wanglab/gogpt-training-data huggingface dataset:
Protein: Albumin (P02768)
Organism: Homo sapiens (Human)
Function: Binds water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs (Probable). Its main function is the regulation of the colloidal osmotic pressure of blood (Probable). Major zinc transporter in plasma, typically binds about 80% of all plasma zinc. Major calcium and magnesium transporter in plasma, binds approximately 45% of circulating calcium and magnesium in plasma (By similarity). Potentially has more than two calcium-binding sites and might additionally bind calcium in a non-specific manner (By similarity). The shared binding site between zinc and calcium at residue Asp-273 suggests a crosstalk between zinc and calcium transport in the blood (By similarity). The rank order of affinity is zinc > calcium > magnesium (By similarity). Binds to the bacterial siderophore enterobactin and inhibits enterobactin-mediated iron uptake of E.coli from ferric transferrin, and may thereby limit the utilization of iron and growth of enteric bacteria such as E.coli. Does not prevent iron uptake by the bacterial siderophore aerobactin.
Subcellular location: Secreted.
Interaction partners:
- IgG receptor FcRn large subunit p51
- Insulin
- Alpha-2-HS-glycoprotein
- Alpha-1-acid glycoprotein 1
- Apolipoprotein A-I
- Alpha-1-antitrypsin
- Alpha-1-acid glycoprotein 2
- Fibronectin
- Alpha-lactalbumin
- Sex hormone-binding globulin
Sequence:
MKWVTFISLLFLFSSAYSRGVFRRDAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLVAASQAALGL
Protein: Small ribosomal subunit protein eS21B (40S ribosomal protein S21-B) (S26) (YS25) (Q3E754)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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. eS21 is required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. Has a physiological role leading to 18S rRNA stability.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14627813, ECO:0000269|PubMed:22096102}.
Interaction partners:
- Small ribosomal subunit protein uS11B
- Small ribosomal subunit protein eS10A
- Small ribosomal subunit protein eS27A
- Large ribosomal subunit protein eL24B
- Small ribosomal subunit protein uS14B
- Small ribosomal subunit protein eS1A
- Small ribosomal subunit protein eS4A
- Small ribosomal subunit protein eS10B
- Small ribosomal subunit protein uS2A
- Small ribosomal subunit protein uS3
Sequence:
MENDKGQLVELYVPRKCSATNRIIKADDHASVQINVAKVDEEGRAIPGEYITYALSGYVRSRGESDDSLNRLAQNDGLLKNVWSYSR
Protein: Transcription factor spt8 (O60097)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Functions as a component of the transcription regulatory histone acetylation (HAT) complex SAGA. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- SAGA complex subunit Spt7
- Histone acetyltransferase gcn5
- Probable ubiquitin carboxyl-terminal hydrolase 8
- SAGA complex/transcription factor TFIID complex subunit Taf6
- SAGA complex/transcription factor TFIID complex subunit Taf12
- SAGA complex/transcription factor TFIID complex subunit Taf9
- SAGA complex subunit Sgf73
- SAGA complex/transcription factor TFIID complex subunit Taf5
- SAGA complex subunit Hfi1
- SAGA complex subunit Spt3
Sequence:
MEAEESESFSYPMLLPSDGLYPEDDDDADMDQDKNPEENVMNEKEDEDVDAVDEKSGEEDVEMDTMEDENENDEDTEQTSEKKETEETPKENPLEKLKQKASTASFYDVVPTLAIPMATSINAFAFTSDLKWLFTGGEDGYIRKYDFFPSINGDLSLTVAQRHPFVDTVTKAGILLNYWENAYDGNKPSSVYSLAAHSRGLWVLSGVNNGDIILYSTRHQEGYPVTSLKKHTAPVSCLALHGSEKKVLSGSWDKMVYYWDLNTGDAISTYNCESGQISNIVYRPSGAVNPWGSESDDMRSLFGTPASSSSYDALFDEEVEKAIEEETKSVQANEENETEKPSQTESTTNNDNIKAPSESSSEESNIFLTTSIDGVMNVWDHRMVDSVLKYPVPKGVPPWAMSACWSPDGNNIYIGRRNGIVEEYNIHSGKEPVRSLKMPLDSGPVSNVYSMPNGRHLVISSFDNIRLYDLQSKAGIGFLIIPGHHGGLVSSLYVDTSCQFMFSASGNRGWQGTTTEVFLGYQIMTS
Protein: Glucosidase YgjK (EC 3.2.1.-) (P42592)
Organism: Escherichia coli (strain K12)
Function: Glucoside hydrolase that cleaves the alpha-1,3-glucosidic linkage in nigerose. Has very low activity towards maltooligosaccharides, soluble starch, nigerotriose, kojibiose and trehalose.
Interaction partners:
- Inner membrane transporter YgjI
- Evolved beta-galactosidase subunit beta
- Uncharacterized protein YgjJ
- Evolved beta-galactosidase subunit alpha
- Maltodextrin phosphorylase
- Glycogen phosphorylase
Sequence:
MKIKTILTPVTCALLISFSAHAANADNYKNVINRTGAPQYMKDYDYDDHQRFNPFFDLGAWHGHLLPDGPNTMGGFPGVALLTEEYINFMASNFDRLTVWQDGKKVDFTLEAYSIPGALVQKLTAKDVQVEMTLRFATPRTSLLETKITSNKPLDLVWDGELLEKLEAKEGKPLSDKTIAGEYPDYQRKISATRDGLKVTFGKVRATWDLLTSGESEYQVHKSLPVQTEINGNRFTSKAHINGSTTLYTTYSHLLTAQEVSKEQMQIRDILARPAFYLTASQQRWEEYLKKGLTNPDATPEQTRVAVKAIETLNGNWRSPGGAVKFNTVTPSVTGRWFSGNQTWPWDTWKQAFAMAHFNPDIAKENIRAVFSWQIQPGDSVRPQDVGFVPDLIAWNLSPERGGDGGNWNERNTKPSLAAWSVMEVYNVTQDKTWVAEMYPKLVAYHDWWLRNRDHNGNGVPEYGATRDKAHNTESGEMLFTVKKGDKEETQSGLNNYARVVEKGQYDSLEIPAQVAASWESGRDDAAVFGFIDKEQLDKYVANGGKRSDWTVKFAENRSQDGTLLGYSLLQESVDQASYMYSDNHYLAEMATILGKPEEAKRYRQLAQQLADYINTCMFDPTTQFYYDVRIEDKPLANGCAGKPIVERGKGPEGWSPLFNGAATQANADAVVKVMLDPKEFNTFVPLGTAALTNPAFGADIYWRGRVWVDQFWFGLKGMERYGYRDDALKLADTFFRHAKGLTADGPIQENYNPLTGAQQGAPNFSWSAAHLYMLYNDFFRKQ
Protein: Growth/differentiation factor 3 (Gdf-3) (Derriere protein) (Q9YGV1)
Organism: Xenopus laevis (African clawed frog)
Function: Required for posterior mesoderm formation during embryogenesis. Acts indirectly to suppress head formation by altering mesodermal patterning. Also involved in the establishment of left-right axis asymmetry, acting upstream of nodal/nr-1. Can exert long-range effects in the embryo.
Subcellular location: Secreted {ECO:0000269|PubMed:11256621}. Cytoplasm {ECO:0000250|UniProtKB:Q9NR23}.
Interaction partners:
Sequence:
MAELWLSLSCMFSLLLLTNSSPLTFQERMLLKALGLNTRPNPIAPAPVPKSLRDIFEKGINQDNPCMMEGFGVPGNIVRSYRDQGTIAAIEEPQGSLCLKKFLFFDLSAVENKEQLTLGQLEIKFKHNTYYGQQFHLRLYRTLQLSLKGMRDSKMNRKLLVTQSFRLLHKSLYFNLTKVAEDWKNPEKNMGLILEIYASSELAGGNRSFVVCEPIQSFIYTSLLTVSLDPSNCKTQRAKRSTHSSPPTPSNICKKRRLYIDFKDVGWQNWVIAPRGYMANYCHGECPYPLTEMLRGTNHAVLQTLVHSVEPENTPLPCCAPTKLSPISMLYYDNNDNVVLRHYEDMVVDECGCK
Protein: Nitrogen permease regulator 3-like protein (Q9HGM7)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Nitrogen permease regulator 2 homolog
- Vacuolar membrane-associated protein iml1
- Uncharacterized RWD, RING finger and WD repeat-containing protein C11E3.05
- Uncharacterized WD repeat-containing protein C4F8.11
- Uncharacterized WD repeat-containing protein C12G12.01c
- GTP-binding protein gtr1
- Nucleoporin seh1
- Protein transport protein sec13
- GTP-binding protein gtr2
- Uncharacterized protein C1778.05c
Sequence:
MVRLTPRLVAIFLVEKTTSGANFVFHWPLQPQVRLQATHHNNDSAESAIGMLDLDDSDDDENNRFTEVADDTHVLGYEKGFLANMLSPRIELCNQKFEIWVDGLTFLGCPVHIGPNGEWAKRRKPRTTVESNASSSHLVSKPESSHPSTGSFEVKSSSSKSRSSMSLFHVVFVLNVPTATVYRPTVNTMYDHIVVKLVTGLKYEQAKRNYVENECIHILKLTEKYSSQNVPFDVYAAQIPHHSNLASVLATTYEALINMHTAYLEINQSINLSLLWPMSVSTNTLENYELQVRPSTILASQTIFSEEHPSSIEPFVAPYWTLLLLKDTDTIMKRVPLLQNSLLSSFIAIVKPNLTFTDIANRLGISVSECFILAKHLIHWRKAIAIPPLLIRNTYVTSPTANLFNLEEESKLFKKEFPSLPSLSTFLAILSFKPRPFASIIPSKDHELVYLEMLAWLCRRNWVYEQNIYMYILVPEEIKKKAIALIESDESSKNDMQLRKQLEQDNGKESIIIDPHSASLLEQKWIQIIAYERGPEMAPLFTSIVKYLNGRFALQTIWVAEGLPRKLMRNILNEYNDYILRWHSW
Protein: Long-chain-fatty-acid--CoA ligase 6 (EC 6.2.1.3) (Arachidonate--CoA ligase) (EC 6.2.1.15) (Long-chain acyl-CoA synthetase 6) (LACS 6) (Q91WC3)
Organism: Mus musculus (Mouse)
Function: Catalyzes the conversion of long-chain fatty acids to their active form acyl-CoA for both synthesis of cellular lipids, and degradation via beta-oxidation (By similarity). Plays an important role in fatty acid metabolism in brain and the acyl-CoAs produced may be utilized exclusively for the synthesis of the brain lipid (By similarity).
Subcellular location: Mitochondrion outer membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Peroxisome membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Microsome membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9UKU0}; Single-pass type III membrane protein {ECO:0000250}.
Interaction partners:
- Carnitine O-palmitoyltransferase 1, liver isoform
- Fatty acid synthase
- Lipoprotein lipase
- Monoglyceride lipase
- Lysosomal thioesterase PPT2
- Palmitoyl-protein thioesterase 1
- Beta-alanine-activating enzyme
- Palmitoyl thioesterase CPT1C
- Carnitine O-palmitoyltransferase 1, muscle isoform
- Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
Sequence:
MQTQEILRILRLPELSDLGQFFRSLSATTLVSVGALAAVLAYWLTHRPKALQPPCNLLKQSEEVEDGGGARRSVIGGCTQLLTHYYDDARTMYQVFRRGLSISGNGPCLGFRKPEQPYQWLSYQEVAKRAEFLGSGLLQHDCKVGTEQFVGVFAQNRPEWIIAELACYTYSMVVVPLYDTLGPGSISYIINTADICTVIVDKPHKATLLLEHVERKETPGLKLVILMEPFEDALRERGKKCGVDIKSMQAIEDCGRENHHAPVPPRPDDLSIVCFTSGTTGNPKGAMLTHGNVVADFSGFLKVTEKVIFPRQDDVLISFLPLAHMFERVIQSVVYCHGGRVGFFQGDIRLLSDDMKALRPTIFPVVPRLLNRMYDKIFHQADTSLKRWLLEFAAKRKQAEVRSGIIRNNSIWDELFFNKIQASLGGHVRMIVTGAAPASPTVLGFLRAALGCQVYEGYGQTECTAGCTFTTPGDWTSGHVGAPLPCNHIKLVDAEELNYWTCKGEGEICVKGPNVFKGYLKDEDRTKEALDSDGWLHTGDIGKWLPEGTLKIIDRKKHIFKLAQGEYVAPEKIENIYIRSEPVAQIYVHGDSLKAFLVGIVVPDPEVMPSWAQKKGIEGTYQELCMKKELKKAILDDMVMLGKESGLHSFEQVKAIYIHCDMFSVQNGLLTPTLKAKRPELREYFKKQIEELYLVSV
Protein: Recombination repair protein 1 (DNA-(apurinic or apyrimidinic site) endonuclease) (EC 3.1.11.2) (P27864)
Organism: Drosophila melanogaster (Fruit fly)
Function: Plays a role in the cellular response to oxidative stress by promoting DNA repair mechanisms such as base excision repair and possibly homologous recombination repair. Functions as an apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents. Likely to initiate repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends (By similarity). Has a 3'-5' exoribonuclease activity on mismatched deoxyribonucleotides at the 3' termini of nicked or gapped DNA molecules during short-patch BER. Has apurinic endonuclease and double-stranded DNA 3'-exonuclease activities and carries out single-stranded DNA renaturation in a Mg(2+)-dependent manner. Activity is more efficient in purine-rich regions of dsDNA than in pyrimidine-rich regions.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00764, ECO:0000269|PubMed:1713691, ECO:0000269|PubMed:8918793}.
Interaction partners:
- Endonuclease III homolog lyase)
- Flap endonuclease 1
- DNA repair endonuclease XPF
- DNA ligase 1
- N-glycosylase/DNA lyase
- rRNA 2'-O-methyltransferase fibrillarin
- rRNA 2'-O-methyltransferase fibrillarin
- Nucleolar protein 56
- Proliferating cell nuclear antigen
- Nucleolar protein 58
Sequence:
MPRVKAVKKQAEALASEPTDPTPNANGNGVDENADSAAEELKVPAKGKPRARKATKTAVSAENSEEVEPQKAPTAAARGKKKQPKDTDENGQMEVVAKPKGRAKKATAEAEPEPKVDLPAGKATKPRAKKEPTPAPDEVTSSPPKGRAKAEKPTNAQAKGRKRKELPAEANGGAEEAAEPPKQRARKEAVPTLKEQAEPGTISKEKVQKAETAAKRARGTKRLADSEIAAALDEPEVDEVPPKAASKRAKKGKMVEPSPETVGDFQSVQEEVESPPKTAAAPKKRAKKTTNGETAVELEPKTKAKPTKQRAKKEGKEPAPGKKQKKSADKENGVVEEEAKPSTETKPAKGRKKAPVKAEDVEDIEEAAEESKPARGRKKAAAKAEEPDVDEESGSKTTKKAKKAETKTTVTLDKDAFALPADKEFNLKICSWNVAGLRAWLKKDGLQLIDLEEPDIFCLQETKCANDQLPEEVTRLPGYHPYWLCMPGGYAGVAIYSKIMPIHVEYGIGNEEFDDVGRMITAEYEKFYLINVYVPNSGRKLVNLEPRMRWEKLFQAYVKKLDALKPVVICGDMNVSHMPIDLENPKNNTKNAGFTQEERDKMTELLGLGFVDTFRHLYPDRKGAYTFWTYMANARARNVGWRLDYCLVSERFVPKVVEHEIRSQCLGSDHCPITIFFNI
Protein: FI16115p1 (Sclp, isoform C) (H0RNK3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Polyprenal reductase
Sequence:
MRPFGNDITNIPNGGNNGGNNGGNNGNNDPNDGNDNRNTNISSEDPSEESGLSDDPSIPPHIARIGGIVTCPPIAGQGVIRVVQRCEDAKENHKLDLSSCELMQIPDAVYHLMRNTELITCNLSGNVLKSVSPKFSQKFSTITDLNLSHNKLSRLPEEFASLSALTKLNISNNSFIVLPQVVFKLQSLASLDAQNNAILEIDTDEAITSDNLALVDLRNNPLSRNCRRKLQSFKTPFHLEISKDVEDDWFLTKSREITRWDSHLGFGNFSNYDSTRKRGTANSYPVMSHVSIRRQITANKSWFMTFRKRTSDFFGLPSLFQLLLKFQNVLGLKMGILGF
Protein: Neuronal acetylcholine receptor subunit alpha-7 (nAChR7) (Nicotinic acetylcholine receptor subunit alpha-7) (P22770)
Organism: Gallus gallus (Chicken)
Function: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Subcellular location: Postsynaptic cell membrane {ECO:0000250|UniProtKB:P36544}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:P36544}; Multi-pass membrane protein {ECO:0000255}. Note=TMEM35A/NACHO promotes its trafficking to the cell membrane (By similarity). RIC3 promotes its trafficking to the cell membrane (By similarity). {ECO:0000250|UniProtKB:P36544, ECO:0000250|UniProtKB:Q05941}.
Interaction partners:
- Dynein axonemal heavy chain 10.
- Uncharacterized protein.
- Ess-2 splicing factor homolog.
Sequence:
MGLRALMLWLLAAAGLVRESLQGEFQRKLYKELLKNYNPLERPVANDSQPLTVYFTLSLMQIMDVDEKNQVLTTNIWLQMYWTDHYLQWNVSEYPGVKNVRFPDGLIWKPDILLYNSADERFDATFHTNVLVNSSGHCQYLPPGIFKSSCYIDVRWFPFDVQKCNLKFGSWTYGGWSLDLQMQEADISGYISNGEWDLVGIPGKRTESFYECCKEPYPDITFTVTMRRRTLYYGLNLLIPCVLISALALLVFLLPADSGEKISLGITVLLSLTVFMLLVAEIMPATSDSVPLIAQYFASTMIIVGLSVVVTVIVLQYHHHDPDGGKMPKWTRVILLNWCAWFLRMKRPGEDKVRPACQHKQRRCSLSSMEMNTVSGQQCSNGNMLYIGFRGLDGVHCTPTTDSGVICGRMTCSPTEEENLLHSGHPSEGDPDLAKILEEVRYIANRFRDQDEEEAICNEWKFAASVVDRLCLMAFSVFTIICTIGILMSAPNFVEAVSKDFA
Protein: Protein inhibitor of activated STAT, 1 (A0A8I6AJT7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus, nuclear body {ECO:0000256|ARBA:ARBA00034306}.
Interaction partners:
Sequence:
MVSDTNILHFTFFPKQMVMSLRVSELQVLLGYAGRNKHGRKHELLTKALHLLKAGCSPAVQMKIKELYRRRFPQKIMTPADLSIPNVHSSPMPATLSPSTIPQLTYDGHPASSPLLPVSLLGPKHELELPHLTSALHPVHPDIKLQKLPFYDLLDELIKPTSLASDNSQRFRETCFAFALTPQQVQQISSSMDISGTKCDFTVQVQLRFCLSETSCPQEDHFPPNLCVKVNTKPCSLPGYLPPTKNGVEPKRPSRPINITSLVRLSTTVPNTIVVSWTAEIGRTYSMAVYLVKQLSSTVLLQRLRAKGIRNPDHSRALIKEKLTADPDSEIATTSLRVSLLCPLGKMRLTIPCRALTCSHLQCFDATLYIQMNEKKPTWVCPVCDKKAPYEHLIIDGLFMEILKYCTDCDEIQFKEDGSWAPMRSKKEVQEVTASYNGVDGCLSSTLEHQVASHNQSSNKNKKVEVIDLTIDSSSDEEEEEPPAKRTCPSLSPTSPLSNKGILSLPHQASPVSRTPSLPAVDTSYINTSLIQDYRHPFHMTPMPYDLQGLDFFPFLSGDNQHYNTSLLAAAAAAVSDDQDLLHSSRFFPYTSSQMFLDQLSAGGSTSLPATNGSSSGSNSSLVSSNSLRESHGHGVASRSSADTASIFGIIPDIISLD
Protein: Uncharacterized protein YGR122W (P53272)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Calpain-like protease 1
- pH-response regulator protein palA/RIM20
- Vacuolar-sorting protein SNF7
- pH-response transcription factor pacC/RIM101
- Protein DFG16
- pH-response regulator protein palH/RIM21
- pH-response regulator protein palF/RIM8
- pH-response regulator protein palI/RIM9
Sequence:
MRENAMSTKKLPYKLSGSSKITTSIPNDLIILRNNCINSLNSSSSKADSITCIDTWLKYTEGLLTHRYEANNDAALIEEEIAIALINVAVFYQDIGIETLYRAYESSQASNNLWTTSGTYLKRGLGLICFLGKNFQINTANDCQKMQVLNVLNQLSLEFQLLQQLGIVVLALSKLRSKISKDAVADLEPQELEELGKSSVFYAKLCIGSYSTASQCQGGRIVDALFMNYLQSLTYLFLSINQYNNDECGIAIGMLQESIKKLLNIVPNSQLKELDILSSTDITKKRDLIKMSFKRKIHGSTLKNQRIFEKKVPFSSKAYMMPLLKSSLDDFVIPLTILLRYRYQTTNENYSFKTVETDVSKLKELFPRGKSSDIEGTVWSFQDGHLTFADSNNATHNCGNYF
Protein: U-box domain-containing protein 57 (EC 2.3.2.27) (Plant U-box protein 57) (OsPUB57) (RING-type E3 ubiquitin transferase PUB57) (Q0DR28)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Possesses E3 ubiquitin-protein ligase in vitro. May be involved in cell death signaling.
Interaction partners:
Sequence:
MQTGFSNSRMNSFISSVLVLHFNKQEIKFEPSVWCEAIDIHNTFSAGEIITGDIICFQKILKPPDIPKYPSVASFLQHVCDRKTYEEVRKVHILEEEIVTLKHQADTYLVQKEKAVTAYDQLKHERDNAVQQVNELRDQSTHIILDFSRKDMEQATEHFKNAREVGDTEYGHTYKGMIHNMKVLIKLSSSQKLFQQEVSILRQWRHPNIITFIGVCSEVSALVYEWLPNGNLEDRIICTNNSAPLSWYNRTQIIGEICCALLFLHSNKSTALVHGDLRPCNILIDANYRSKICNFGMSNLFLQLGTFPPNLTARLPYMDPEFNTTGELTTLSDVYSLGVIILRLLTGMPPLTLSEKVAEALGSDSLHLLIDKSAGDWPYIEAKQLALIGLSCTGMTRKKRPDLLNEVWIVIEPLTRKPPAATWPYLQSASGDSSVPAAFICPISMEIMKDPQVASDGFTYEAEAIRCWFDRGISRSPMTNLALPNLNLVPNRVLRSFIHGYLQQQQPNPAYQQQLSET
Protein: Sulfate adenylyltransferase subunit 1 (EC 2.7.7.4) (ATP-sulfurylase large subunit) (Sulfate adenylate transferase) (SAT) (P23845)
Organism: Escherichia coli (strain K12)
Function: With CysD forms the ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric-sulfuric acid anhydride bond driven by GTP hydrolysis by CysN coupled to ATP hydrolysis by CysD.
Interaction partners:
- Sulfate/thiosulfate import ATP-binding protein CysA
- Sulfate-binding protein
- Adenylyl-sulfate kinase
- Sulfite reductase flavoprotein alpha-component
- Thiosulfate-binding protein
- Sulfate adenylyltransferase subunit 2
- Sulfate transport system permease protein CysW
- Sulfite reductase hemoprotein beta-component
- Phosphoadenosine 5'-phosphosulfate reductase
- Sulfate transport system permease protein CysT
Sequence:
MNTALAQQIANEGGVEAWMIAQQHKSLLRFLTCGSVDDGKSTLIGRLLHDTRQIYEDQLSSLHNDSKRHGTQGEKLDLALLVDGLQAEREQGITIDVAYRYFSTEKRKFIIADTPGHEQYTRNMATGASTCELAILLIDARKGVLDQTRRHSFISTLLGIKHLVVAINKMDLVDYSEETFTRIREDYLTFAGQLPGNLDIRFVPLSALEGDNVASQSESMPWYSGPTLLEVLETVEIQRVVDAQPMRFPVQYVNRPNLDFRGYAGTLASGRVEVGQRVKVLPSGVESNVARIVTFDGDREEAFAGEAITLVLTDEIDISRGDLLLAADEALPAVQSASVDVVWMAEQPLSPGQSYDIKIAGKKTRARVDGIRYQVDINNLTQREVENLPLNGIGLVDLTFDEPLVLDRYQQNPVTGGLIFIDRLSNVTVGAGMVHEPVSQATAAPSEFSAFELELNALVRRHFPHWGARDLLGDK
Protein: Sulfite oxidase, mitochondrial (EC 1.8.3.1) (Q8R086)
Organism: Mus musculus (Mouse)
Function: Catalyzes the oxidation of sulfite to sulfate, the terminal reaction in the oxidative degradation of sulfur-containing amino acids.
Subcellular location: Mitochondrion intermembrane space {ECO:0000250|UniProtKB:Q07116}.
Interaction partners:
- Persulfide dioxygenase ETHE1, mitochondrial
- Thiosulfate sulfurtransferase
- 3-mercaptopyruvate sulfurtransferase
- NADH-cytochrome b5 reductase 3
- Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 2
- NADH-cytochrome b5 reductase 1
- Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1
- NADH-cytochrome b5 reductase 2
- Aldehyde oxidase 3
- Sulfide:quinone oxidoreductase, mitochondrial
Sequence:
MLLQLYRSVVVRLPQAIRVKSTPLRLCIQACSTNDSLEPQHPSLTFSDDNSRTRRWKVMGTLLGLGVVLVYHEHRCRASQESPRMYSKEDVRSHNNPKTGVWVTLGSEVFDVTKFVDLHPGGPSKLMLAAGGPLEPFWALYAVHNQPHVRELLAEYKIGELNPEDSMSPSVEASDPYADDPIRHPALRINSQRPFNAEPPPELLTEGYITPNPIFFTRNHLPVPNLDPHTYRLHVVGAPGGQSLSLSLDDLHKFPKHEVTVTLQCAGNRRSEMSKVKEVKGLEWRTGAISTARWAGARLCDVLAQAGHRLCDSEAHVCFEGLDSDPTGTAYGASIPLARAMDPEAEVLLAYEMNGQPLPRDHGFPVRVVVPGVVGARHVKWLGRVSVESEESYSHWQRRDYKGFSPSVDWDTVNFDLAPSIQELPIQSAITQPQDGAIVESGEVTIKGYAWSGGGRAVIRVDVSVDGGLTWQEAELEGEEQCPRKAWAWRIWQLKAQVPAEQKELNIICKAVDDSYNVQPDTVAPIWNLRGVLSNAWHRVHVQVVP
Protein: Exosome complex component RRP45 (Exosome component 9) (Q4QR75)
Organism: Rattus norvegicus (Rat)
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 promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. 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. EXOSC9 binds to ARE-containing RNAs (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q06265}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q06265}. Nucleus {ECO:0000250|UniProtKB:Q06265}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q06265}. Note=Colocalizes with SETX in nuclear foci upon induction of transcription-related DNA damage at the S phase (By similarity). {ECO:0000250|UniProtKB:Q06265}.
Interaction partners:
- Exosome complex component RRP40
- Exosome component 7
- Exosome complex component CSL4
- Exosome complex component RRP41
- Exosome complex component RRP46
- Exosome complex component RRP4
- Exosome complex component MTR3
- Exosome complex exonuclease RRP44
- DIS3-like exonuclease 1
- Exosome complex component RRP43
Sequence:
MKETPLSNCERRFLLRAIEEKKRLDGRQTYDYRNIRISFGTDYGCCIVELGKTRVLGQVSCELVSPKLNRATEGILFFNLELSQMAAPAFEPGRQSDLLVKLNRLLERCLRNSKCIDTESLCVVAGEKVWQIRVDLHLLNHDGNIIDAASIAAIVALCHFRRPDVSVQGEEVTLYTPEERDPVPLSIHHMPICVSFAFFQQGTYLLVDPNEREERVMDGLLVIAMNKHREICTIQSSGGIMLLKDQVFRCSKIAGVKVAEITELIQKALENDQRVRKEGGKFGFAESIANQRITAFKMEKAPIDTSNIEEKAEEIIAEAEPPPEVVSKPVLWTPGTAQIGEGIENSWGDLEDSEKEEEEEGGIDETVILDDTKMDTGEVSDIGSQGAPIVLSDSEEEEMIILEPEKSPKKIRAQTSANQKAPSKSQGKRRKKKRTAN
Protein: Starvin, isoform B (Starvin, isoform D) (Starvin, isoform G) (Q9VU83)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDMDNMFPRSHLGRMHDPFAGFGDSHFGFPRFSTMGRRGRMAGGANTHMDHDDDFFNRLPSEFRQYIPDGFGGRRGTGAAPAPGQVPQQQQPQPQPQYTQQQPQTHFQFGVPPQQQPVYAGPTQQQVPQTPSKRLCDAAIQTEDPAGRSEVDCAPPTNLNQHGLRNTVDMGVKSVAEQDQGLRSHSAPPPEQQQQNLQYHQQQQQHQQPGVHSQPFGTQTSPPVQGQQFKTYYAPHQQTHPQQKQQTPPPAPQTPGGTYVRTIPIFVEGRSEPIINAHKEIPNQNAPPSAQAQAQAQAYAQAQPQAHAAPQQHNRPTPLNTQAQPEQQVPVEGAAGLPPQTPHTLNSINKIQDIQRDVLELMGKVEQFKGTREEKEYAYLDEMLTRNLLKLDTIDTNGKDSIRLARKEAIKCIQASINVLEAKAEENARAASGAAPAPSATAPAVDTGAVAASEAAGQNAEPVTPQPQDATKMQEPIPLPAPPNAAAVEGAAASEATAAEATQSAVQSETTTTTSE
Protein: Sperm histone (Galline) (Protamine) (P15340)
Organism: Gallus gallus (Chicken)
Function: Protamines substitute for histones in the chromatin of sperm during the haploid phase of spermatogenesis. They compact sperm DNA into a highly condensed, stable and inactive complex.
Subcellular location: Nucleus. Chromosome.
Interaction partners:
Sequence:
MARYRRSRTRSRSPRSRRRRRRSGRRRSPRRRRRYGSARRSRRSVGGRRRRYGSRRRRRRRY