome regulatory subunit p27
Sequence:
MCSAGGIRRPIQIEEFKTAISGMSDMELAQIKTEIENSINHLQRSNARLGKYIAKLEGADDRLEADDSDDLENIDSGDLALYKDSVRENEIVLNNYNERVDALEQETVYRKTGHGKSKHEVEAKDNTNKGPDVDMDNSNVDVVTPNSIFI
Protein: Ribosomal RNA small subunit methyltransferase NEP1 (EC 2.1.1.-) (18S rRNA (pseudouridine(1248)-N1)-methyltransferase) (18S rRNA Psi1248 methyltransferase) (Nucleolar protein EMG1 homolog) (Protein C2f) (Ribosome biogenesis protein NEP1) (Q92979)
Organism: Homo sapiens (Human)
Function: S-adenosyl-L-methionine-dependent pseudouridine N(1)-methyltransferase that methylates pseudouridine at position 1248 (Psi1248) in 18S rRNA. Involved the biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi) conserved in eukaryotic 18S rRNA. Is not able to methylate uridine at this position. Has also an essential role in 40S ribosomal subunit biogenesis independent on its methyltransferase activity, facilitating the incorporation of ribosomal protein S19 during the formation of pre-ribosomes (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:11935223, ECO:0000269|PubMed:34516797}.
Interaction partners:
- Bystin
- KRR1 small subunit processome component homolog
- Nucleolar complex protein 4 homolog
- Nucleolar protein 58
- Nucleolar protein 14
- rRNA-processing protein FCF1 homolog
- WD repeat-containing protein 46
- U3 small nucleolar RNA-associated protein 4 homolog
- HEAT repeat-containing protein 1
- U3 small nucleolar RNA-associated protein 6 homolog
Sequence:
MAAPSDGFKPRERSGGEQAQDWDALPPKRPRLGAGNKIGGRRLIVVLEGASLETVKVGKTYELLNCDKHKSILLKNGRDPGEARPDITHQSLLMLMDSPLNRAGLLQVYIHTQKNVLIEVNPQTRIPRTFDRFCGLMVQLLHKLSVRAADGPQKLLKVIKNPVSDHFPVGCMKVGTSFSIPVVSDVRELVPSSDPIVFVVGAFAHGKVSVEYTEKMVSISNYPLSAALTCAKLTTAFEEVWGVI
Protein: Serine-arginine repetitive matrix 2/3/4, isoform F (A8JNI2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Cell division cycle 5, isoform A
- 116 kDa U5 small nuclear ribonucleoprotein component
- U5 small nuclear ribonucleoprotein 200 kDa helicase
- Pre-mRNA-processing factor 17
- Protein BUD31 homolog
- Pre-mRNA-processing-splicing factor 8
- Pre-mRNA-processing factor 19
- Serine/arginine repetitive matrix protein 1
- Probable U2 small nuclear ribonucleoprotein A'
- Cwc25
Sequence:
MYNGIGLTTPRGSGTNGHVQRNWACVRPGKKDKDYRAEDDTKKLDAQLNRPPNKEILDHDRKRKIEVKCLELEDILEKQGRTPEEIKSQVDSFRQKLMGQGKTDLAKDEFGRVANTTTSTATAAVRTTATASAATASTMTTTTEATTVKVAKPKKRRKRRKRAGHAITTTTTEKSAAISTPGSKTSSPRTQTGEPASSAPSATSNGARKTKAPYFQHDNREYLAKYESFRLTAHTWNYAAVARKFKPLRPALASGANKTRRPAVSKRTHPDCACACQQKDPEPALEPAHRTAEHSIQKELPSSQMKINIDGSVLLELLKYSSSSLLGTLLGAGSAVATSARDTHQIAEAQQQKNARLREAFNISEYFVEGSSFDGDRKAKEDLAKSVALQKELDAQRESLAAAAAAAAAGKDKETGKRYALVRTPSRERDRDAGDAAANGDERDHVSKTDKKKRKKRARESSASPERKKKKKSKKHKKESKSKKKRSRKRKHSESGRDSDRDSDEEDDSSEEERRESKNVRKKAKKDKKKRDKKLKKKSRARASSSDSERTNSPSRKENKSDRSRGAKASKSDEKAPQQENVMRSRSRERKDTRSSRPLEASIDSRQRKPRERSAATPPRKEPERHRERSKDRQRSKEKHRSRDRLRSRERQRSRERQRSRERQRSKERQRSKERQRSIERQRSKERQRSKERQRSRSKDALRCKEKPQCNEKERSRERRRSKSKDRQRSKEKHRPKDEQQSVDKRRDRSTDRSKENQRSNERQRSKERQRSKERERSKDRQRSRERRRSKEGQLSKDRQGLKERQRSNERKRSKERQPSKEKQRSRERQRSREPLQSKDRQRSKERQRSRERPAKEARPTRSPRERSSKSRDDRRHRSPTNASRKQKDDTKLSRNARFKSPAHSPEAPPKKSVPTPAFNPFKAAEDTVNDILGTKSVMVALEQTKRQRAASSSSSDSDSSGSSSTSSRTPSPKPTPRKQKKRSKTPELKEVKKEISPRKESRVSVKREQSNSPQKSKSKSKVDESSPKRTSRRSRSISSELRYSPAERHPERYHDIVQDKKRPSKVREAHSTKPAPVVRLRAQSDDGSDAETGVDGAALEEFQQSRREREEQQELRMLEQLKSGIAAKAKQKIKIMEKDPAKEGSEVSGSDQVTATKRNSLSEFLVANNVTALINTLTTTTVTLTTTPPPPLAVVVPLEQRQEQPQQRDPDRELSVPVEDTVKKRDTSTPPICKTPQVTANGDAKSPTLVHKNHVHHNRPPPQHMHHHSQQQQHHQHPPGKRIFHNRTLNNNPNSRHSTNNPHACGGGGVPHSNSNSSNSGGNNNNAAMLPFLAGTPGTYNRTTNRLNHGPLLTATHYNICKNHQHSLQQQQAHHLARGLVYNSALFGHGQRHPGLLSLTGAGVGMSGPGAPLLGHPSHVRGGGGPISFNAAAAAAAVAANSISYLHHHHQHQQKPKIVIKPFKIHDPQPLVAALADSSLVDAIVSKVSTATVAAAESAARRSRSRERRSRSKRRTSTSHHRHDSSSESRSRYSSSSSRSGSHSSRSGSHSSRTSCSTNSSSGSSSSGSGSGSSQSGSRSPSIPRRRGSPSFLDRRRITSARKRPIPYHHKANAEGEVEDASSCCSSCFSRASSPATPLLTPLRNSRSPSMAAF
Protein: Kinetochore-associated protein MTW1 (Mis12-like protein) (P39731)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acts as essential component of the kinetochore MIND complex, which is required for the spindle checkpoint and kinetochore integrity. MIND plays a role in establishing a bipolar spindle-kinetochore interaction by joining kinetochore subunits contacting DNA to those contacting microtubules.
Subcellular location: Chromosome, centromere, kinetochore {ECO:0000269|PubMed:14602074, ECO:0000269|PubMed:14657030}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:12455957}. Note=Associated with the kinetochore. {ECO:0000269|PubMed:14602074, ECO:0000269|PubMed:14657030}.
Interaction partners:
- Kinetochore-associated protein NSL1
- Kinetochore-associated protein DSN1
- Kinetochore-associated protein NNF1
- Inner kinetochore subunit AME1
- Inner kinetochore subunit CTF19
- Kinetochore protein SPC24
- Outer kinetochore KNL1 complex subunit SPC105
- Histone H3-like centromeric protein CSE4
- Inner kinetochore subunit OKP1
- Kinetochore protein SPC25
Sequence:
MSAPTMRSTSILTEHLGYPPISLVDDIINAVNEIMYKCTAAMEKYLLSKSKIGEEDYGEEIKSGVAKLESLLENSVDKNFDKLELYVLRNVLRIPEEYLDANVFRLENQKDLVIVDENELKKSEEKLREKVNDVELAFKKNEMLLKRVTKVKRLLFTIRGFKQKLNELLKCKDDVQLQKILESLKPIDDTMTLLTDSLRKLYVDSESTSSTEEVEALLQRLKTNGKQNNKDFRTRYIDIRTNNVLRKLGLLGDKEDEKQSAKPDARTQAGDIVSIDIEEPQLDLLDDVL
Protein: Probable hydroxyacylglutathione hydrolase SPCC13B11.03c (EC 3.1.2.6) (Glyoxalase II) (Glx II) (O94250)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Lactoylglutathione lyase
- Glutathione-independent glyoxalase hsp3101
- Glutathione-independent glyoxalase hsp3102
- Putative glutathione-independent glyoxalase hsp3105
- Putative D-lactate dehydrogenase C713.03, mitochondrial
- Probable glutathione-independent glyoxalase hsp3103
- Probable glutathione-independent glyoxalase hsp3104
- Glutathione-independent glyoxalase DJ-1
- 2-hydroxyacid dehydrogenase homolog 2
- Probable hydroxyacylglutathione hydrolase glo2
Sequence:
MSFQILPIPMWVGTQDNYAYLLLCEETRQAAIVDPAEVNVVMPILKKKLKNKEIDLQAILTTHHHADHSGGNLNLKKEFPHVTIYGGSDQNGVSHVLQDKETLRIGNVQIEALHTPCHTRDSICFYAHSSNEHAVFTGDTLFNAGCGRFFEGTAAEMHIALNAVLSSLPNNTVIYPGHEYTKSNVKFASKHLQSEALNHLEGLCNHNQFIAGHITMGQEKQFNPFMRVTDPELQKHLGLNDPIKVMDELRTLKNQG
Protein: Succinyl-CoA:3-ketoacid-coenzyme A transferase (EC 2.8.3.5) (G8BJM6)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Interaction partners:
- acetyl-CoA C-acetyltransferase
- Acetyl-CoA C-acyltransferase
- acetyl-CoA C-acyltransferase
- acetyl-CoA C-acyltransferase
- Hydroxymethylglutaryl-CoA synthase
- Oleate-induced peroxisomal protein POX18
- Urea amidolyase
- Uncharacterized protein
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- 3-hydroxyisobutyryl-CoA hydrolase
Sequence:
MLSVFNKHKVTTVVQCFVRCYSLVHPKSKVVYSTDEALEGITSNVTLLSGGFGLSGVPDTIINALVKKPEIKNITAVSNNAGLDGRGLSQLLVTGQITKMISSYIGGNRTFEKLYLTGAIDLELTPQGNLAERVRAGAAGIPAFYSPTGVGTWLEEGKLPVRYDSTGEKVLKASQAREVREFNGKKYLLEPAIFGDVALVKAYKADTLGNCWFRGAARNFNSVMGRNAKLTIVEAENIVEPGEITPEDVHLPAIYVDRVIQSTTPKDIEIFKYSETSQDPSLEEPKSESELKRSKIVKRAAQEFKDGSFANLGIGMPTLAPNYLPESINVTLQSENGILGLGPYPHKGQEDPDLINAGKETVTLAPGASLFGSEESFAMIRSGKIDLTILGGLQVAANGDLANWGLPGRVKGMGGAMDLVSNPQNTRVVVVMEHVDRKGRPKILPQCQFPLTGQKCVSRIITDLAVFDIVDEKLVLIEYDPESSIEEIKAKTGAPFEISPDLKPIEV
Protein: Aldolase vrtJ (EC 4.1.2.-) (Viridicatumtoxin synthesis protein J) (D7PHZ0)
Organism: Penicillium aethiopicum
Function: Aldolase; part of the gene cluster that mediates the biosynthesis of viridicatumtoxin, a tetracycline-like fungal meroterpenoid with a unique, fused spirobicyclic ring system. The first step of the pathway is the production of the malonamoyl-CoA starter unit for the polyketide synthase vrtA. The aldolase vrtJ may be involved in the synthesis of the malonamate substrate for malonamoyl-CoA synthetase vrtB. The polyketide synthase vrtA then may utilize the malonamoyl-CoA starter unit, followed by sequential condensation of eight malonyl-CoA units to form the polyketide backbone. The cyclization of the last ring could be mediated by the lactamase-like protein vrtG. The proposed post-PKS tailoring steps are an hydroxylation at C5 catalyzed the cytochrome P450 monooxygenase vrtE, a hydroxylation at C12a catalyzed by VrtH and/or VrtI, and an O-methylation by the O-methyltransferase vrtF. VrtC is then proposed to catalyze the transfer of a geranyl group synthesized by vrtD to the aromatic C ring of the tetracyclic polyketide intermediate of viridicatumtoxin to yield previridicatumtoxin. Finally, the cytochrome P450 monooxygenase vrtK catalyzes the spirocyclization of the geranyl moiety of previridicatumtoxin to afford viridicatumtoxin.
Interaction partners:
Sequence:
MTNSPIADLVHHPERVQSPSLVNSKMNGDAKAVTEWTEPGPAAFDFRSDTVTRPTEQMLAAIAATTLQDDDFRQDPTTLGLEAWMAELTGKAAGLFVVSGTMGNQLGVRAHLQSPPHSVLCDARSHLVTHEAGGVASLSGAMVSCVTPVNGRYMTQADLEAHVNRGTLITDCPTRLVVLEIPLGGVILPLDKCRRISEWARAQGIALHLDGARLWEAVAAGAGSLRDYCACFDSVSLCFSKGLGAPIGSVLVGSETLRERARWIRKSIGGGMRQAGVVCAAARVAVEATFLGGLLKRSHARARDIATFWEIHGGRLTYPTETNMVWLDLEAVGWTPERLIRRGAELGLRFMGARLVVHYQIGDEAIGRLQDLMLEILVSGLVDHPRDS
Protein: Transition protein-like 94D, isoform B (A0A0B4KHN9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGSVLSRSDQPRDSVAYRNFLTVYRNQHKQMSSNDALLSASREWGTLSQAQRNRYANMDSPKRGTKNITENAAARRKITKKNSRSKRISQRRIQDKGSAYKPLTLNRSYVIRKSLVPSRGFLNLVQFFQEIHSEMPRSLAVKEAVSSWCAMNADQRGIFISDL
Protein: ADP-ribosylation factor-binding protein GGA2 (Gamma-adaptin-related protein 2) (Golgi-localized, gamma ear-containing, ARF-binding protein 2) (Q6P5E6)
Organism: Mus musculus (Mouse)
Function: Plays a role in protein sorting and trafficking between the trans-Golgi network (TGN) and endosomes. Mediates the ARF-dependent recruitment of clathrin to the TGN and binds ubiquitinated proteins and membrane cargo molecules with a cytosolic acidic cluster-dileucine (DXXLL) motif. Mediates export of the GPCR receptor ADRA2B to the cell surface. Regulates retrograde transport of phosphorylated form of BACE1 from endosomes to the trans-Golgi network.
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q9UJY4}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9UJY4}. Endosome membrane {ECO:0000250|UniProtKB:Q9UJY4}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9UJY4}. Early endosome membrane {ECO:0000250|UniProtKB:Q9UJY4}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9UJY4}.
Interaction partners:
- ADP-ribosylation factor-binding protein GGA3
- ADP-ribosylation factor-binding protein GGA1
- Sortilin-related receptor
- Cation-independent mannose-6-phosphate receptor
- Rab GTPase-binding effector protein 1
- Sortilin
- Consortin
Sequence:
MAATAVAAGTGSPAGTESAEGGPGAAAALELWLNKATDPSMAEQDWSAIQKFCEQVNTDPSGPTHAPWLLAHKIQSPQEKEALYALTVLEICMNHCGEKFHSEVAKFRFLNELIKVLSPKYLGAWATEKVKGRVIEILFSWTVWFPEDIKIRDAYQMLKKQGIIKQDPKLPMDKILPPPSPWPKSIFDADEEKSKLLTRLLKSNHPEDLQAANRLIKNLVKEEQEKSEKVSRRVSAVEEVRSHVRVLREMLSMYRRPGHALPDQQALQVVYERCEKLRPTLFRLASDTTDDDDALAEILQANDLLTQGVRLYKQVVEGRVSAGNAVPAAVGAIPAPRAFPNPEPCGLNCPLIDLETPSLLHQDLAALGINDVPTRNQVVIPSCCNDKKQPGAITLMGGGIQSLSADRNLLDLFSPQPSPGLNYVPQKSIPKEVPPGTKASPGWSWEAGPLASSTASQNTPLAHVFVPLESVKPSSLPPIVVYDRNGFRILLHFSQTGAPGHPDVKVLLLTMMSTATQPVWDVMFQVAVPKSMRVKLQPASSSKLPAFSPLMPPAVISQTLLLDNPHKEPIRLRYKLTFNQGGQPFSEVGEVKDFPDLAVLSTA
Protein: Proteasome subunit alpha type-3 (Q27563)
Organism: Dictyostelium discoideum (Social amoeba)
Function: The proteasome is a multicatalytic proteinase complex which 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. The proteasome has an ATP-dependent proteolytic activity.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Proteasome subunit alpha type-4
- Proteasome subunit beta type-2
- Proteasome subunit beta type-6
- Proteasome subunit beta type-4
- Proteasome subunit alpha type-5
- Proteasome subunit alpha type-1
- Proteasome subunit alpha type-6
- Proteasome subunit beta type-5
- Proteasome subunit beta type-3
- Proteasome subunit alpha type-7
Sequence:
MSSVGSGYDLYVSTYSPDGKLFQVDYANKAVENSGTLVAIKAKDGVVLGVEKLVPSKMLCSGSNRRVHHIDTHVGVAIAGFLADARQLITRARSEAKNYKSTYGQPIPIKVLSQRIASYNHMHTLYGSVRPFGCSIAITGIDQYGPQLFLVEPSGSCVGYFGASLGKGKQAAKNELEKIKFSEMTCREAIKEVSRIIYSVHDEVKDKDFELELGWISTETNNVHQIVPKELHDEAEAYAKQSLEDANM
Protein: Lipoate-protein ligase A subunit 2 (EC 6.3.1.20) (C-terminal domain of LplA) (CTD) (Lipoate--protein ligase subunit 2) (Q9HKT2)
Organism: Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Function: Part of a lipoate-protein ligase complex that catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes. Can also use octanoate as substrate.
Interaction partners:
- Lipoate-protein ligase A subunit 1
- Probable glycine cleavage system H protein
- dihydrolipoyllysine-residue
- Probable 3-methyl-2-oxobutanoate dehydrogenase chain E1-beta
- Probable 3-methyl-2-oxobutanoate dehydrogenase alpha chain
Sequence:
MVLNYTMHMMYSKNWKAKKGLIRVTLDLDGNRIKDIHISGDFFMFPEDSINRLEDMLRGSSIEKINDIIRDFYNQGVITPGVEPEDFIQALRVI