wanglab/gogpt-training-data huggingface dataset:
Protein: DNA repair protein complementing XP-A cells homolog (Xeroderma pigmentosum group A-complementing protein homolog) (P27089)
Organism: Gallus gallus (Chicken)
Function: Involved in DNA excision repair. Initiates repair by binding to damaged sites with various affinities, depending on the photoproduct and the transcriptional state of the region (By similarity).
Subcellular location: Nucleus.
Interaction partners:
- ERCC4 domain-containing protein.
- General transcription and DNA repair factor IIH helicase/translocase subunit XPB
- Fanconi anemia group M protein
- RAD23 homolog B, nucleotide excision repair protein.
- Fanconi anemia core complex associated protein 24
- ERCC excision repair 6, chromatin remodeling factor.
- DNA damage-binding protein 1
- ERCC excision repair 5, endonuclease
- General transcription factor IIH subunit 5
- DNA damage-binding protein 2
Sequence:
MGRAAPGPDEGAEGERPSISATALARMERNRRRALALRQARLAARPYPQAAAGAGPPQGRDTGGGFFLEEEEEEEEQRRAAERIVHPPAPVLQFDYLICGDCGKEFMDSYLMQHFDWATCDNCRDAEDKHKLITRTEAKEEYLLKDCDLDKREPVLRFIVKKNPHNPRWGDMKLYLKLQVIKRALEVWGNEESLQEAKEQRRDSREKMKQKRFDKKVKELRRAVRSSLWKKTASIHEHEYGPEENVDEETYKKTCTVCGHELTYEKM
Protein: Prolactin-3B1 (Chorionic somatomammotropin hormone 2) (Placental lactogen II) (PL-II) (P09586)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted.
Interaction partners:
- Trophoblast-specific protein alpha
- Cathepsin Q
Sequence:
MKLSLSQPCSFSGALLLLAVSNLLVWEKVTSLPNYRLPTESLYQRVIVVSHNAHDLASKAFMEFEMKFGRTAWTYGLMLSPCHTAAILTPENSEQVHQTTSEDLLKVSITILQAWEEPLKHMVAAVAALPHVPDTLLSRTKELEERIQGLLEGLKIIFNRVYPGAVASDYTFWSAWSDLQSSDESTKNSALRTLWRCVRRDTHKVDNYLKVLKCRDVHNNNC
Protein: C9orf72-SMCR8 complex subunit (A0A2R8Y5U5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSTLCPPPSPAVAKTEIALSGKSPLLAATFAYWDNILGPRVRHIWAPKTEQVLLSDGEITFLANHTLNGEILRNAESGAIDVKFFVLSEKGVIIVSLIFDGNWNGDRSTYGLSIILPQTELSFYLPLHRVCVDRLTHIIRKGRIWMHKERQENVQKIILEGTERMEDQGQSIIPMLTGEVIPVMELLSSMKSHSVPEEIDIADTVLNDDDIGDSCHEGFLLNAISSHLQTCGCSVVVGSSAEKVNKIVRTLCLFLTPAERKCSRLCEAESSFKYESGLFVQGLLKDSTGSFVLPFRQVMYAPYPTTHIDVDVNTVKQMPPCHEHIYNQRRYMRSELTAFWRATSEEDMAQDTIIYTDESFTPDLYVMLCLLVL
Protein: Matrix metalloproteinase-26 (MMP-26) (EC 3.4.24.-) (Endometase) (Matrilysin-2) (Q9NRE1)
Organism: Homo sapiens (Human)
Function: May hydrolyze collagen type IV, fibronectin, fibrinogen, beta-casein, type I gelatin and alpha-1 proteinase inhibitor. Is also able to activate progelatinase B.
Subcellular location: Secreted, extracellular space, extracellular matrix.
Interaction partners:
- Hemopexin
- Metalloproteinase inhibitor 4
Sequence:
MQLVILRVTIFLPWCFAVPVPPAADHKGWDFVEGYFHQFFLTKKESPLLTQETQTQLLQQFHRNGTDLLDMQMHALLHQPHCGVPDGSDTSISPGRCKWNKHTLTYRIINYPHDMKPSAVKDSIYNAVSIWSNVTPLIFQQVQNGDADIKVSFWQWAHEDGWPFDGPGGILGHAFLPNSGNPGVVHFDKNEHWSASDTGYNLFLVATHEIGHSLGLQHSGNQSSIMYPTYWYHDPRTFQLSADDIQRIQHLYGEKCSSDIP
Protein: Ice-structuring protein A (ISP A) (Antifreeze protein A) (HPLC6) (P04002)
Organism: Pseudopleuronectes americanus (Winter flounder) (Pleuronectes americanus)
Function: Contributes to protect fish blood from freezing at subzero sea water temperatures. Lowers the blood freezing point. Binds to nascent ice crystals and prevents further growth.
Subcellular location: Secreted {ECO:0000269|PubMed:6952188}.
Interaction partners:
Sequence:
MALSLFTVGQLIFLFWTMRITEASPDPAAKAAPAAAAAPAAAAPDTASDAAAAAALTAANAKAAAELTAANAAAAAAATARG
Protein: Ribose-5-phosphate isomerase (EC 5.3.1.6) (D-ribose-5-phosphate ketol-isomerase) (Phosphoriboisomerase) (Q12189)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Ribulose-phosphate 3-epimerase
- Transketolase 1
- Transketolase 2
- 6-phosphogluconate dehydrogenase, decarboxylating 1
- 6-phosphogluconate dehydrogenase, decarboxylating 2
- Ribose-phosphate pyrophosphokinase 1
- Transaldolase
- Ribokinase
- Transaldolase NQM1
- Phosphoglucomutase 1
Sequence:
MAAGVPKIDALESLGNPLEDAKRAAAYRAVDENLKFDDHKIIGIGSGSTVVYVAERIGQYLHDPKFYEVASKFICIPTGFQSRNLILDNKLQLGSIEQYPRIDIAFDGADEVDENLQLIKGGGACLFQEKLVSTSAKTFIVVADSRKKSPKHLGKNWRQGVPIEIVPSSYVRVKNDLLEQLHAEKVDIRQGGSAKAGPVVTDNNNFIIDADFGEISDPRKLHREIKLLVGVVETGLFIDNASKAYFGNSDGSVEVTEK
Protein: Prolactin receptor (PRL-R) (Lactogen receptor) (P05710)
Organism: Rattus norvegicus (Rat)
Function: This is a receptor for the anterior pituitary hormone prolactin.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Prolactin
- Prolactin-6A1
- Tyrosine-protein kinase JAK2
- Cytokine-inducible SH2-containing protein
- Signal transducer and activator of transcription 5A
- Prolactin-5A1
- Somatotropin
- Tyrosine-protein kinase
- Prolactin-3B1
- Tyrosine-protein kinase JAK3
Sequence:
MPSALAFVLLVLNISLLKGQSPPGKPEIHKCRSPDKETFTCWWNPGTDGGLPTNYSLTYSKEGEKTTYECPDYKTSGPNSCFFSKQYTSIWKIYIITVNATNQMGSSSSDPLYVDVTYIVEPEPPRNLTLEVKQLKDKKTYLWVKWSPPTITDVKTGWFTMEYEIRLKPEEAEEWEIHFTGHQTQFKVFDLYPGQKYLVQTRCKPDHGYWSRWSQESSVEMPNDFTLKDTTVWIIVAILSAVICLIMVWAVALKGYSMMTCIFPPVPGPKIKGFDTHLLEKGKSEELLSALGCQDFPPTSDCEDLLVEFLEVDDNEDERLMPSHSKEYPGQGVKPTHLDPDSDSGHGSYDSHSLLSEKCEEPQAYPPTLHIPEITEKPENPEANIPPTVDPQSTNPNFHVDAPKSSTWPLLPGQHMPRSPYHSVADVCKLAGSPVNTLDSFLDKAEENVLKLSKALETGEEEVAEQKGAKSFPSDKQNTPWPLLQEKSPTVYVKPPDYVEIHKVNKDGVLSLFPKQRENNQTEKPGVPETSKEYAKVSGITDNNILVLVPDSRAQNTALLEESAKKAPPSFEADQSEKDLASFTATSSNRRLQLGRLDYLDPTCFMHSFH
Protein: Small ribosomal subunit protein uS12m (40S ribosomal protein S12, mitochondrial) (MRP-S12) (S12mt) (MT-RPS12) (Protein technical knockout locus) (P10735)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion.
Interaction partners:
- Large ribosomal subunit protein bL17m
- Small ribosomal subunit protein uS15m
- Ribosomal protein
- Mitochondrial ribosomal protein S11
- Small ribosomal subunit protein bS6m
- Small ribosomal subunit protein bS16m
- Small ribosomal subunit protein uS5m
- Small ribosomal subunit protein uS7m
- Small ribosomal subunit protein uS10m
- 28S ribosomal protein S14
Sequence:
MNFLRQSFGITKQLASQAIQCSYETAVRGMASLQQMHRSGPHIKTRPPRQPLDGKPFAKGVVLKTLIKKPKKPNSANRKCVLVRLSTGKEMVAYIPGIGHNLQEHNIVLCRVGRLQDVPGVKLKAVRGVYDLAHVVKKSQ
Protein: Deoxycytidylate deaminase (EC 3.5.4.12) (dCMP deaminase) (P06773)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the hydrolytic deamination of dCMP to yield dUMP, the nucleotide substrate for thymidylate synthetase.
Interaction partners:
- Thymidylate synthase
- Deoxyuridine 5'-triphosphate nucleotidohydrolase
- Thymidylate kinase
- Cytidine deaminase
- Cytosine deaminase
- Uridylate kinase
- Bifunctional purine biosynthesis protein ADE17
- Bifunctional purine biosynthesis protein ADE16
- tRNA-specific adenosine deaminase subunit TAD2
- tRNA-specific adenosine deaminase subunit TAD3
Sequence:
MLIGVSGTKFCGCEDVINMLVDHFHFELLNHLDNPEEILDYATKNYTKNSVIFLEKLSLLEKLEKRPFFVHLSIDAPVTTRVALYRKTTQAESLSLEQIIQAIDQHDFQPEGIKLREKSHLRFKIVNEDRRGRRQSLINNITTQLKILDDKEKQMAPLMRPSWDSYFMKLATLAASRSNCMKRRVGCVIVRECRVIATGYNGTPRHLTNCFNGGCPRCNDGDSRNLHTCLCLHAEENALLEAGRDRVGQNATLYCDTCPCLTCSVKIVQTGISEVVYSQSYRMDEESFKVLKNAGITVRQFSFTEEPRIVMI
Protein: ECF RNA polymerase sigma factor SigL (ECF sigma factor SigL) (Alternative RNA polymerase sigma factor SigL) (RNA polymerase sigma-L factor) (Sigma-L factor) (P9WGH5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. Extracytoplasmic function (ECF) sigma factors are held in an inactive form by an anti-sigma factor until released by regulated intramembrane proteolysis. Over-expression of SigL induces 19-28 genes including polyketide synthases, secreted and membrane proteins. Might play a minor role in regulating SigB.
Interaction partners:
- DNA-directed RNA polymerase subunit beta
- Anti-sigma-L factor RslA
- DNA-directed RNA polymerase subunit beta'
- ECF RNA polymerase sigma factor SigC
- ECF RNA polymerase sigma factor SigM
- DNA-directed RNA polymerase subunit alpha
- DNA-directed RNA polymerase subunit omega
- RNA polymerase sigma factor SigF
- Methionine aminopeptidase 1
- ECF RNA polymerase sigma factor SigG
Sequence:
MARVSGAAAAEAALMRALYDEHAAVLWRYALRLTGDAAQAEDVVQETLLRAWQHPEVIGDTARPARAWLFTVARNMIIDERRSARFRNVVGSTDQSGTPEQSTPDEVNAALDRLLIADALAQLSAEHRAVIQRSYYRGWSTAQIATDLGIAEGTVKSRLHYAVRALRLTLQELGVTR
Protein: tetrahydrofolate synthase (EC 6.3.2.17) (Folylpoly-gamma-glutamate synthetase) (Tetrahydrofolylpolyglutamate synthase) (Q38AL2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Bifunctional dihydrofolate reductase-thymidylate synthase
- Prohibitin
- Prohibitin
- Valine--tRNA ligase, mitochondrial
Sequence:
MTAWHRLPAAARALFGAKGGCTGSQRSYDDVLRVMYELTLRVVNPTYRNRTLANTSGKSAELVGLLVERLNMRRCLDTLRFVHVAGTKGKGTTASYTAALLEAYGLKVGLFTSPHVKDVRERIMVNNEVLPMDTFVHYFFQVVDCFVELAGADKEVTWDLPAPCSFFCLMFLVSLVAFAGESVDVAVVEVGIGGSRDPTNIIIPEASVITALGIDHTEILGDTVEEIALQKAGIMKPGVVCYAAPQGDHPSTRRVLKDYAEGVDSPLVFADDVAVPTDGWPCLSIGGEHAVENSRLALLAARSVMGIPLTQPLDDVERHVLQRTTVMGRSQVLPVGDGSKGTFYLDGAHTYESLRCATRWFVKESTKRTCDSKPRRVLLMYSSRQPERIVEAFRPFVDSFSKAVFVCALDPKGMREIWKNNSDAYTQDKATGLIRCWKTLCGAVPCFSRAAPFVSVEEVVEVVSAASSDDEDTSKPVQVFVTGSFFLVSDIVNLYDSQGS
Protein: Zinc phosphodiesterase ELAC protein 2 (EC 3.1.26.11) (ElaC homolog protein 2) (Ribonuclease Z 2) (tRNA 3 endonuclease 2) (tRNase Z 2) (G5E9D5)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion matrix, mitochondrion nucleoid {ECO:0000256|ARBA:ARBA00004436}.
Interaction partners:
Sequence:
MWALCSLLRSAAGRTMSQGRTISQAPARRERPRKDPLRHLRTREKRGPSGCSGGPNTVYLQVVAAGSRDSGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKETGLPKCVLSGPPQLEKYLEAIKIFSGPLKGIELAVRPHSAPEYEDETMTVYQIPIHSEQRRGKHQPWQSPERPLSRLSPERSSDSESNENEPHLPHGVSQRRGVRDSSLVVAFICKLHLKRGNFLVLKAKEMGLPVGTAAIAPIIAAVKDGKSITHEGREILAEELCTPPDPGAAFVVVECPDESFIQPICENATFQRYQGKADAPVALVVHMAPASVLVDSRYQQWMERFGPDTQHLVLNENCASVHNLRSHKIQTQLNLIHPDIFPLLTSFRCKKEGPTLSVPMVQGECLLKYQLRPRREWQRDAIITCNPEEFIVEALQLPNFQQSVQEYRRSAQDGPAPAEKRSQYPEIIFLGTGSAIPMKIRNVSATLVNISPDTSLLLDCGEGTFGQLCRHYGDQVDRVLGTLAAVFVSHLHADHHTGLPSILLQRERALASLGKPLHPLLVVAPNQLKAWLQQYHNQCQEVLHHISMIPAKCLQEGAEISSPAVERLISSLLRTCDLEEFQTCLVRHCKHAFGCALVHTSGWKVVYSGDTMPCEALVRMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAISVGMRMNAEFIMLNHFSQRYAKVPLFSPNFSEKVGVAFDHMKVCFGDFPTMPKLIPPLKALFAGDIEEMEERREKRELRQVRAALLSRELAGGLEDGEPQQKRAHTEEPQAKKVRAQ
Protein: BOC cell adhesion associated, oncogene regulated (D4A0Z7)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Sonic hedgehog protein
- Hedgehog protein
- Hedgehog protein
- Patched
- Growth arrest-specific 1.
- Protein smoothened
- Cell adhesion molecule-related/down-regulated by oncogenes
- Low-density lipoprotein receptor-related protein 2
Sequence:
MVTCRGEQPMLTLLWFLLAIAGCLADLNEVPQVTVQPMSTVQKLGGTVILGCVVEPPWVNVTWRFNGKELNGSDDALGVLITRGTLVIAALNNHTVGRYQCVARMPAGAVASVPATVTLANLQDFKLDVQHVIEVDEGNTAVIACHLPESHPKAQVRYSVKQEWLEASRDNYLIMPSGNLQIVNASQEDEGTYKCAAYNPVTQEVKTSGSSDRLRVRRSTAEAARIIYPLEAQTVIVTKGQSLILECVASGIPPPRVTWAKDGSSIAAYNKTRFLLSNLLIDTTSEEDSGTYRCMASNGVGDPGAAVILYNVQVFEPPEVTVELSQLVIPWGQSAKLTCEVRGNPPPSVLWLRNAVPLSSNQRLRLSRKALRVVSVRPEDEGVYQCMAENAVGSAHAVVQLRTARPDTTLRPGRDTKPIAATPPMPPSRPNRPDQMLREQPGLVKPPTSVQPTSLKCLGEEQVAPAEAPVILSSPRTSKTDSYELVWRPRHEGSSRAPILYYVVKHRKQVTNSSDDWIISGIPANQHHLTLTRLDPGSLYEVEMAAYNCAGEGQTAMVTFRTGRRPKPEIVASKEQQIQRDDPGASLQSSSQPDHGRLSPPEAPDRPTISTASETSVYVTWIPRGNGGFPIQSFRVEYKKLKKVGDWILATSAIPPSRLSVEITGLEKGISYKFRVRALNMLGESEPSAPSRPYVVSGYSGRVYERPVAGPYITFTDAVNETTIMLKWMYIPASNNNTPIHGFYIYYRPTDSDNDSDYKKDMVEGDRYWHSISHLQPETSYDIKMQCFNEGGESEFSNVMICETKARKFSGQPGRPPPLTLAPPQPPPLEAMERPMGTGAMVARASDLPYLIVGVVLGSIVLIIVTFIPFCLWRAWSKQKHTTDLGFPRSALLSSSCQYTMVPLGGLPGHQANGQPYLSGIGGRACVSRLHGSRGYPAATVGCPGRKLQQHCPGELAQQREDSNSLLRQPIVSNGYDLQNQQVARGTKSGSEEGSFLYTLPDDSTHQLLQPQDCCHLQKQPVTTCQTAVRRAPEGPGLEASWDPQYHSGPRCCLGLVPVEEVDSSDSCQVGGGDCCPQHPSGTYTGQELGVRLSPSPSVHVSFETPPPTI
Protein: EOR-2 (G5EE70)
Organism: Caenorhabditis elegans
Interaction partners:
- EOR-1
- Protein lin-25
- Mediator of RNA polymerase II transcription subunit 23
Sequence:
MDQRNQKSLLPDFSANGFSGQFNGIPHGNTNAIMSTIQSLQMHSMGNQLLPHGDLQTDLQNQFLIEQFQLRAMQSMYNTFNNGNQKQPQASLTMSQFNSMTGNEPSTSSNVFSASIPTTSGTQINASQPMIPTTSMHNLAVQSSMMLENKLGQNLNLKTTQLAQTTIPQAQAAVEDWMKNICVDSLLDPKQAKTPSTTPSAQVSAGTTFNSTPAVSCATPLTATVSLATKPSEPSAASSMPTSSESVDATKGDAIDFDDEAHDDVDNIFGLSLSESDVRSGSMYRRPDSADRVHSPIDFTPPDSPQAELTFDEIFGISAPSTSAKAATKEKPVPKPRSEMVFHDVPSTSKDDIATGTRGNKEFPAIATPQRVPKPAPTAASKEEDDFVNNFVKPQNVPVYKQKAALMSLEARENARKEDPNYDAFEFEDDDDFVFGGPSADLRREPELTKKIEQKAKSVYITGVGFSIRNDKEKEYSSKKYYSKPSATHQPNFNDTINEKAFFTTADEIRAQKDQQLVCAFLKPEQVTSTECVRNMRKVTREEPMLPKFIIRVEQVQNQHEEPMTRRRYKRKKNKSDNDDSDFEDVAYRKRKTAKKVYTMHKENDPTFRRTVLDFSIGPCVSDEEKKRVSMFGPAEGILPKGTYVICKADMLKEDCAVWRVDNQNLLQKFPPFRDSKANRLVYRSSSTYSGWCEQISSQYFRVAVKIIKQTRSETTVEPEVPLAELFPASSVEWFKNPGTVFFEEETKVEPIDDDSILTEPRRVSLNTLVNAYLTQVFTKTHVESLIDDKDWTYSRSIAELETNNKQCEGLIKKRIPVEPKHNRWIAKYTRLAISKSSFHCFTKCQICKRKKPRRVIHFFDKTSCNEKLLVENLSSDIHDENEDDEEYPIVSDAISCGRCSMAVDFLHRMHHIKFHMLRICEDKLEEIGTSDIDLTSDKIVEKAKADKVWTLGVIQKYCDLWDQVRYEFRDV
Protein: Putative peptidyl-prolyl cis-trans isomerase dodo (PPIase dodo) (EC 5.2.1.8) (Rotamase dodo) (P54353)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- DNA-directed RNA polymerase II subunit RPB1
- UDP-glucose 4-epimerase
- Phosphatidylinositol 5-phosphate 4-kinase, isoform A
- U6 snRNA-associated Sm-like protein LSm7
Sequence:
MPDAEQLPDGWEKRTSRSTGMSYYLNMYTKESQWDQPTEPAKKAGGGSAGGGDAPDEVHCLHLLVKHKGSRRPSSWREANITRTKEEAQLLLEVYRNKIVQQEATFDELARSYSDCSSAKRGGDLGKFGRGQMQAAFEDAAFKLNVNQLSGIVDSDSGLHIILRKA
Protein: Transcription factor protein (Q4H3V8)
Organism: Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- BZIP domain-containing protein
- Large ribosomal subunit protein eL30
- Transcription factor protein
Sequence:
MLGSMYESEDIPLFGGNLLGDGSLGTGHEELVEKLVGGSTMYPQTAPSSGVCYQENPLNDTAGLSLGSEWMTDNIDLSLLDDLVDSGFLGNQEELKNSAYYACQPISPASSFDSGVASPGSSSYPSIESPVSNYSGSDSYIDTPLEQLSPLPANTAVNTLSTEQNAFPDFGIDGDLLLEELGIKVIEDNNCESSFPSLQVHEVQPATTTTNTINCSSELSFLLSSTNAQPTHQTPPVPQVSQVNYIPVKTSPPPSKSRGGRKSKVTTTVERKQRKRDQNKNAATRYRERKRLEFSKQESEQRVLEEKNKSLHDNVNRVTREIEYLKELMIEVYKIKGLIK
Protein: Exosome complex component RRP45 (Ribosomal RNA-processing protein 45) (Q05636)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and cryptic unstable transcripts (CUTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and in RNA surveillance pathways, preventing translation of aberrant mRNAs. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. RRP45 is part of the hexameric ring of RNase PH domain-containing subunits proposed to form a central channel which threads RNA substrates for degradation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus, nucleolus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Exosome complex exonuclease DIS3
- Exosome complex component RRP42
- Exosome complex component RRP4
- Exosome complex exonuclease RRP6
- Exosome complex component CSL4
- Exosome complex component RRP46
- Exosome complex component RRP40
- ATP-dependent RNA helicase DOB1
- Superkiller protein 7
- M-phase phosphoprotein 6 homolog
Sequence:
MAKDIEISASESKFILEALRQNYRLDGRSFDQFRDVEITFGKEFGDVSVKMGNTKVHCRISCQIAQPYEDRPFEGLFVISTEISPMAGSQFENGNITGEDEVLCSRIIEKSVRRSGALDVEGLCIVAGSKCWAVRADVHFLDCDGGFIDASCIAVMAGLMHFKKPDITVHGEQIIVHPVNEREPVPLGILHIPICVTFSFFNPQDTEENIKGETNSEISIIDATLKEELLRDGVLTVTLNKNREVVQVSKAGGLPMDALTLMKCCHEAYSIIEKITDQILQLLKEDSEKRNKYAAMLTSENAREI
Protein: Tryptophan 2,3-dioxygenase (TDO) (EC 1.13.11.11) (Tryptamin 2,3-dioxygenase) (Tryptophan oxygenase) (TO) (TRPO) (Tryptophan pyrrolase) (Tryptophanase) (Q17P71)
Organism: Aedes aegypti (Yellowfever mosquito) (Culex aegypti)
Function: Heme-dependent dioxygenase that catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring and converts L-tryptophan to N-formyl-L-kynurenine. Catalyzes the oxidative cleavage of the indole moiety.
Interaction partners:
- Kynurenine formamidase
- Tryptophan 5-hydroxylase 2
- AAEL005706-PA
- Aromatic-L-amino-acid decarboxylase
- AAEL000420-PA
- Tyrosine aminotransferase
- Kynurenine aminotransferase
- Kynurenine 3-monooxygenase
Sequence:
MSCPVGNHNGDPQGGQRLGSEAGMLYGEYLMLDKVLSAQRMLSVESNKPVHDEHLFIVTHQAYELWFKQIIFELDSIRSLFSTEHMEESRTLEILKRLNRIVMILKLLVDQVPILETMTPLDFMDFRDFLSPASGFQSLQFRLLENKLGVKTEHRVKYNQKYSEVFASDPCAIERLSITESEPSLADLVQKWLERTPGLETNGFNFWGKFEESVEQLLADQEASAMEEEHENVKNYRLMDIEKRREVYKSIFDASVHDALVARGDRRFTHRALQGAIMITFYRDEPRFSQPHQLLMLLMDIDSLITKWRYNHVIMVQRMIGSQQLGTGGSSGYQYLRSTLSDRYKVFIDLFNLSTFLIPRGSIPPLTCEMQKALNLAWGSPVHQAKQINYAAK
Protein: Proteasome subunit alpha (20S proteasome alpha subunit) (Proteasome core protein PrcA) (P9WHU1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The M.tuberculosis proteasome is able to cleave oligopeptides not only after hydrophobic but also after basic, acidic and small neutral residues. In complex with the ATPase Mpa, degrades protein targets conjugated to a prokaryotic ubiquitin-like protein (Pup). Among the identified substrates of the M.tuberculosis proteasome are the pupylated FabD, PanB and Mpa proteins. One function of the proteasome is to contribute to M.tuberculosis ability to resist killing by host macrophages, since the core proteasome is essential for persistence of the pathogen during the chronic phase of infection in mice. Likely functions to recycle amino acids under nutrient starvation, thereby enabling the cell to maintain basal metabolic activities (By similarity). The mechanism of protection against bactericidal chemistries of the host's immune response probably involves the degradation of proteins that are irreversibly oxidized, nitrated, or nitrosated. A proteolysis-independent activity of the proteasome core is required for optimal growth of M.tuberculosis in mouse lungs and for RNI resistance; in contrast, long-term survival of M.tuberculosis in stationary phase and during starvation in vitro and in the chronic phase of mouse infection required a proteolytically active proteasome.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00289}.
Interaction partners:
- Proteasome subunit beta
- Proteasome-associated ATPase
- Prokaryotic ubiquitin-like protein Pup
- Pup--protein ligase
- Bacterial proteasome activator
- Pup deamidase/depupylase
- CysO-cysteine peptidase
- Glycerol kinase
- Uncharacterized protein Rv0738
- Protein PafC
Sequence:
MSFPYFISPEQAMRERSELARKGIARAKSVVALAYAGGVLFVAENPSRSLQKISELYDRVGFAAAGKFNEFDNLRRGGIQFADTRGYAYDRRDVTGRQLANVYAQTLGTIFTEQAKPYEVELCVAEVAHYGETKRPELYRITYDGSIADEPHFVVMGGTTEPIANALKESYAENASLTDALRIAVAALRAGSADTSGGDQPTLGVASLEVAVLDANRPRRAFRRITGSALQALLVDQESPQSDGESSG
Protein: VPS9 domain-containing protein 1 (Protein ATP-BL) (Q9Y2B5)
Organism: Homo sapiens (Human)
Interaction partners:
- Spermatogenesis-associated protein 2-like protein
Sequence:
MAAAAGDGTVKPLQSAMKLANGAIELDTGNRPREAYTEYLRSIHYISQVLLEEVETTKEAGETVPPDTSKMLKLAQQCLERAQSTAAKLGKTRLKPTMPAAAPIPQPAGRHRRVYSDEGGKLSPFLPPEIFQKLQGAESQSCKKELTPLEEASLQNQKLKAAYEARMARLDPSQAMQKTSLTLSLQRQMMENLVIAKAREETLQRKMEERRLRLQEAANRRFCSQVALTPEEREQRALYAAILEYEQDHDWPKHWKAKLKRNPGDLSLVTSLVSHLLSLPDHPIAQLLRRLQCSVYSALYPAVSRAAAPAPGCCPPTPNPGSRRLRPSQSLHCMLSPPEPSAAPRPQDSPPTPPLQPGPVGSPSPLGDTASGLPDKDSSFEDLEQFLGTSERQGRGRGVQPEPQLQQLKTAVEEIHNAVDRLLSLTLLAFEGLNTAASKDRCLACIEEPFFSPLWPLLLALYRSVHRAREAALSRSMELYRNAPPTAIGIPTKLLPQNPEAKGATGYPYCAAAQELGLLVLESCPQKKLECIVRTLRIICVCAEDYCPTPEATPQAGPPPIAAAAIGADDLLPILSFVVLRSGLPQLVSECAALEEFIHEGYLIGEEGYCLTSLQSALSYVELLPRGGLAK
Protein: Slr1160 protein (P74233)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Interaction partners:
- Slr2144 protein
- Ssr0332 protein
- Slr2025 protein
- Uncharacterized protein slr1353
- Sll0359 protein
- Slr1704 protein
- NAD
- High light-inducible protein HliD
- Ycf51-like protein
- Ssr2551 protein
Sequence:
MLQRLVHILALTVCGLAVVSSLTPSVRGQGVTEVEEVIIEGSGPENSREFRPLNQEGSILSVGAGRRLMNEANEAINLNQYTVALEKLQEARKIFNQLSNFHLQLANSFSGINTVIFEEQRIAALETGQLRDEATYRLALVHRANNEPALAVPLLLQIIRSQNPTTDLGRKSYQQLYELGFVASPFEGPTPTGTNAAPTAPVVN
Protein: Prokineticin-2 (PK2) (Q8R413)
Organism: Rattus norvegicus (Rat)
Function: May function as an output molecule from the suprachiasmatic nucleus (SCN) that transmits behavioral circadian rhythm. May also function locally within the SCN to synchronize output. Potently contracts gastrointestinal (GI) smooth muscle (By similarity).
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Prokineticin receptor 2
- Prokineticin receptor 1
- Chromodomain-helicase-DNA-binding protein 7
- NMDA receptor synaptonuclear signaling and neuronal migration factor
Sequence:
MEDPRCAPLLLLLLLPLLLTPPAGDAAVITGACDKDSQCGGGMCCAVSIWVKSIRICTPMGQVGDSCHPLTRKVPFWGRRMHHTCPCLPGLACLRTSFNRFICLARK
Protein: Tubulin-tyrosine ligase (Q580T7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MITDVTSTKRPVESRKCIVVMCADTRYHVVRTAAVSLGWHVEDGERDDVPSSFHGISLNKDMNSLSETISLLGAKCNAALNPQIIWLDKSVLSSRVAALSCFHRVNHFPGMHVIARKATLFKRLMRIRRQHDLSPTLRRSLDAFPWSFSPSTELLQLERFISDGREGEIFILKPNKGCEGKGIIITAEPLHVVERMTDEERNECLVQQYVPHPLCIDRKKFDLRIYVLVTSVVVGKPPRKGFRGAAPPKETHGGSSFPLNGLQLFVHKEGLVRICTEDYATPNASNCKRQGMHLTNYAVNKRAQGFSVGDVLNTDDSSSNGICEGNKRDFKFLEHYINGLVGCKSDTTEDDVSGGETTSRWERVLHRIDRCILLTVLSGLENLRREFIGTGASRGSRSDGRNCFELLGVDILLTEDLKPVLMEVNHSPSLFCDSDFDFRTKHRVLMDVFRLLEPYVPSLENCNDAAYATLQESITAGGNMSSTGFRQISPLRVGGDDWADEEMQMFEEMLRHANGLR
Protein: Keratin 75 (Type II alpha-keratin IIC) (H2EQW7)
Organism: Gallus gallus (Chicken)
Interaction partners:
Sequence:
MSRQSTVRIQRGRSGFSAASAIVPGTCRTSFSSRSVTRVGGCNAGSGFARVGGGFGSRSLYNFGGCKRISAAGRGGGFYGTAGFGGGAGSMLGYGYGAFGGPGFPAGGIQEVSINQSLLKPLNLEIDPSIQRIRKEEKEQIKTLNNKFASFIDKVRFLEQQNKVLETKWSLLQEQGMKTVRNNLEPLFETYINNLRMQLNSLLSDKGRLEGELVNTQYLVEDFKKKYEDEINRRTIAENEFVTLKKDVDASYMNKVELQAKADALTEEINFLRALYEAELSQMQTQISDTSVVLTMDNNRNLDLDSIIAEYEELQATAGRHGDDLRSTKQEISELNRHVQRLRAEIDSVKKQCANLKAAIADAEERGEIALKDAKAKLAELEDALQQAKADLARQLREYQELMNVKLALDIEIATYRKLLEGEECRLAGDGVPVNISVTRTTVGSGYGGGSNLSMGGGMCSMGNNYSCSGPGGSSALGGGSSSSVKFFSSSSSRRSYRS
Protein: RE34768p (Q8SYT2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
VAYNHDGMPDQQFLWDVFQRVDKDRSGHISADELQVALSNGTWSAFNPETIRLMIGMFDRENKGTVSFKDFGALWKYVTDWQNCFRSFDRDNSGNIDKTELKTALTSFGYRLSDHLIDVLLRKFDRFGRGTILFDDFIQCCIVLYVSMTVIAIYEYKVAVGSRDFRCLAYEKIFEIALKPARKNCMAFRVFSNVFANKRSPLINMSERYSRVLYYQLLR