wanglab/gogpt-training-data huggingface dataset:
Protein: ABSCISIC ACID-INSENSITIVE 5-like protein 2 (ABA-responsive element-binding protein 3) (Dc3 promoter-binding factor 3) (AtDPBF3) (bZIP transcription factor 66) (AtbZIP66) (Q9LES3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds to the embryo specification element and the ABA-responsive element (ABRE) of the Dc3 gene promoter. Could participate in abscisic acid-regulated gene expression during seed development.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:15642716}.
Interaction partners:
- Serine/threonine-protein kinase SRK2D
- Serine/threonine-protein kinase SRK2E
- Serine/threonine-protein kinase SRK2A
- Serine/threonine-protein kinase SRK2I
- Basic leucine zipper 8
- ABSCISIC ACID-INSENSITIVE 5-like protein 1
- Serine/threonine-protein kinase SRK2B
- Serine/threonine-protein kinase SRK2F
Sequence:
MDSQRGIVEQAKSQSLNRQSSLYSLTLDEVQNHLGSSGKALGSMNLDELLKSVCSVEANQPSSMAVNGGAAAQEGLSRQGSLTLPRDLSKKTVDEVWKDIQQNKNGGSAHERRDKQPTLGEMTLEDLLLKAGVVTETIPGSNHDGPVGGGSAGSGAGLGQNITQVGPWIQYHQLPSMPQPQAFMPYPVSDMQAMVSQSSLMGGLSDTQTPGRKRVASGEVVEKTVERRQKRMIKNRESAARSRARKQAYTHELEIKVSRLEEENERLRKQKEVEKILPSVPPPDPKRQLRRTSSAPF
Protein: Cuticular protein 72Ec (GH03623p) (Q9VV46)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Uncharacterized protein
- AT15826p
- Beta-alanyl-dopamine/carcinine hydrolase
Sequence:
MHCFTWTILGGLLALTSAAGLPQRPSSGYQEQDTARAFYSYGYRDENAARAEYSSRDGTSRGFYSYVDADGKLQTVRYEANGVQGFKAEASNQPQAPVDKGKAPLPVTDTEEVQQARLNHLNALREAREKALATSLREEADRRQQEQIRNNNEDQQSGEQSLTDEDAAILERVRAELSAMLADRQRELNLPRNRDDREQREKQEIRQDQRKELRQDLRQEQRQDQREDRRQDQREDRRQNQREDRRQDQREERREDQREERGEDQREERREDRREDRREDRRQDLRIDQESRQDLLQDLRQDLRQDLRQELRQDLRQDQSRNQESLRDSSQIRENARQISSDRDGDDLRLRTVYSLADLSSSSYLKLGDLASAEKLLEDRLDNSDLRVPIGAYYTLVSPNTKYSVTTPTELRTLRPVALSRSLLVSKRN
Protein: Ubiquitin carboxyl-terminal hydrolase 30 homolog (dUSP30) (EC 3.4.19.12) (Deubiquitinating enzyme 30 homolog) (Ubiquitin thioesterase 30 homolog) (Ubiquitin-specific-processing protease 30 homolog) (Ub-specific protease 30 homolog) (Q9W462)
Organism: Drosophila melanogaster (Fruit fly)
Function: Deubiquitinating enzyme that acts as a key inhibitor of mitophagy by counteracting the action of parkin (park).
Subcellular location: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q70CQ3}.
Interaction partners:
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin-ribosomal protein eL40 fusion protein
- ubiquitinyl hydrolase 1
- Uncharacterized protein
- Transcription-associated protein 1
- Transcriptional adaptor 3, isoform C
- Serine/threonine-protein kinase Pink1, mitochondrial
- LD34461p
- Transcription initiation factor TFIID subunit 9
- Polyubiquitin
Sequence:
MESEKILMAAGVTVAAVVGAFVFWGPSGSRLRQRRGQIAGLHNFGLTCFLNTLLQAMAACPQFIAWLQLYNNASPDRKSLITSMLNTLEVVNGTHATLRGDPYSPGAVLRALNALGWVIPQEEHDAHELFHVLLTCLEEEAIRPQPLGCLSDALPTDNDDNSSLAGTATPVGGFRSFSSMAAGLGASQRIGDQPNRPSSAMLTDFLNMEYDESTSLQRLVRSEAHTPDSPASVCERDGNDRLGSVLLDAVSPGTPFGFPLVSNPDSLATPMLGGERSSRPRLPQSQQQQDEGLNRRVSSSCRSLERLHRGPGRVSIWSNMMPSQVAHPFQGAMGAQIVCNGCGSKSAVRYDKFDSITLNLPPQRRTGLSLGHLLSEYITSEDLSDVKCDSCNETTTHTKSVTFAKLPACLCIHVARTVWLPTGQVCKRKDYVHFPESLSMAPYSFVQPHLNSQAGTPWGSTMSLYSSSLPMNNGVGGGEGFGTMFPKNLYRLLAVVVHSGEANSGHFVTYRRGSLRNAHRWYYTSDTIVREVSIDEVLSVPAYLLFYDRGQQRQLNLR
Protein: Aminoglycoside N(6')-acetyltransferase type 1 (EC 2.3.1.82) (AAC(6')-Iz) (Aminoglycoside resistance protein) (Q9RBW7)
Organism: Stenotrophomonas maltophilia (Pseudomonas maltophilia) (Xanthomonas maltophilia)
Function: Catalyzes the transfer of an acetyl group from acetyl-CoA to the 6'-amino group of aminoglycoside molecules conferring resistance to antibiotics containing the purpurosamine ring including amikacin, gentamicin, kanamycin B, tobramycin, netilmicin, and isepamicin.
Interaction partners:
Sequence:
MIASAPTIRQATPADAAAWAQLRLGLWPDADDPLEELTQSLADAEGAVFLACAADGETVGFAEVRLRHDYVNGTESSPVGFLEGWYVQPQWQGSGVGRALLAAVQAWTRDAGCRELASDSRVEDVQAHAAHRACGFEETERVVYFRMPLEPSA
Protein: Probable actin-related protein 2/3 complex subunit 2 (Arp2/3 complex 34 kDa subunit) (p34-ARC) (Q8WTM6)
Organism: Caenorhabditis elegans
Function: Functions as actin-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the mother actin filament (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- Actin-related protein 2/3 complex subunit 5
- Probable actin-related protein 2/3 complex subunit 3
- Actin-related protein 3
- Probable actin-related protein 2/3 complex subunit 4
- Probable actin-related protein 2/3 complex subunit 5
- Actin-related protein 2/3 complex subunit
- Actin-related protein 2
- CRIB domain-containing protein
- SPIN90/Ldb17 leucine-rich domain-containing protein
- Guanine nucleotide-binding protein G
Sequence:
MIILEQNNRIIVELLEQKFANAKEGGKPESVNVTFADFDGVLYKLSNPDGDRTKIILSISLKFYTELQQHGADDLLRRVYGGHMRSTPEQGFNVTLEYNLADLPADTTDLVQAASALKRNCFASVFEKYFEFQEAGQEGHKRAVINYRDDETMYIEAKADRVTVIFSTVFKDADDVIIGKVFLQEFREGRKASQTAPAVLYSLGEPPLELKDLPEARVGDNVGYITFVLFPRHTNKKTKDNTIDLIHSFRDYLHYHIKCSKVYLHTRMRAKTTDFLKVLNRARPEVKGEKKTFHGRTFQTQ
Protein: Transcriptional adapter 3 (ADA3 homolog) (Transcriptional adapter 3-like) (ADA3-like protein) (Q4V8F5)
Organism: Rattus norvegicus (Rat)
Function: Functions as a component of the PCAF complex. The PCAF complex is capable of efficiently acetylating histones in a nucleosomal context. The PCAF complex could be considered as the human version of the yeast SAGA complex. Also known as a coactivator for p53/TP53-dependent transcriptional activation (By similarity). Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4 (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- SAGA-associated factor 29
- Transcription initiation factor TFIID subunit 6
- Transcription initiation factor TFIID subunit 10
- Histone acetyltransferase
- Transcription initiation factor TFIID subunit 12
- Transcriptional adapter 2-alpha
- Transcription initiation factor TFIID subunit 9B
- SPT3 homolog, SAGA and STAGA complex component
- Transcriptional adapter 1
- Transcriptional adapter
Sequence:
MSELKDCPLQFHDFKSVDHMKVCPRYTAVLARSEDDGIGIEELDTLQLELETLLSSASRRLRVLEAETQILTDWQDKKGDRRILKLARDHELGAPPKHGKPKKQKLEGKTGHGPGPGPGRPKSKNVQPKIQEYEFTDDPIDVPRIPKNDAPNRFWASVEPYCADITSEEVRTLEELLKPPEDEAEHYKIPPLGKHYSQRWAQEDLLEEQKDGARAAAVADKKKGLIGPLTELDTKDVDALLKKSEAQHEQPEDGCPFGALTQRLLQALVEENIISPMEDSPIPDMSGKESGADGASTSPRNQNKPFSVPHTKSLESRIKEELIAQGLLESEDRPAEDSEDEVLAELRKRQAELKALSAHNRTKKHDLLRLAKEEVSRQELRQRVRMADNEVMDAFRKIMAARQKKRTPTKKEKDQAWKTLKERESILKLLDG
Protein: Cyclin-D2-1 (Cyclin-delta-2) (Cyclin-d2) (G1/S-specific cyclin-D2-1) (CycD2;1) (P42752)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts on the G1 phase of the cell cycle to control cell division rate in both shoot and root meristems. The complex formed with CDKA-1 phosphorylates plant retinoblastoma protein.
Interaction partners:
- Cyclin-dependent kinase A-1
- Retinoblastoma-related protein 1
- Cyclin-dependent kinase inhibitor 1
- Cyclin-dependent kinase B2-1
- Cyclin-dependent kinase B1-1
- Cyclin-dependent kinase inhibitor 2
- Cyclin-dependent kinase inhibitor 7
- Cyclin-dependent kinase B1-2
- Cyclin-dependent kinase B2-2
- Cyclin-dependent kinase inhibitor 3
Sequence:
MAENLACGETSESWIIDNDDDDINYGGGFTNEIDYNHQLFAKDDNFGGNGSIPMMGSSSSSLSEDRIKEMLVREIEFCPGTDYVKRLLSGDLDLSVRNQALDWILKVCAHYHFGHLCICLSMNYLDRFLTSYELPKDKDWAAQLLAVSCLSLASKMEETDVPHIVDLQVEDPKFVFEAKTIKRMELLVVTTLNWRLQALTPFSFIDYFVDKISGHVSENLIYRSSRFILNTTKAIEFLDFRPSEIAAAAAVSVSISGETECIDEEKALSSLIYVKQERVKRCLNLMRSLTGEENVRGTSLSQEQARVAVRAVPASPVGVLEATCLSYRSEERTVESCTNSSQSSPDNNNNNNNSNKRRRKQ
Protein: Inactive rhomboid protein 2 (iRhom2) (Rhomboid 5 homolog 2) (Rhomboid family member 2) (Rhomboid veinlet-like protein 5) (Rhomboid veinlet-like protein 6) (Q6PJF5)
Organism: Homo sapiens (Human)
Function: Regulates ADAM17 protease, a sheddase of the epidermal growth factor (EGF) receptor ligands and TNF, thereby plays a role in sleep, cell survival, proliferation, migration and inflammation. Does not exhibit any protease activity on its own.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q80WQ6}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q80WQ6}. Cell membrane {ECO:0000269|PubMed:22265016, ECO:0000269|PubMed:29897333}.
Interaction partners:
- Disintegrin and metalloproteinase domain-containing protein 17
- Eukaryotic translation initiation factor 3 subunit F
- Translocon-associated protein subunit beta
- Cytoglobin
- FERM domain-containing protein 8
Sequence:
MASADKNGGSVSSVSSSRLQSRKPPNLSITIPPPEKETQAPGEQDSMLPEGFQNRRLKKSQPRTWAAHTTACPPSFLPKRKNPAYLKSVSLQEPRSRWQESSEKRPGFRRQASLSQSIRKGAAQWFGVSGDWEGQRQQWQRRSLHHCSMRYGRLKASCQRDLELPSQEAPSFQGTESPKPCKMPKIVDPLARGRAFRHPEEMDRPHAPHPPLTPGVLSLTSFTSVRSGYSHLPRRKRMSVAHMSLQAAAALLKGRSVLDATGQRCRVVKRSFAFPSFLEEDVVDGADTFDSSFFSKEEMSSMPDDVFESPPLSASYFRGIPHSASPVSPDGVQIPLKEYGRAPVPGPRRGKRIASKVKHFAFDRKKRHYGLGVVGNWLNRSYRRSISSTVQRQLESFDSHRPYFTYWLTFVHVIITLLVICTYGIAPVGFAQHVTTQLVLRNKGVYESVKYIQQENFWVGPSSIDLIHLGAKFSPCIRKDGQIEQLVLRERDLERDSGCCVQNDHSGCIQTQRKDCSETLATFVKWQDDTGPPMDKSDLGQKRTSGAVCHQDPRTCEEPASSGAHIWPDDITKWPICTEQARSNHTGFLHMDCEIKGRPCCIGTKGSCEITTREYCEFMHGYFHEEATLCSQVHCLDKVCGLLPFLNPEVPDQFYRLWLSLFLHAGVVHCLVSVVFQMTILRDLEKLAGWHRIAIIFILSGITGNLASAIFLPYRAEVGPAGSQFGLLACLFVELFQSWPLLERPWKAFLNLSAIVLFLFICGLLPWIDNIAHIFGFLSGLLLAFAFLPYITFGTSDKYRKRALILVSLLAFAGLFAALVLWLYIYPINWPWIEHLTCFPFTSRFCEKYELDQVLH
Protein: Annexin (A0A8I6AH11)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MSYPGYPPTGYPPFPGYPPAGQESSFPTSGQYPYPSGFPPMGGGAYPPAPSGGYPGAGGYPSPGGYPAPGGYPGTLNPGGPPSYPGGQGFGAPPGGAGFSGYPQPPAQSYGGGPAQVPVPGGFPGGQMPSQYPGGQSPYPGQPAAMTQGTQGTIRPASNFDAMRDAEILRKAMKGFGTDEQAIVDVVSNRSNDQRQQIKAAFKTMYGKDLIKDLKSELSGNMEELILALFMPPTYYDAWSLRKAIQGAGTQERVLIEILCTRTNQEIRDIVRCYQLEFGRELERDIRSDTSGHFERLLVSMCQGNRDESPSINHQMAQEDAQRLYQAGEGRLGTDESCFNMILATRSFPQLRATMEAYSRMANRDLLSSVSREFSGYVESGLKTILQCALNRPAFFAERLYYSMKGAGTDDSTLVRIVVTRSEIDLVQIKQMFTQMYQKTLSTMIARMKLFRAYLSEQ
Protein: LD33980p (Q95TP2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGDGQQTLASAASNPGIYASSTANSAAVSISELMKPGQTAVEKRVEAWNPFEEEQPFSQMTEDHIFEAEFDKIRQRGSQGSITAKSASTTSTLTPTEQIPSAVVAPVTAAPGAVPPPPIAAAVSPYPSQVSEDPFGSAPFSLPPGLREKASSLRKTGAKFIGVSSGGTGGGVATPIGLVAGGANTATSSNSSKWMLSPTLEVSSEEKTSLISKLKTDSECGIPGAVGGAGEGVSGYVKLPVEDRNKYEKLRSKDQPTSDDSDSEASEFFQQDSDEGGGGIFRQMQMVTSNLPETIHKIQQVAYHKVDKTAHLPIVKKLRDKTKKPTTAAHQAAQQLNLMAAAVAAQAEEAAKAAESDGDSIGSASDLRAEDDDLFDENPRQTQAKQRRPLPTEMDGISESVKTCSSSAYHAECESVTTHEDDVRSRVVVKVRMRKKDRALVTATGDPSAPSEELSPTSSDLLHKFGDRPLLLDDELDYGSGESKSSTESPVAPILPTNPDVQESEEDVFALAPFKLPVGVPLKRKTKPKAKPKPSEPEMWTSTPVKSAAVGDPSTNFASFPAQLTPTNNVGNSAQLDEFNEPIFNPFQENAQNTQSGETNQCDLFGLEPFPQVIRTIEQNPQHHQIHQFPSHNNNNNVIKVPASVSVALPASVPVSVSVNSSAPQLVTINHSIIINKTPEPPMNYNNNNNNQTAKSSGTSSVYVNVPSFSSMSTSSCSINQPQSSPAAVIPVQAPLPVPVPAPVSVPAVPVPIPAVVTHLRPLLPIADNAYVQISQDRCSDFTPDDEEEPVVLRDADVVADGIGIPTPAKPKKEKSNLAVRVLPGKLTQKVKGHSYKKVSAAALGSTSSLSSGSKQKHQRLQYQSHDDDDDEQDQDENRGAGGGRNFQSNTIQNSAKTGFSNMSFEDFPSDQEMDRLSRTIPFEVVRNEKMLLEAEKKFGSLKRRNNLFS
Protein: Gastrin/cholecystokinin type B receptor (CCK-B receptor) (CCK-BR) (Cholecystokinin-2 receptor) (CCK2-R) (P30553)
Organism: Rattus norvegicus (Rat)
Function: Receptor for gastrin and cholecystokinin. The CCK-B receptors occur throughout the central nervous system where they modulate anxiety, analgesia, arousal, and neuroleptic activity. This receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Gastrin
- Cholecystokinin
- Guanine nucleotide-binding protein G
- Cholecystokinin receptor type A
- Guanine nucleotide-binding protein subunit alpha-11
- Guanine nucleotide-binding protein subunit alpha
- Guanine nucleotide-binding protein G
Sequence:
MELLKLNRSVQGPGPGSGSSLCRPGVSLLNSSSAGNLSCDPPRIRGTGTRELEMAIRITLYAVIFLMSVGGNVLIIVVLGLSRRLRTVTNAFLLSLAVSDLLLAVACMPFTLLPNLMGTFIFGTVICKAISYLMGVSVSVSTLNLVAIALERYSAICRPLQARVWQTRSHAARVILATWLLSGLLMVPYPVYTMVQPVGPRVLQCMHRWPSARVQQTWSVLLLLLLFFIPGVVIAVAYGLISRELYLGLHFDGENDSETQSRARNQGGLPGGAAPGPVHQNGGCRPVTSVAGEDSDGCCVQLPRSRLEMTTLTTPTPGPVPGPRPNQAKLLAKKRVVRMLLVIVLLFFLCWLPVYSVNTWRAFDGPGAQRALSGAPISFIHLLSYVSACVNPLVYCFMHRRFRQACLDTCARCCPRPPRARPQPLPDEDPPTPSIASLSRLSYTTISTLGPG
Protein: Guanine nucleotide-binding protein subunit beta-2 (P29829)
Organism: Drosophila melanogaster (Fruit fly)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10608815}. Cell projection, axon {ECO:0000269|PubMed:10608815}. Cell projection, rhabdomere {ECO:0000269|PubMed:10608815}.
Interaction partners:
- Guanine nucleotide-binding protein subunit gamma-e
- Latrophilin Cirl
- Opsin Rh1
- Guanine nucleotide-binding protein subunit alpha
- G protein alpha o subunit subunit alpha 47A)
- G protein alpha s subunit subunit alpha)
- Guanine nucleotide-binding protein subunit alpha
- G protein alpha q subunit subunit alpha)
- Guanine nucleotide-binding protein subunit gamma-1
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase
Sequence:
MPKIDPETQKLYDEINGMIQKFKDDQKSKADCTLADKCGDMGDVPKIRFSSKKILKGHINKVNSVHFAGDSRHCVTGSLDGKLIIWDTWTANKVQIIPLRSAWVMTVAFSPSGNFVACGGMDNQCTVYDVNNRDASGVAKMVKELMGYEGFLSSCRFLDDGHLITGSGDMKICHWDLEKGVKTMDFNGHAGDIAGLSLSPDMKTYITGSVDKTAKLWDVREEGHKQMFFGHDMDVSSVCYHPSGFGFASCSEDQTARMYDLRADQQIAQYEPPQKNTGFTSCALSTSGRYLMCGGIEGNVHSWDTMKQRHTGTLSGHENRITCISLCPNGMCLASTSWDQQVRLWL
Protein: Coatomer subunit alpha (Alpha-coat protein) (Alpha-COP) (HEP-COP) (HEPCOP) [Cleaved into: Xenin (Xenopsin-related peptide); Proxenin] (Q27954)
Organism: Bos taurus (Bovine)
Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. {ECO:0000250}.; SUBCELLULAR LOCATION: [Xenin]: Secreted {ECO:0000250}.
Interaction partners:
- Coatomer subunit epsilon
- Coatomer subunit beta'
- Coatomer subunit delta
- Coatomer subunit beta
- Coatomer subunit gamma-1
- Coatomer subunit zeta-1
- Coatomer subunit gamma-2
- Coatomer subunit zeta
- Testis-specific gene 13 protein
- ADP-ribosylation factor 1
Sequence:
MLTKFETKSARVKGLSFHPKRPWILTSLHNGVIQLWDYRMCTLIDKFDEHDGPVRGIDFHKQQPLFVSGGDDYKIKVWNYKLRRCLFTLLGHLDYIRTTFFHHEYPWILSASDDQTIRVWNWQSRTCVCVLTGHNHYVMCAQFHPSEDLVVSASLDQTVRVWDISGLRKKNLSPGAVESDVRGITGVDLFGTTDAVVKHVLEGHDRGVNWAAFHPTMPLIVSGADDRQVKIWRMNESKAWEVDTCRGHYNNVSCAVFHPRQELILSNSEDKSIRVWDMSKRTGVQTFRRDHDRFWVLAAHPNLNLFAAGHDGGMIVFKLERERPAYAVHGNMLHYVKDRFLRQLDFNSSKDVAVMQLRSGSKFPVFSMSYNPAENAVLLCTRASNLENSTYDLYTIPKDADTQNPDAPEGKRSSGLTAVWVARNRFAVLDRMHSLLIKNLKNEITKKVQVPNCDEIFYAGTGNLLLRDAESITLFDVQQKRTLASVKISKVKYVIWSADMSHVALLAKHAIVICNRKLEALCNIHENIRVKSGAWDESGVFIYTTSNHIKYAVTTGDYGIIRTLDLPIYVTRVKGNNVYCLDRECRPRVLTIDPTEFKFKLALINRKYDEVLHMVRNAKLVGQSIIAYLQKKGYPEVALHFVKDEKTRFSLALECGNIEIALEAAKALDDKNCWEKLGEVALLQGNHQIVEMCYQRTKNFDKLSFLYLITGNLEKLRKMMKIAEIRKDMSGHYQNALYLGDVSERVRILKNCGQKSLAYLTAATHGLDEEAESLKETFDPEKETIPDIDPNAKLLQPPAPIMPLDTNWPLLTVSKGFFEGSIASKGKGGALAADIDIDTVGTEGWGEDAELQLDEDGFVEATEGLGDDALGKGQEEGGGWDVEEDLELPPELDIPPGAAGGAEDGFFVPPTKGTSPTQIWCNNSQLPVDHILAGSFETAMRLLHDQVGVTQFGPYKQLFLQTYARGRTTYQALPCLPSMYGYPNRNWKDAGLKNGVPAVGLKLNDLIQRLQLCYQLTTVGKFEEAVEKFRSILLSVPLLVVDNKQEIAEAQQLITICREYIVGLSMETERKKLPKETLEQQKRICEMAAYFTHSNLQPVHMILVLRTALNLFFKLKNFRTAAAFARRLLELGPKPEVAQQTRKILSACEKNPTDAYQLNYDMHNPFDICAASYRPIYRGKPVEKCPLSGACYSPEFKGQICKVTTVTEIGKDVIGLRISPLQFR
Protein: Transforming acidic coiled-coil containing protein 3 (E7EMT0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSLQVLNDKNVSNEKNTENCDFLFSPPEVTGRSSVLRVSQKENVPPKNLAKAMKVTFQTPLRDPQTHRILSPSMASKLEAPFTQDDTLGLENSHPVWTQKENQQLIKEVDAKTTHGILQKPVEADTDLLGDASPAFGSGSSSESGPGALADLDCSSSSQSPGSSENQMVSPGKVSGSPEQAVEENLSSYSLDRRVTPASETLEDPCRTESQHKAETPHGAEEECKAETPHGAEEECRHGGVCAPAAVATSPPGAIPKEACGGAPLQGLPGEA
Protein: Phospholipid:diacylglycerol acyltransferase 1 (AtPDAT) (EC 2.3.1.158) (Q9FNA9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Triacylglycerol formation by an acyl-CoA independent pathway. The enzyme preferentially transfers acyl groups from the sn-2 position of a phospholipid to diacylglycerol, thus forming an sn-1-lysophospholipid. Involved in epoxy and hydroxy fatty acid accumulation in seeds. Has complementary functions with DAG1 that are essential for triacylglycerol synthesis and normal development of both seeds and pollen.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Diacylglycerol O-acyltransferase 2
- Diacylglycerol O-acyltransferase 3
- Diacylglycerol O-acyltransferase 1
- Triacylglycerol lipase SDP1
- Phosphatidate phosphatase PAH1
- Phosphatidate phosphatase PAH2
- Lipid phosphate phosphatase 1
- Wax ester synthase/diacylglycerol acyltransferase 1
- Lipid phosphate phosphatase 2
- Triacylglycerol lipase SDP1L
Sequence:
MPLIHRKKPTEKPSTPPSEEVVHDEDSQKKPHESSKSHHKKSNGGGKWSCIDSCCWFIGCVCVTWWFLLFLYNAMPASFPQYVTERITGPLPDPPGVKLKKEGLKAKHPVVFIPGIVTGGLELWEGKQCADGLFRKRLWGGTFGEVYKRPLCWVEHMSLDNETGLDPAGIRVRAVSGLVAADYFAPGYFVWAVLIANLAHIGYEEKNMYMAAYDWRLSFQNTEVRDQTLSRMKSNIELMVSTNGGKKAVIVPHSMGVLYFLHFMKWVEAPAPLGGGGGPDWCAKYIKAVMNIGGPFLGVPKAVAGLFSAEAKDVAVARAIAPGFLDTDIFRLQTLQHVMRMTRTWDSTMSMLPKGGDTIWGGLDWSPEKGHTCCGKKQKNNETCGEAGENGVSKKSPVNYGRMISFGKEVAEAAPSEINNIDFRGAVKGQSIPNHTCRDVWTEYHDMGIAGIKAIAEYKVYTAGEAIDLLHYVAPKMMARGAAHFSYGIADDLDDTKYQDPKYWSNPLETKLPNAPEMEIYSLYGVGIPTERAYVYKLNQSPDSCIPFQIFTSAHEEDEDSCLKAGVYNVDGDETVPVLSAGYMCAKAWRGKTRFNPSGIKTYIREYNHSPPANLLEGRGTQSGAHVDIMGNFALIEDIMRVAAGGNGSDIGHDQVHSGIFEWSERIDLKL
Protein: Natriuretic peptide A (Natriuretic peptides A precursor) (F1QVW0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU003686}.
Interaction partners:
- Natriuretic peptide B
- Natriuretic peptide receptor 3.
- Guanylate cyclase
- Guanylate cyclase.
- NK2 homeobox 5.
- Myosin light chain 2 Mlc2a
- Corin, serine peptidase.
- GATA-binding protein 4.
- T-box transcription factor TBX5-A
- Myosin heavy chain 7
Sequence:
MAGGLILTGLLLLVWQQTDVQAHTLSRHSSDSNMAKLKSLLQQFEEALATEEASERAVDYEDSNTVLEQSPPSTSWDRDREEAAAPGEDSNPSDGFDTQRNRLLDLLLSTRSKSLSGCFGGRLDRIGSSSTLGCNSKKG
Protein: Photosystem I P700 chlorophyll a apoprotein A2 (EC 1.97.1.12) (PsaB) (P29255)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Function: PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin or cytochrome c6.
Subcellular location: Cellular thylakoid membrane; Multi-pass membrane protein.
Interaction partners:
- Photosystem I reaction center subunit PsaK 1
- Iron stress-induced chlorophyll-binding protein
- Photosystem I reaction center subunit XI
- Photosystem I reaction center subunit PsaK 2
- Photosystem I reaction center subunit VIII
- Photosystem I reaction center subunit III
- Photosystem I reaction center subunit IV
- Photosystem I reaction center subunit II
- Photosystem I reaction center subunit IX
- Photosystem I P700 chlorophyll a apoprotein A1
Sequence:
MATKFPKFSQDLAQDPTTRRIWYGIATAHDFETHDGMTEENLYQKIFASHFGHIAIIFLWTSGTLFHVAWQGNFEQWIKDPLNIRPIAHAIWDPHFGEGAVNAFTQAGASNPVNIAYSGVYHWFYTIGMTTNQELYSGAVFLLVLASLFLFAGWLHLQPKFRPSLAWFKNAESRLNHHLAGLFGVSSLAWAGHLVHVAIPEARGQHVGWDNFLSTPPHPAGLMPFFTGNWGVYAADPDTAGHIFGTSEGAGTAILTFLGGFHPQTESLWLTDIAHHHLAIAVIFIIAGHMYRTNWGIGHSIKEILNAHKGPLTGAGHTNLYDTINNSLHFQLGLALASLGVITSLVAQHMYSLPSYAFIAQDHTTQAALYTHHQYIAGFLMVGAFAHGAIFFVRDYDPVANKDNVLARMLEHKEALISHLSWVSLFLGFHTLGLYVHNDVVVAFGTPEKQILIEPVFAQWIQATSGKALYGFDVLLSNPDSIASTTGAAWLPGWLDAINSGTNSLFLTIGPGDFLVHHAIALGLHTTALILIKGALDARGSKLMPDKKDFGYSFPCDGPGRGGTCDISAWDAFYLAMFWMLNTLGWLTFYWHWKHLGVWSGNVAQFNENSTYLMGWFRDYLWANSAQLINGYNPYGVNNLSVWAWMFLFGHLVWATGFMFLISWRGYWQELIETIVWAHERTPLANLVRWKDKPVALSIVQARLVGLAHFTVGYVLTYAAFLIASTAGKFG
Protein: Serine/threonine-protein kinase receptor (EC 2.7.11.30) (F1QG01)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}. Membrane {ECO:0000256|RuleBase:RU361271}; Single-pass type I membrane protein {ECO:0000256|RuleBase:RU361271}.
Interaction partners:
Sequence:
MGPATKLAFGVFLISCSSGAILGRSETQECVFYNYNPSLENRGNRSGIEPCVGDKDKRLHCFATWRNVSGTVEIVKQGCWLDDVNCYDSTECVEKKEDPDVFFCCCEGNMCNEKFFYNPNTAPVQTTSNPLTQKPPLFSTLLYSIVPIMGIAAIVLLSFWMYRHHKLAYPPVLVPTQDPGPMPPSPTLVQKPLQLLEIKARGRFGCVWKAQLLNDYVAVKIFPIQDKLSWQNEYDIYNIPGMRHENILQFIGAEKRGSNLDIELWLITAYHEKSSLTDYLKANVVTWNELCHIAQTMARGLAYLHSDFPGHRDGHKPAIAHRDFKSKNVLLKTNLTACIADFGLALKFEAGKSAGDTHGQVGTRRYMAPEVLEGAINFQRDAFLRIDMYAVGLVLWELAARCTASDGPVDEYMLPFEEEVGQHPTLEDMQEVVVHKKLRPTLRECWQKHPGLAMLCETIEECWDHEAEARLSAGCVEERVVQMQRQTSVSAPEEIVTVVTMVTNVDYPPKESSL
Protein: Valine--tRNA ligase, mitochondrial 1 (EC 6.1.1.9) (AtSYV1) (Protein TWIN 2) (Valyl-tRNA synthetase) (ValRS) (P93736)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for embryo development and seed viability.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:10583378, ECO:0000305|PubMed:25732537}. Cytoplasm, cytosol {ECO:0000269|PubMed:10583378}.
Interaction partners:
- Histidine--tRNA ligase, cytoplasmic
- Methionine--tRNA ligase, cytoplasmic
- Probable threonine--tRNA ligase, cytoplasmic
- Threonine--tRNA ligase, mitochondrial 1
- Threonine--tRNA ligase, chloroplastic/mitochondrial 2
- Putative glycine--tRNA ligase, cytoplasmic
- Cysteine--tRNA ligase 1, cytoplasmic
- Cysteine--tRNA ligase 2, cytoplasmic
- Cysteine--tRNA ligase, chloroplastic/mitochondrial
- Probable elongation factor 1-gamma 2
Sequence:
MSLLFLRRAKPLFVSCCSATHSRSSFLSPTLTNQLVRSFHGSRTMSESEKKILTEEELERKKKKEEKAKEKELKKQKALEKERLAELKAKQAKDGTNVPKKSAKKSSKRDASEENPEDFVDPETPLGERKRLSSQMAKQYSPATVEKSWYAWWEKSDLFKADAKSSKPPFVIVLPPPNVTGALHIGHALTSAIEDTIIRWKRMSGYNALWVPGVDHAGIATQVVVEKKIMRDRGMTRHDVGREEFVKEVWKWKNQYGGTILTQLRRLGASLDWSRECFTMDEQRSKAVTEAFVRLYKEGLIYRDIRLVNWDCILRTAISDVEVEYIDIKEKTLLKVPGYEKPVEFGLLTSFAYPLEGGLGEVIVATTRVETMLGDTAIAIHPDDARYKHLHGKFAVHPFNGRKLPIICDGILVDPNFGTGCVKITPAHDPNDCEVGKRHKLEFINIFTDDGKINTNGGSDFAGMPRFAAREAVVEALQKQGLYRGAKNNEMRLGLCSRTNDVIEPMIKPQWYVNCSMIGKEALDVAITDENKKLEFVPKQYTAEWRRWLENIRDWCISRQLWWGHRIPAWYATLEEDQLKEVGAYSDHWVVARTEDDAREEAAQKFLGKKFELTRDPDVLDTWFSSGLFPLSVLGWPDVTDDFKAFYPTSVLETGHDILFFWVARMVMMGMKLGGEVPFSKVYFHPMIRDAHGRKMSKSLGNVIDPLEVINGVTLEGLHKRLEEGNLDPKEVIVAKEGQVKDFPNGIPECGTDALRFALVSYTAQSDKINLDILRVVGYRQWCNKLWNAVRFAMMKLGDGYTPPQTLSPETMPFSCQWILSVLNKAISKTVVSLDAFEFSDAANTIYAWWQYQFCDVYIEAIKPYFAGDNPTFASERAHAQHALWISLETGLRLLHPFMPFVTEELWQRLPAPKDTERKASIMICDYPSAIENWSNEKVESEMDTVLATVKCMRALRAGLLEKQKNERLPAFALCENNVTSEIVKSHELEIRTLANLSSLEVVSKGQHAAPPGSSVETVNENLKVYLEVDGAINTEAEQEKIRNKIGELQKQKEKLQKMMSVSTYEEKVPANIKEDNANKLAKILQEFDFFEKESARLAAETSNSGNQ