wanglab/gogpt-training-data huggingface dataset:
Protein: Interleukin-1 beta (IL-1 beta) (P26889)
Organism: Sus scrofa (Pig)
Function: Potent pro-inflammatory cytokine. Initially discovered as the major endogenous pyrogen, induces prostaglandin synthesis, neutrophil influx and activation, T-cell activation and cytokine production, B-cell activation and antibody production, and fibroblast proliferation and collagen production. Promotes Th17 differentiation of T-cells. Synergizes with IL12/interleukin-12 to induce IFNG synthesis from T-helper 1 (Th1) cells. Plays a role in angiogenesis by inducing VEGF production synergistically with TNF and IL6. Involved in transduction of inflammation downstream of pyroptosis: its mature form is specifically released in the extracellular milieu by passing through the gasdermin-D (GSDMD) pore.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P01584}. Secreted {ECO:0000250|UniProtKB:P01584}. Lysosome {ECO:0000250|UniProtKB:P01584}. Secreted, extracellular exosome {ECO:0000250|UniProtKB:P10749}. Note=The precursor is cytosolic. In response to inflammasome-activating signals, such as ATP for NLRP3 inflammasome or bacterial flagellin for NLRC4 inflammasome, cleaved and secreted. Mature form is secreted and released in the extracellular milieu by passing through the gasdermin-D (GSDMD) pore. In contrast, the precursor form is not released, due to the presence of an acidic region that is proteolytically removed by CASP1 during maturation. The secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10. {ECO:0000250|UniProtKB:P01584}.
Interaction partners:
- Interleukin-1 alpha
- Caspase-1
- Interleukin-1 receptor type 1
- Interleukin 1 receptor type 2.
- NACHT, LRR and PYD domains-containing protein 3
- Interleukin-10
- Apoptosis-associated speck-like protein containing a CARD
- Interleukin-6
- Interleukin-18
- Interferon gamma
Sequence:
MAIVPEPAKEVMANYGDNNNDLLFEADGPKEMKCCTQNLDLGSLRNGSIQLQISHQLWNKSIRQMVSVIVAVEKPMKNPSSQAFCDDDQKSIFSFIFEEEPIILETCNDDFVCDANVQSMECKLQDKDHKSLVLAGPHMLKALHLLTGDLKREVVFCMSFVQGDDSNNKIPVTLGIKGKNLYLSCVMKDNTPTLQLEDIDPKRYPKRDMEKRFVFYKTEIKNRVEFESALYPNWYISTSQAEQKPVFLGNSKGRQDITDFTMEVLSP
Protein: Sarcoplasmic/endoplasmic reticulum calcium ATPase 2 (SERCA2) (SR Ca(2+)-ATPase 2) (EC 7.2.2.10) (Calcium pump 2) (Calcium-transporting ATPase sarcoplasmic reticulum type, slow twitch skeletal muscle isoform) (Endoplasmic reticulum class 1/2 Ca(2+) ATPase) (Q03669)
Organism: Gallus gallus (Chicken)
Function: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Isoform SERCA2A is involved in the regulation of the contraction/relaxation cycle. May act as a regulator of TNFSF11-mediated Ca(2+) signaling during osteoclastogenesis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O55143}; Multi-pass membrane protein {ECO:0000255}. Sarcoplasmic reticulum membrane {ECO:0000250|UniProtKB:O55143}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Phospholamban
- Sarcolipin
- Sarcoplasmic/endoplasmic reticulum calcium ATPase 3
- Ryanodine receptor 2.
- Plasma membrane calcium-transporting ATPase 1
- Sodium/calcium exchanger 1
- Coiled-coil domain containing 92
- Calcium-transporting ATPase
Sequence:
MENAHTKTVEEVLAYFGVNESTGLSLEQVKKLKEKWGSNELPAEEGKTLLELVIEQFEDLLVRILLLAACISFVLAWFEEGEETITAFVEPFVILLILVANAIVGVWQERNAENAIEALKEYEPEMGKVYRQDRKSVQRIKARDIVPGDIVEVAVGDKVPADIRITSIKSTTLRVDQSILTGESVSVIKHTDPVPDPRAVNQDKKNMLFSGTNIAAGKAMGVVIATGVNTEIGKIRDEMVATEQERTPLQQKLDEFGEQLSKVISLICIAVWIINIGHFNDPVHGGSWIRGAIYYFKIAVALAVAAIPEGLPAVITTCLALGTRRMAKKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVCRMFILDKVEGDSCSLNEFTVTGSTYAPMGEVHKDDKLIKCSQYDGLVELATICALCNDSSLDYNEAKGVYEKVGEATETALTCLVEKMNVFDTDLKGLSRIERANACNSVIKQLMKKEFTLEFSRDRKSMSVYCTPNKPSRTSMSKMFVKGAPEGVIDRCTHVRVGNAKIPLSSGIKQKIMSVIREWGTGRDTLRCLALATHDNPPRKEEMNLEDSSNFINYETNLTFVGCVGMLDPPRIEVASSIKLCKQAGIRVIMITGDNKGTAVAICRRIGIFVEDEDVSTKAFTGREFDELSLAAQRDACHHARCFARVEPSHKSKIVEFLQSFDEITAMTGDGVNDAPALKKAEIGIAMGSGTAVAKTASEMVLADDNFSTIVAAVEEGRAIYNNMKQFIRYLISSNVGEVVCIFLTAALGFPEALIPVQLLWVNLVTDGLPATALGFNPPDLDIMNKPPRNPKEPLISGWLFFRYLAIGCYVGAATVGAAAWWFIAADGGPRVTFYQLSHFLQCKEDNPDFSGVDCVVFESPYPMTMALSVLVTIEMCNALNSLSENQSLMRMPPWENIWLVGAICLSMSLHFLILYVEPLPIIFQITPLNVTQWLMVLKISLPVILLDETLKYVARNYLEPGKDSVQPATKPCSLSACTEGVSWPFVFITLPLVIWLYSTDTNFSDMFW
Protein: Adenylate kinase (EC 2.7.4.3) (ATP-AMP transphosphorylase) (ATP:AMP phosphotransferase) (Adenylate kinase cytosolic and mitochondrial) (Adenylate monophosphate kinase) (P33075)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. Adenylate kinase activity is critical for regulation of the phosphate utilization and the AMP de novo biosynthesis pathways.
Subcellular location: Cytoplasm, cytosol {ECO:0000255|HAMAP-Rule:MF_03168, ECO:0000269|PubMed:16823372}. Mitochondrion intermembrane space {ECO:0000255|HAMAP-Rule:MF_03168}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Adenosine kinase
- Ribonucleoside-diphosphate reductase large chain
- Nucleoside diphosphate kinase
- Adenine phosphoribosyltransferase
- Adenylosuccinate lyase
- Ribonucleoside-diphosphate reductase small chain
- Guanylate kinase
- Adenylate kinase isoenzyme 6 homolog
- Thymidylate kinase
- AMP deaminase
Sequence:
MAGMRLILVGPPGAGKGTQAPNIQKKYGIAHLATGDMLRSQVARQTELGKEAKKIMDQGGLVSDDIVTGMIKDEILNNPECKNGFILDGFPRTVVQAEKLTALLDELKLDLNTVLELQVDDELLVRRITGRLVHPGSGRSYHLEFNPPKVPMKDDVTGEPLIQRSDDNADALRKRLVTYHEQTTPVVEFYKKKGKWAAVDAAQKPEQVWEQIVAILEKAE
Protein: At1g68680 (SH3/FCH domain protein) (Q8L9R6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- At5g14105
- At4g16450
- MICOS complex subunit, putative
- Mitochondrial import inner membrane translocase subunit TIM22-1
- Mitochondrial import inner membrane translocase subunit TIM22-4
- At2g28430/T1B3.5
- AT3g52230/F4F15_340
- At2g46540/F11C10.23
- Early endosome antigen
- Expressed protein
Sequence:
MASSSDPSKPVMERKKKGAPIKFLVPLIYAPALPLIRLSLRHKPVLRDRLFGLVLVGAFAHGFYLVTDIYDAESK
Protein: Shaggy-related protein kinase epsilon (EC 2.7.11.1) (ASK-epsilon) (Shaggy-related protein kinase 13) (AtSK13) (Q8VZD5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May mediate extracellular signals to regulate transcription in differentiating cells.
Interaction partners:
- HR-like lesion-inducing protein
- At3g23190
- Serine/threonine-protein kinase BSK6
- Protein phosphatase 2C and cyclic nucleotide-binding/kinase domain-containing protein
- 14-3-3-like protein GF14 phi
- Hydroxyproline-rich glycoprotein family protein
- Serine/threonine-protein phosphatase BSL3
- Pre-rRNA-processing ESF1-like protein
- Probable ADP-ribosylation factor GTPase-activating protein AGD13
- Protein LIFEGUARD 2
Sequence:
MASVGTLPASSMATKQSNASICAEKLPEGINEMKIKDDKEMEAAVVDGNGTETGHIIVTTIGGKNGQPKQTISYMAERIVGQGSFGIVFQAKCLETGETVAIKKVLQDKRYKNRELQTMRLLDHPNVVSLKHCFFSTTEKDELYLNLVLEYVPETVYRVSKHYSRANQRMPIIYVKLYTYQICRALAYIHGGVGVCHRDIKPQNLLVNPHTHQVKLCDFGSAKVLVKGEPNISYICSRYYRAPELIFGATEYTTTIDIWSAGCVLAELLLGQPLFPGESGVDQLVEIIKVLGTPTREEIKCMNPNYTEFKFPQIKAHPWHKIFHKRTPPEAVDLVSRLLQYSPNLRSTAMEAIVHPFFDELRDPNTRLPNGRALPPLFNFKPQELKGASLELLSKLIPDHARKQCSFLAL
Protein: Alanine aminotransferase 1, mitochondrial (AtAlaAT1) (AtAlaATc) (EC 2.6.1.2) (Alanine-2-oxoglutarate aminotransferase 4) (EC 2.6.1.-) (F4I7I0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Is the major alanine aminotransferase in roots that catalyzes the conversion of alanine to pyruvate. Involved in the rapid conversion of alanine to pyruvate during recovery from low-oxygen stress.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14671022}.
Interaction partners:
- Aspartate aminotransferase, chloroplastic
- Alanine--glyoxylate aminotransferase 2 homolog 3, mitochondrial
- Pyruvate, phosphate dikinase 1, chloroplastic
- Serine--glyoxylate aminotransferase
- Aspartate aminotransferase, mitochondrial
- Glutamate dehydrogenase 1
- Alanine--glyoxylate aminotransferase 2 homolog 2, mitochondrial
- NAD-dependent malic enzyme 2, mitochondrial
- Alanine--glyoxylate aminotransferase 2 homolog 1, mitochondrial
- Glutamate dehydrogenase 2
Sequence:
MRRFVIGQAKNLIDQSRRRQLHHHKNLSFVSLIPPFSAPSDSSSRHLSSSSSSDMSASDSSSSLPVTLDTINPKVIKCEYAVRGEIVNIAQKLQEDLKTNKDAYPFDEIIYCNIGNPQSLGQQPITFFREVLALCSYTALLDESATHGLFSSDSIERAWKILDQIPGRATGAYSHSQGIKGLRDAIADGIEARDGFPADPNDIFMTDGASPGVHMMMQLLITSEKDGILCPIPQYPLYSASIALHGGTLVPYYLDEASGWGLEISELKKQLEDARSKGITVRALAVINPGNPTGQVLSEENQRDVVKFCKQEGLVLLADEVYQENVYVPDKKFHSFKKVARSMGYGEKDLALVSFQSVSKGYYGECGKRGGYMEVTGFTSDVREQIYKMASVNLCSNISGQILASLIMSPPKPGDDSYESYIAEKDGILSSLARRAKTLEEALNKLEGVTCNRAEGAMYLFPCLHLPQKAIAAAEAEKTAPDNFYCKRLLKATGIVVVPGSGFRQVPGTWHFRCTILPQEDKIPAIVDRLTAFHQSFMDEFRD
Protein: Phosphatidylinositol 3-kinase age-1 (PI3-kinase age-1) (PI3K age-1) (PtdIns-3-kinase age-1) (EC 2.7.1.137) (Aging alteration protein 1) (Q94125)
Organism: Caenorhabditis elegans
Function: Phosphatidylinositol 3-kinase homolog that regulates longevity and diapause. Promotes cell survival during embryonic development by recruiting akt-1/2 to the plasma membrane through the production of PtdIns(3,4,5)P3. Could function in the development or neuroendocrine signaling of the dauer pathway. Mediates susceptibility to enteropathogenic E.coli infection. May negatively regulate AYI interneuron neurite outgrowth. Plays a role in aversive olfactory learning when an odor is associated with food deprivation. Regulates this process by promoting the nuclear relocalization of egl-4 in AWC olfactory neurons after odor conditioning.
Interaction partners:
- Phosphoinositide 3-kinase adapter subunit
- Insulin-like receptor
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase daf-18
- Serine/threonine-protein kinase akt-1
- Serine/threonine-protein kinase akt-2
- Forkhead box protein O
- Target of rapamycin homolog
- Ras protein let-60
- 1-phosphatidylinositol-5-phosphate 4-kinase
- PIPK domain-containing protein
Sequence:
MSMGRSPSTTFRSRTGSHGARDLIAGHGRNSRRISQMHVNILHPQLQTMVEQWQMRERPSLETENGKGSLLLENEGVADIITMCPFGEVISVVFPWFLANVRTSLEIKLSDFKHQLFELIAPMKWGTYSVKPQDYVFRQLNNFGEIEVIFNDDQPLSKLELHGTFPMLFLYQPDGINRDKELMSDISHCLGYSLDKLEESLDEELRQFRASLWARTKKTCLTRGLEGTSHYAFPEEQYLCVGESCPKDLESKVKAAKLSYQMFWRKRKAEINGVCEKMMKIQIEFNPNETPKSLLHTFLYEMRKLDVYDTDDPADEGWFLQLAGRTTFVTNPDVKLTSYDGVRSELESYRCPGFVVRRQSLVLKDYCRPKPLYEPHYVRAHERKLALDVLSVSIDSTPKQSKNSDMVMTDFRPTASLKQVSLWDLDANLMIRPVNISGFDFPADVDMYVRIEFSVYVGTLTLASKSTTKVNAQFAKWNKEMYTFDLYMKDMPPSAVLSIRVLYGKVKLKSEEFEVGWVNMSLTDWRDELRQGQFLFHLWAPEPTANRSRIGENGARIGTNAAVTIEISSYGGRVRMPSQGQYTYLVKHRSTWTETLNIMGDDYESCIRDPGYKKLQMLVKKHESGIVLEEDEQRHVWMWRRYIQKQEPDLLIVLSELAFVWTDRENFSELYVMLEKWKPPSVAAALTLLGKRCTDRVIRKFAVEKLNEQLSPVTFHLFILPLIQALKYEPRAQSEVGMMLLTRALCDYRIGHRLFWLLRAEIARLRDCDLKSEEYRRISLLMEAYLRGNEEHIKIITRQVDMVDELTRISTLVKGMPKDVATMKLRDELRSISHKMENMDSPLDPVYKLGEMIIDKAIVLGSAKRPLMLHWKNKNPKSDLHLPFCAMIFKNGDDLRQDMLVLQVLEVMDNIWKAANIDCCLNPYAVLPMGEMIGIIEVVPNCKTIFEIQVGTGFMNTAVRSIDPSFMNKWIRKQCGIEDEKKKSKKDSTKNPIEKKIDNTQAMKKYFESVDRFLYSCVGYSVATYIMGIKDRHSDNLMLTEDGKYFHIDFGHILGHGKTKLGIQRDRQPFILTEHFMTVIRSGKSVDGNSHELQKFKTLCVEAYEVMWNNRDLFVSLFTLMLGMELPELSTKADLDHLKKTLFCNGESKEEARKFFAGIYEEAFNGSWSTKTNWLFHAVKHY
Protein: Mucin 16 (A0A140LIA5)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
XYHHQYWTPKTSTTNPSLVPFTLNFTITNLHHTEGMASQGSEIFNSTERILNSLLKPMFKNSSIGHLYSGCRLITLRPEKDGTATGVDAVCTLHSDPLGLQLDREKMYWELSHNTQGVTKLGSFTLEKDSLYINGFTHIKTSASTLNTPVTSSLFFTETSTAKPTLSTVPGSPLVPFIINFTITNLEYEEGMSHAGSWKFNATEKILQRLLWSLFNKTSIGLLYSDCRLALLRPEKDGAATGVDAICTHHAGPIGPGLDSERVFWELCNLTNNVTKLGPYTLDKNSLYINGYTHQIQSITSPTTSPSLLPFTLNFTITNLQHTEGMAFQGSEIFNNTERILNSLLKPIFKNSSIGHLYYGCRLISL
Protein: Adenosylhomocysteinase (AdoHcyase) (EC 3.13.2.1) (S-adenosyl-L-homocysteine hydrolase) (O13639)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Adenosylhomocysteine is a competitive inhibitor of S-adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine.
Interaction partners:
- Probable 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
- Cystathionine beta-lyase
- Probable cystathionine gamma-synthase
- Cysteine synthase 1
- Cysteine synthase 2
- Homocysteine synthase
- S-adenosylmethionine synthase
- Uncharacterized protein C57A7.07c
- Threonine dehydratase, mitochondrial
- Methylthioribulose-1-phosphate dehydratase
Sequence:
MATQNYKVADISLAAFGRKELEIAENEMPGLIAVREKYAKSQPLKGARIAGCLHMTIQTAVLIETLVALGAEVTWSSCNIYSTQDHAAAAIAATGVPVFAWKGETEEEYLWCIEQQLKSFPSGKPLNMILDDGGDLTALVHERHPELLVDIRGISEETTTGVHNLYKMFKENKLKVPAINVNDSVTKSKFDNLFGCKESLVDGIKRATDVMIAGKVAVVAGFGDVGKGCSTSLRSQGARVIVTEVDPINALQAAMDGFEVTTMEEAVKEGQIFVTTTGCRDIIRGEHFNEMKEDSIVCNIGHFDVEIDVAWLKANAKDVVNIKPQVDRYELKNGRHIILLADGRLVNLGCATGHPSFVMSCSFTNQVLAQIALWTDNTSYPLGVHMLPKKLDEEVARLHLGKLGVKLTTLTSVQSDYLGIPVDGPYKADHYRY
Protein: Basement membrane proteoglycan (H9G352)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MKRSSTVLAALLALLLVATNDAARHRKYRQTYQDIDSDDDDTSDVQITVFPSEKEVRDGRDVSFECRARTSDNSVYPTVRWARVGGPLPSSAHDSGGRLTINPVQLSDAGTYICVSDYNGNTVEARATLSVVSYGPQEVSNGLRQAGQCMADEKACGNNECVKNDYVCDGEPDCRDRSDEANCPAISRTCEPNEFKCNNNKCVQKMWLCDGDDDCGDNSDELNCNAKPSSSDCKPTEFQCHDRRQCVPSSFHCDGTNDCHDGSDEVGCVQPTVVDPPQTNLQVPRGTTFSLTCKAVAVPEPYINWRLNWGPVCEPPRCLQTSEGGYGTLTIHDAQPVDQGAYTCEAINVKGRVLATPDCIVRVVDDPRPQPPQPPTAPPQRASCDTRGAVTPYPNNYGTCECKSQVTGPNCDQCKPGAFHLSEKSPEGCLKCFCFGVSNDCRSSGHYRTKVSIDYARGDRDQLELTTSDSRQPYSPQTRAELSGQAIEFRSFEEARGQTLYWKLPEKFLGDKVTSYGGTLEYTFKFSGNGNSDQSADVILRGNDIALQYKHREPFYADRENKVQIKIIETSWQRVDGQQATREHLLMTLADLDTLLIKSTYNDDCTDSQLLSANLEFAEPYGQGLTAAEVEQCICPPGYVGTSCEDCAPGYSRTGGGLYLGLCEKCECNGHASQCDKEYGYCLDCQHNTEGDQCERCKPGFVGDARRGTPNDCQPEATRAPCHCNNHSPRGCDSFGRCLLCEHNTEGTHCERCKKGYYGDATKGSPYDCTPCPCPGASDCYLDNEGQVACRICPAGLQGRLCNECAPGYTRSNKPAGRVCEPIGQVTNEDITFVQKPHEVLRVRIMEPKRQIALPGDRVHWICQVTGYTTEKIHVEWTKVGEMSLPPNAKAYDGYLVLKGVEAENAGQYRCTATTITQYATDDALLTISKRISGRPPQPVIDPPHLVVNEGEPAAFRCWVPGIPDCQITWHREQLGGPLPHGVYQTGNALKIPQSQLHHAGRYICSAANQYGTGQSPPAVLEVKKPVIPPKVDPIRQTVDRDQPARFKCWVPGNSNVQLRWSRPGGAPLPSGVQEQQGILHIPRASDQEVGQYVCTATDPSDNTPLQSEPVQLNIRDPAPPQRGAAPQIDPPNQTVNVNDPAQFRCWVPGQPRAQLKWSRKDGRPLPNGILERDGFLRIDKSQLHDAGEYECTSTEPDGSTQLSPPARLNVNQPQAIQPQVDPPVQTVNEGEPSRIRCWVPGHPNIQLQFVKRGRRPLPAHARFSQGNLEIPRTLKSDEDEYICIATDPTTNRPVESNPARVIVKSPIRPIIDPAEQTVPEGSPFKIRCYVPGHPSVQLTFRRVSGQLNEDADENNGLLAVQRAELTDEGDYICTARDPDTGAPIDSTPATVHVTNAAAPPQVEARPPQHPVITPQTQTIPEGDPARIQCTVPGNPSAAQHLSFERVDGKGLPFGSSDDRGVLTIPSTQLQDAGEYVCLYSPENSPPVKTNPSTLNVTPEGTPPRPVATPPLLSVAPGSPARFNCVAHSDTPARIRWGFREENGPLPEHVNQDGDDIVISEAGDRNVGEYVCSATNDFGTGVADPVRLEVTEDQEPPTAVVEPRTWNGKPGERHQFRCITTGSPTPKITWTGPNGSPLPHDVTPLEPNILDFSNGRSELNGDYTCTASNPIGEASDHGNVNIGPSLTVKTNPPGPKLIVTVGEPLQVKCEAFGAPGDPEPEVEWLHDPGPERGDLPDDFKPVTISEQFIRHPNVGLGNAGVYTCKGSSAHATATKNIYIEVVEPSRIATVSILGGSSQWFDQGEKGELICTATGSSLVDRLEWEKVDDQLPTDVEEHNEPGLLHFPSFKNSYAGEYRCNGYRNNEIIASAAVHVHSSANADDEPKVEIEPPRVRVVSQGDNIVLKCSVQGAENGEHFKWALLRGGSLVRQLGTEPTLEITKADPSNDFGVYRCNVEDNNGLVIGSAFTAVSVGQQDKSHAQIVKFDDKSDASFTCPIYSVPGSKVDWTYENGDLPSKAVPNGNKIEIKEFDDASAGTYVCKVSFDGNVVEGFVTAQMFVPDTIIQVLLEVSSESPQIGDRAWFDCKVTGDPSAVISWTKEGNDDLPPNAQVTGGRLLFTDLKEDNAGVYRCVAKTKAGPLQTRTVLNVGSGKRKRKHLGNRRGRRLRHRRRNAQNGPLSRKTRTTTKLFGSWF
Protein: Aspartate--tRNA ligase, cytoplasmic (EC 6.1.1.12) (Aspartyl-tRNA synthetase) (AspRS) (P15178)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA.
Subcellular location: Cytoplasm.
Interaction partners:
- Methionine--tRNA ligase, cytoplasmic
- Bifunctional glutamate/proline--tRNA ligase
- Aminoacyl tRNA synthase complex-interacting multifunctional protein 2
- Leucine--tRNA ligase, cytoplasmic
- Glutamine--tRNA ligase
- Isoleucine--tRNA ligase, cytoplasmic
- Lysine--tRNA ligase
- Arginine--tRNA ligase, cytoplasmic
- Aminoacyl tRNA synthetase complex-interacting multifunctional protein 1
- Eukaryotic translation elongation factor 1 epsilon-1
Sequence:
MPSANASRKGQEKPREIVDAAEDYAKERYGVSSMIQSQEKPDRVLVRVKDLTVQKADEVVWVRARVHTSRAKGKQCFLVLRQQQFNVQALVAVGDHASKQMVKFAANINKESIIDVEGIVRKVNQKIGSCTQQDVELHVQKIYVISLAEPRLPLQLDDAIRPEVEGEEDGRATVNQDTRLDNRIIDLRTSTSQAIFHLQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVSYFKSNAYLAQSPQLYKQMCICADFEKVFCIGPVFRAEDSNTHRHLTEFVGLDIEMAFNYHYHEVVEEIADTLVQIFKGLQERFQTEIQTVNKQFPCEPFKFLEPTLRLEYCEALAMLREAGVEMDDEEDLSTPNEKLLGRLVKEKYDTDFYVLDKYPLAVRPFYTMPDPRNPKQSNSYDMFMRGEEILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRDPKRLTP
Protein: DNA polymerase alpha catalytic subunit (EC 2.7.7.7) (O48653)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Polymerase alpha in a complex with DNA primase is a replicative polymerase.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Os05g0358200 protein
- DNA polymerase alpha subunit B
- Os09g0241100 protein
- DNA primase large subunit
- DNA replication licensing factor MCM4
- DNA replication licensing factor MCM5
- DNA polymerase epsilon catalytic subunit
- Proliferating cell nuclear antigen
- DNA polymerase II subunit 2
- DNA polymerase epsilon catalytic subunit
Sequence:
MDEGSADAGASGRRSRARGSEAVARSAALERLRAIRDGGARAAAAVQVRIEAPIYDTVAEEDYAALVARRRKDAGAFIVDDDGLGYADDGREEDWTHRTIHSSSDEGSDGEDGAPRKRKQPRPQSKRPPQQSAAAASLSAAAAMMGKQRLSSMFTSSVFRKPGSDRGRDSSLAADSIVDDVIAEFAPDDNDREERRRRVGRVCAPAPAPTTTAHIKAENVAVDTAMAFRSDNVFEAHEVSDHGNDMDMELKPDVEMEPKLDTPLGASAELANNSNSLEEPKQEANGEVKIEKVHRLNAKIKTEDSRNGDMASATAGWMKICGDGDNAGGEGAVAANSNTGVDESSEFELKDGALPFYILDAYEEPFGANSGTVYLFGKVEVGKRFHSCCVVVKNMQRCIYAIPSSSIFPRDTISRLEKNSTTSDSSPSLRASLHELASGLKSEIADKLSDFNVSNFAMTPVKRNYAFERTDLPNGEQYVLKINYPYKDPALPTDLRGQHFHALLGTNNSALELLLIKRKIKGPSWLSISKFLACPATQRVSWCKFEVTVDSPKDISVLMTSTTLEVPPVVVAAVNLKTIINEKHNVHEIVSASVICCHRVKIDSPMRSEDWQKRGMLSHFTVMRKLEGSIFPIGLSKESSDRNQKAGSNVLALESSERALLNRLMIELSKLDCDVLVGHNISGFDLDVLLHRAQTCKVPSNMWSKIGRLRRSVMPRLTKGNTLYGSGASPGIMSCIAGRLLCDTYLCSRDLLKEVSYSLTQLAETQLKKERKEVSPHDIPPMFQSSGALLKLVEYGETDACLALELMFHLSVLPLTRQLTNISGNLWGKTLQGSRAQRVEYLLLHAFHARKFIVPDKFARSKEFNSTKRKMNPDTEAARPDEADPSIDDEGHHVDQGKTKKGPSYAGGLVLEPKKGLYDKYVLLLDFNSLYPSIIQEYNICFTTVDRSADGNVPNLPASKTTGVLPELLKSLVERRRMVKSWLKTASGLKRQQFDIQQQALKLTANSMYGCLGFSNSRFYAKPLAELITLQGREILQNTVDLVQNNLNLEVIYGDTDSIMIHTGLDDISRAKGIAGKVIQEVNKKYRCLEIDLDGIYKRMLLLKKKKYAAIKVALDGSLRENIERKGLDMVRRDWSLLSKEIGDFCLNQILSGGSCDDVIESIHSSLVQVQEQMRGGQTELEKYIITKSLTKAPEDYPDAKNQPHVQVALRLKQNGYSGCSAGDTVPYIICSQQDSESTHSGGIAQRARHPEELKRNPDKWMIDIDYYLSQQIHPVVSRLCASIQGTSPARLAECLGLDSSKFQSRLTESDNQDTSSMLLSVIDDEDERYRGCEPLRLSCPSCSTTFDCPPVSSLIIGSSSGNVSNPNEGNDASINFWRRMRCPRCPDDTDESRVSPAVLANQMKRQADSFINLYYKGLLMCDDEGCKYSTHSVNLRVMGDSERGTICPNYPRCNGHLVRQYTEADLYRQLSYFCYVVDATRCLEKLDQKARLPFEKEFAALSQTINLALMEVQKIRDRCAFGWVQLKDLAISI
Protein: Translocon-associated protein subunit beta (TRAP-beta) (Glycoprotein 25H) (gp25H) (Signal sequence receptor subunit beta) (SSR-beta) (P23438)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins.
Subcellular location: Endoplasmic reticulum membrane; Single-pass type I membrane protein.
Interaction partners:
- Signal sequence receptor subunit 4.
- Translocon-associated protein subunit alpha
- Signal sequence receptor subunit 3.
- Uncharacterized protein.
- Protein transport protein Sec61 subunit beta
- Cancer antigen 1.
- Translocation protein SEC62.
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
- Serpin family A member 4
- Protein transport protein Sec61 subunit alpha isoform 1.
Sequence:
MRLLASVLLALFAVSHAEEGARLLASKSLLNRYAVEGRDLTLQYNIYNVGSSAALDVELSDDSFPPEDFGIVSGMLNVKWDRIAPASNVSHTVVLRPLKAGYFNFTSATVTYLAQEDGPVVIGFTSAPGQGGILAQREFDRRFSPHFLDWAAFGVMTLPSIGIPLLLWYSSKRKYDTPKSKKN
Protein: adenylate cyclase (EC 4.6.1.1) (M9PH04)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MDPAYSKNVVDYRSLGNMPGYEWKLLRYKCRELRLEGVYHRHCHLVSVALVTQLIIVIEILMLIHVILLFSVVKNIDFLTVLPYFAVMLLTPSILMPSREPNVEQYESIAILVSCLMALLLTAMDLILPICYFRPFSLVPSYDHVVIVLIYLMFPIAFVKNGRAYFLGLAVSLFYFGYMALIDKISTLDKVWELTAYGAYLFFLNMLCMFLSRFQEYNMRSGILSRYQVVYQNLVFQMAMKEEKALLDSIIPVTLARSLQDAIASHIEEDPSNLMPFTKTRHLFMEPHPEVSILEADMVDFTGLTTTMEVSDLVAILHELFVSFDLAANHNRATRIKFLGDSYTCVTGIPSYFPTHANACVNQALDMIEISREVSKRRNKKIDLRIGVHSGEILAGIIGLTKWQFDIWSKDVDITNRLESSGLPGMVHISSRTLGLLDNHYVYEEGTDTAKLDPLLQRSNLSTYLIRSRLPNFEDTDDLEDDNFSLNDYRFSFSFSQDYEDIQVKAQRDMILEVEHMPVNRVQTCKIRRPMHRIAKEDINEEYRFHLESYYLFTTFRSWRMEWSFNKMRDLLMKYSLGMMVFAGATIIAMDLLVKSEAMDYTMLFSLFLLILLPLLLASYKKLWLRGRRLSPITQPTFFLSRWFIKASDLIEKSVFVRIPLAIMVLFLLYVMSSETVPGSSWRL
Protein: Lytic chitin monooxygenase (EC 1.14.99.53) (Lytic polysaccharide monooxygenase) (LPMO) (SamLPMO10B) (A3KIM2)
Organism: Streptomyces ambofaciens (strain ATCC 23877 / 3486 / DSM 40053 / JCM 4204 / NBRC 12836 / NRRL B-2516)
Function: Involved in chitin degradation. Catalyzes the oxidative cleavage of glycosidic bonds in chitin via a copper-dependent mechanism, leading to oxidized chitooligomers with degrees of polymerization of 4-6. Is not active on cellulose.
Subcellular location: Secreted {ECO:0000305|PubMed:28366436}.
Interaction partners:
- chitinase
- chitinase
- Putative secreted chitinase
Sequence:
MHAGRKTAVLIGAALAPVIAVSLPAASASAHGYISNPPSRQAQCAAGTVSCGDITYEPQSVEGPKGLTSCSGGNSRFAELDDDSKGWAVTPVPRNATFSWKLTAQHSTSTWEYYVGGQRIALFDDGGAKPGAVVDHQVDFGGLDGRQKVLAVWNVADTDNAFYACIDVNVGG
Protein: Beta-1 adrenergic receptor (Beta-1 adrenoreceptor) (G1NEX5)
Organism: Meleagris gallopavo (Wild turkey)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Early endosome {ECO:0000256|ARBA:ARBA00004412}.
Interaction partners:
Sequence:
TGSRQVSAELLSQQWEAGMSLLMALVVLLIVAGNVLVIAAIGRTQRLQTLTNLFITSLACADLVMGLLVVPFGATLVVRGTWLWGSFLCECWTSLDVLCVTASIETLCVIAIDRYLAITSPFRYQSLMTRARAKVIICTVWAISALVSFLPIMMHWWRDEDPQALKCYQDPGCCDFVTNRAYAIASSIISFYIPLLIMIFVYLRVYREAKEQIRKIDRCEGRFYGSQEQPQPPPLPHHQPILGNGRASKRKTSRVMAMREHKALKTLGIIMGVFTLCWLPFFLVNIVNVFNRDLVPDWLFVFFNWLGYANSAFNPIIYCRSPDFRKAFKRLLCFPRKADRRLHAGGQPPLPGGFISTLGSPEHSPGGTWSDCNGGTRGGSESSLEERHSKTSRSESKMEREKNILATTRFYCTFLGNGDKAVFCTVLRIVKLFEDATCTCPHTHKLKMKWRFKQHQA
Protein: Cytochrome c biogenesis protein CcsA (P0C377)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Required during biogenesis of c-type cytochromes (cytochrome c6 and cytochrome f) at the step of heme attachment.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01391}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01391}.
Interaction partners:
- Cytochrome c biogenesis protein CcmE family, putative, expressed
- Cytochrome c biogenesis protein CCS1, chloroplastic
- Cytochrome c-type biogenesis ccda-like chloroplastic protein 1
- Cytochrome c-type biogenesis ccda-like chloroplastic protein 2
- uroporphyrinogen-III C-methyltransferase
- Os01g0855200 protein
- ATP-dependent Clp protease proteolytic subunit
- Potassium/proton antiporter CemA
- NAD
- DNA-directed RNA polymerase subunit beta'
Sequence:
MLFATLEHILTHISFSTISIVITIHLITLLVRELGGLRDSSEKGMIATFFCITGFLVSRWASSGHFPLSNLYESLIFLSWALYILHMIPKIQNSKNDLSTITTPSTILTQGFATSGLLTEMHQSTILVPALQSQWLMMHVSMMLLSYATLLCGSLLSAALLMIRFRKNLDFFSKKKKNVLSKTFFFNEIEYFYAKRSALKSTFFPLFPNYYKYQLIERLDSWSYRVISLGFTLLTIGILCGAVWANEAWGSYWNWDPKETWAFITWTIFAIYLHSRTNPNWKGTKSAFVASIGFLIIWICYFGINLLGIGLHSYGSFTLPI