wanglab/gogpt-training-data huggingface dataset:
Protein: ATP-dependent RNA helicase DDX54 (EC 3.6.4.13) (ATP-dependent RNA helicase DP97) (DEAD box RNA helicase 97 kDa) (DEAD box protein 54) (Q8TDD1)
Organism: Homo sapiens (Human)
Function: Has RNA-dependent ATPase activity. Represses the transcriptional activity of nuclear receptors.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:12429849}.
Interaction partners:
- Ribosome biogenesis protein BOP1
- Pescadillo homolog
- pre-rRNA 2'-O-ribose RNA methyltransferase FTSJ3
- MKI67 FHA domain-interacting nucleolar phosphoprotein
- ATP-dependent RNA helicase DDX24
- Nucleolar complex protein 2 homolog
- 28S rRNA
- Probable ATP-dependent RNA helicase DDX10
- Probable RNA-binding protein 19
- RNA-binding protein 34
Sequence:
MAADKGPAAGPRSRAAMAQWRKKKGLRKRRGAASQARGSDSEDGEFEIQAEDDARARKLGPGRPLPTFPTSECTSDVEPDTREMVRAQNKKKKKSGGFQSMGLSYPVFKGIMKKGYKVPTPIQRKTIPVILDGKDVVAMARTGSGKTACFLLPMFERLKTHSAQTGARALILSPTRELALQTLKFTKELGKFTGLKTALILGGDRMEDQFAALHENPDIIIATPGRLVHVAVEMSLKLQSVEYVVFDEADRLFEMGFAEQLQEIIARLPGGHQTVLFSATLPKLLVEFARAGLTEPVLIRLDVDTKLNEQLKTSFFLVREDTKAAVLLHLLHNVVRPQDQTVVFVATKHHAEYLTELLTTQRVSCAHIYSALDPTARKINLAKFTLGKCSTLIVTDLAARGLDIPLLDNVINYSFPAKGKLFLHRVGRVARAGRSGTAYSLVAPDEIPYLLDLHLFLGRSLTLARPLKEPSGVAGVDGMLGRVPQSVVDEEDSGLQSTLEASLELRGLARVADNAQQQYVRSRPAPSPESIKRAKEMDLVGLGLHPLFSSRFEEEELQRLRLVDSIKNYRSRATIFEINASSRDLCSQVMRAKRQKDRKAIARFQQGQQGRQEQQEGPVGPAPSRPALQEKQPEKEEEEEAGESVEDIFSEVVGRKRQRSGPNRGAKRRREEARQRDQEFYIPYRPKDFDSERGLSISGEGGAFEQQAAGAVLDLMGDEAQNLTRGRQQLKWDRKKKRFVGQSGQEDKKKIKTESGRYISSSYKRDLYQKWKQKQKIDDRDSDEEGASDRRGPERRGGKRDRGQGASRPHAPGTPAGRVRPELKTKQQILKQRRRAQKLHFLQRGGLKQLSARNRRRVQELQQGAFGRGARSKKGKMRKRM
Protein: Kinesin (Q388T7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MKDDELERKIEAAQQKLAALKQREEDMEVEQRQKESLLSQLKDQINDLDRKKGMILERVKEVNAETDAVRSYLHSIEHLDMLEGMLFERKTQLLHQQRRRDMLLQQLSDVETALGKSRTQSDEELNNDTECDCTPSVEEWENINLLRRNANGIYRFFRSSMSHALDHPATVFHQSIRKMSRMARDREVELAMQVECIETYTQQMVLQERTLSRIEHEYKQEVGSMQRSGRSMLQAMGEAAEAEVAELRIAIQRALEERSELQSRLRRHNKTSQNNGLLLNGNLLIAENRHSDPLEGEKKCGDEKGDGTSVRVEADTEKQELASPRLVNGEEILSPVETNATRTTDPARFTGEYLPRVSNDPELDGLRRQVATMERYALRMHRRYEELEEDVAKRLKEHDINVKRQETKLKEATNAVTVLEKEKLEWKALKKQMSLLAH
Protein: Transcription regulatory protein SNF6 (SWI/SNF complex component SNF6) (P18888)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in transcriptional activation. Component of the SWI/SNF complex, an ATP-dependent chromatin remodeling complex, which is required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors.
Subcellular location: Nucleus.
Interaction partners:
- Transcription regulatory protein SNF12
- SWI/SNF chromatin-remodeling complex subunit SNF5
- Actin-related protein 7
- Transcription initiation factor TFIID subunit 14
- SWI/SNF global transcription activator complex subunit SWP82
- Regulator of Ty1 transposition protein 102
- SWI/SNF complex subunit SWI3
- SWI/SNF chromatin-remodeling complex subunit SWI1
- Transcription regulatory protein SNF2
- Transcription regulatory protein SNF11
Sequence:
MGVIKKKRSHHGKASRQQYYSGVQVGGVGSMGAINNNIPSLTSFAEENNYQYGYSGSSAGMNGRSLTYAQQQLNKQRQDFERVRLRPEQLSNIIHDESDTISFRSNLLKNFISSNDAFNMLSLTTVPCDRIEKSRLFSEKTIRYLMQKQHEMKTQAAELQEKPLTPLKYTKLIAAAEDGSRSTKDMIDAVFEQDSHLRYQPDGVVVHRDDPALVGKLRGDLREAPADYWTHAYRDVLAQYHEAKERIRQKEVTAGEAQDEASLQQQQQQDLQQQQQVVTTVASQSPHATATEKEPVPAVVDDPLENMFGDYSNEPFNTNFDDEFGDLDAVFF
Protein: Transaminated amino acid decarboxylase (EC 4.1.1.-) (EC 4.1.1.43) (EC 4.1.1.72) (EC 4.1.1.74) (EC 4.1.1.80) (Thiamine diphosphate-dependent phenylpyruvate decarboxylase) (PPDC) (Thiamine pyrophosphate-dependent 2-oxo-acid decarboxylase) (2ODC) (Transaminated branched-chain amino acid decarboxylase) (Q06408)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: One of five 2-oxo acid decarboxylases (PDC1, PDC5, PDC6, ARO10, and THI3) involved in amino acid catabolism. The enzyme catalyzes the decarboxylation of amino acids, which, in a first step, have been transaminated to the corresponding 2-oxo acids (alpha-keto-acids). In a third step, the resulting aldehydes are reduced to alcohols, collectively referred to as fusel oils or alcohols. Its preferred substrates are the transaminated amino acids derived from phenylalanine (phenylpyruvate), tryptophan (3-(indol-3-yl)pyruvate), and probably tyrosine (4-hydroxyphenylpyruvate), but also isoleucine ((3S)-3-methyl-2-oxopentanoate, also alpha-keto-beta-methylvalerate) and methionine (4-methylthio-2-oxobutanoate), whereas transaminated leucine (4-methyl-2-oxopentanoate, also alpha-keto-isocaproate) is a low efficiency substrate and transaminated valine and pyruvate are no substrates. In analogy to the pyruvate decarboxylases the enzyme may in a side-reaction catalyze condensation (or carboligation) reactions leading to the formation of 2-hydroxy ketone, collectively called acyloins.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Aromatic amino acid aminotransferase 2
- Aromatic/aminoadipate aminotransferase 1
- Aspartate aminotransferase, mitochondrial
- Aspartate aminotransferase, cytoplasmic
- Transcriptional activator ARO80
- Chorismate mutase
- Histidinol-phosphate aminotransferase
- Phospho-2-dehydro-3-deoxyheptonate aldolase, tyrosine-inhibited
- Branched-chain-amino-acid aminotransferase, cytosolic
- S-
Sequence:
MAPVTIEKFVNQEERHLVSNRSATIPFGEYIFKRLLSIDTKSVFGVPGDFNLSLLEYLYSPSVESAGLRWVGTCNELNAAYAADGYSRYSNKIGCLITTYGVGELSALNGIAGSFAENVKVLHIVGVAKSIDSRSSNFSDRNLHHLVPQLHDSNFKGPNHKVYHDMVKDRVACSVAYLEDIETACDQVDNVIRDIYKYSKPGYIFVPADFADMSVTCDNLVNVPRISQQDCIVYPSENQLSDIINKITSWIYSSKTPAILGDVLTDRYGVSNFLNKLICKTGIWNFSTVMGKSVIDESNPTYMGQYNGKEGLKQVYEHFELCDLVLHFGVDINEINNGHYTFTYKPNAKIIQFHPNYIRLVDTRQGNEQMFKGINFAPILKELYKRIDVSKLSLQYDSNVTQYTNETMRLEDPTNGQSSIITQVHLQKTMPKFLNPGDVVVCETGSFQFSVRDFAFPSQLKYISQGFFLSIGMALPAALGVGIAMQDHSNAHINGGNVKEDYKPRLILFEGDGAAQMTIQELSTILKCNIPLEVIIWNNNGYTIERAIMGPTRSYNDVMSWKWTKLFEAFGDFDGKYTNSTLIQCPSKLALKLEELKNSNKRSGIELLEVKLGELDFPEQLKCMVEAAALKRNKK
Protein: Ribulose bisphosphate carboxylase-like protein (RuBisCO-like protein) (Q8KBL4)
Organism: Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS) (Chlorobium tepidum)
Function: May be involved in sulfur metabolism and oxidative stress response. Does not show RuBisCO activity.
Interaction partners:
- phosphoglycolate phosphatase
- phosphoglycolate phosphatase
- Transporter, putative
- Thioredoxin
- Uncharacterized protein
Sequence:
MNAEDVKGFFASRESLDMEQYLVLDYYLESVGDIETALAHFCSEQSTAQWKRVGVDEDFRLVHAAKVIDYEVIEELEQLSYPVKHSETGKIHACRVTIAHPHCNFGPKIPNLLTAVCGEGTYFTPGVPVVKLMDIHFPDTYLADFEGPKFGIEGLRDILNAHGRPIFFGVVKPNIGLSPGEFAEIAYQSWLGGLDIAKDDEMLADVTWSSIEERAAHLGKARRKAEAETGEPKIYLANITDEVDSLMEKHDVAVRNGANALLINALPVGLSAVRMLSNYTQVPLIGHFPFIASFSRMEKYGIHSKVMTKLQRLAGLDAVIMPGFGDRMMTPEEEVLENVIECTKPMGRIKPCLPVPGGSDSALTLQTVYEKVGNVDFGFVPGRGVFGHPMGPKAGAKSIRQAWEAIEQGISIETWAETHPELQAMVDQSLLKKQD
Protein: Ubiquitin-ribosomal protein eL40y fusion protein (Protein EARLY-RESPONSIVE TO DEHYDRATION 16) (Protein EMBRYO DEFECTIVE 2167) (Protein HAPLESS 4) [Cleaved into: Ubiquitin; Large ribosomal subunit protein eL40y (60S ribosomal protein L40-2) (CEP52)] (Q42202)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).
Subcellular location: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.; SUBCELLULAR LOCATION: [Large ribosomal subunit protein eL40y]: Cytoplasm {ECO:0000250}.
Interaction partners:
- Small ribosomal subunit protein uS14z/uS14y/uS14x
- Protein NBR1 homolog
- Large ribosomal subunit protein eL42z/eL42y
- Large ribosomal subunit protein eL38z/eL38y
- Small ribosomal subunit protein eS6y
- Small ribosomal subunit protein eS24y
- Small ribosomal subunit protein eS30z/eS30y/eS30x
- Small ribosomal subunit protein uS17z
- Small ribosomal subunit protein eS24z
- Large ribosomal subunit protein uL18y
Sequence:
MQIFVKTLTGKTITLEVESSDTIDNVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLADYNIQKESTLHLVLRLRGGIIEPSLMMLARKYNQDKMICRKCYARLHPRAVNCRKKKCGHSNQLRPKKKIK
Protein: Cell division cycle protein 27 homolog A (CDC27 homolog A) (Anaphase-promoting complex subunit 3) (Q06AN9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex controls several key steps in the cell cycle by mediating ubiquitination and subsequent degradation of target proteins such as cyclins. The APC/C complex is required for the female gametophyte development and is involved in several aspect of development by controlling cell division and cell elongation. Involved in the control of endoreduplication. Functionally redundant with CDC27B in the control of gametophyte development.
Subcellular location: Nucleus.
Interaction partners:
- Anaphase-promoting complex subunit 10
- Anaphase-promoting complex subunit 5
- Anaphase-promoting complex subunit 4
- Anaphase-promoting complex subunit 2
- Anaphase-promoting complex subunit 7
- Anaphase-promoting complex subunit 11
- Anaphase-promoting complex subunit 8
- Anaphase-promoting complex subunit 6
- Anaphase-promoting complex subunit 1
- Cell division cycle 20.3, cofactor of APC complex
Sequence:
MMENLLANCVQKNLNHFMFTNAIFLCELLLAQFPSEVNLQLLARCYLSNSQAYSAYYILKGSKTPQSRYLFAFSCFKLDLLGEAEAALLPCEDYAEEVPGGAAGHYLLGLIYRYSGRKNCSIQQFRMALSFDPLCWEAYGELCSLGAAEEASTVFGNVASQRLQKTCVEQRISFSEGATIDQITDSDKALKDTGLSQTEHIPGENQQDLKIMQQPGDIPPNTDRQLSTNGWDLNTPSPVLLQVMDALPPLLLKNMRRPAVEGSLMSVHGVRVRRRNFFSEELSAEAQEESGRRRSARIAARKKNPMSQSFGKDSHWLHLSPSESNYAPSLSSMIGKCRIQSSKEATTSGQSVSDIGSSVDDEEKSNPSESSPDRFSLISGISEVLSLLKILGDGHRHLHMYKCQEALLAYQKLSQKQYNTHWVLMQVGKAYFELQDYFNADSSFTLAHQKYPYALEGMDTYSTVLYHLKEEMRLGYLAQELISVDRLSPESWCAVGNCYSLRKDHDTALKMFQRAIQLNERFTYAHTLCGHEFAALEEFEDAERCYRKALGIDTRHYNAWYGLGMTYLRQEKFEFAQHQFQLALQINPRSSVIMCYYGIALHESKRNDEALMMMEKAVLTDAKNPLPKYYKAHILTSLGDYHKAQKVLEELKECAPQESSVHASLGKIYNQLKQYDKAVLHFGIALDLSPSPSDAVKIKAYMERLILPDELVTEENL
Protein: ADP,ATP carrier protein 3, mitochondrial (ADP/ATP translocase 3) (Adenine nucleotide translocator 3) (ANT 3) (O49447)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: ADP:ATP antiporter that mediates import of ADP into the mitochondrial matrix for ATP synthesis, and export of ATP out to fuel the cell (By similarity). Cycles between the cytoplasmic-open state (c-state) and the matrix-open state (m-state): operates by the alternating access mechanism with a single substrate-binding site intermittently exposed to either the cytosolic (c-state) or matrix (m-state) side of the inner mitochondrial membrane (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:14671022}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- UPF0235 protein At5g63440
- Mitochondrial phosphate carrier protein 2, mitochondrial
- Probable cysteine protease RD21C
- Cysteine proteinase RD21A
- At1g09850
- Probable cysteine protease RD21B
- Mitochondrial succinate-fumarate transporter 1
- Mitochondrial phosphate carrier protein 1, mitochondrial
- Mitochondrial phosphate carrier protein 3, mitochondrial
- Developmentally-regulated G-protein 3
Sequence:
MDGSKHPSVFQKLHGQSYLINRLSPSVQARGYCVSGAYVNGGLQSLLQPTSHGVGSSLIPHGSFPVLAHAPSEKTGTGFLIDFLMGGVSAAVSKTAAAPIERVKLLIQNQDEMIKAGRLSEPYKGISDCFARTVKDEGMLALWRGNTANVIRYFPTQALNFAFKDYFKRLFNFKKEKDGYWKWFAGNLASGGAAGASSLLFVYSLDYARTRLANDAKAAKKGGQRQFNGMVDVYKKTIASDGIVGLYRGFNISCVGIVVYRGLYFGLYDSLKPVVLVDGLQDSFLASFLLGWGITIGAGLASYPIDTVRRRMMMTSGEAVKYKSSLQAFSQIVKNEGAKSLFKGAGANILRAVAGAGVLAGYDKLQLIVLGKKYGSGGG
Protein: Synaptonemal complex protein 2 (Synaptonemal complex central region protein ZYP1b) (P61430)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for chromosome synapsis and normal fidelity of crossing over.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Meiosis-specific protein ASY3
- Meiosis-specific protein ASY1
- Putative recombination initiation defects 3
- Structural maintenance of chromosomes protein 3
- Structural maintenance of chromosomes protein 4
- Maternal effect embryo arrest 22
- Sister chromatid cohesion 1 protein 1
- E3 ubiquitin-protein ligase CCNB1IP1 homolog
- ARM repeat superfamily protein
- Zinc transporter 1
Sequence:
MQKLGFPAMKSFDQLRSLPGSAKTYFFSTRPPQDSVSSGSFSNLKLTAEKLVKDQAAMRTDLELANCKLKKSMEHVYALEEKLQSAFNENAKLRVRQKEDEKLWRGLESKFSSTKTLCDQLTETLQHLASQVQDAEKDKGFFETKFNTSSEAINSLNQQMRDMSLRLDAAKEEITSRDKELEELKLEKQHKEMFYQTERCGTASLIEKKDAVITELETTAAERKLKIEKLNSQLEKLHLELTTKEDEVIHLVSIQEKLEKEKTNVQLSSDELFEKLVRSEQEVKKLDELVHYLIAELTELDKKNLTFKEKFDKLSGLYDTHFMLLRKDRDLASDRAQRSFDQLQGELFRVAAEKEALESSGNELSEKIVELQNDKESLISQLSGVRCSASQTIDKLEFEAKGLVLKNAETESVISKLKEEIDTLLESVRTSEDKKKELSIKLSSLEIESKDKYEKLQADAQRQVGELETLQKESESHQLQADLLAKEVNQLQTIIEEKGHLILQCNENEKNINQQIIKDKELLATAETKLAEAKKQYDLMLESKQLELSRHLKELSQRNDQAINEIRRKYDVEKHEIINSEKDKVEKIIKELSTKYDKGLSDCKEESKRQLLTIQEEHSSRILNIREEHESKELNLKAKYDQELRQNQIQAENELKERITALKSEHDAQLKAFKCQYEDDCKKLQEELDLQRKKEERQRALVQLQWKVMSDNPPEEQEVNSNKDYSHSSVKVKESRLGGNKRSEHITESPFVKAKVTSVSNILKEATNPKHHSKVTHREYEVETNNGRIPKRRKTRQTTMFQEPQRRSTRLTPKLMTPTIIAKETAMADHPHSANIGDLFSEGSLNPYADDPYAFD
Protein: ATP-dependent 6-phosphofructokinase, platelet type (ATP-PFK) (PFK-P) (EC 2.7.1.11) (6-phosphofructokinase type C) (Phosphofructo-1-kinase isozyme C) (PFK-C) (Phosphohexokinase) (P47859)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184}.
Interaction partners:
- Glucose-6-phosphate isomerase
- Triosephosphate isomerase
- Pyruvate kinase PKM
- Fructose-1,6-bisphosphatase 1
- Fructose-bisphosphate aldolase A
- Enolase
- Phosphoglycerate kinase
- Beta-enolase
- Fructose-bisphosphate aldolase
- Beta-enolase
Sequence:
MDNKVSASPRGSYRKFLEHLSGAGKAIGVLTSGGDAQGMNAAVRAVVRMGIYVGAKVYFIYEGYQGMVDGGSNIVEANWESVSSILQVGGTIIGSARSKAFRTREGRLKAACNLIHRGITNLCVIGGSGSLTGANIFRMEWSGLLEELAQDGKIDNEAVQKYAYLNVVGMVGSIDNDFCGTDMTIGTDSACHRIIEVIDAIMTTAQSHQRTFVLEVMGRHCGYLALVSALACGADWVFLPESPPEEGWEEQMCVKLSENRAQKKRLNIIIVAEGAIDTLNRPITSEKIKELVVTQLGYDTRVTILGHVQRGGTPSAFDRILASRMGVEAVLALLEATPETPACVVSLSGNHAVRLPLVECVQMTQEVQKAMDERRFKDAVQLRGRSFENNLNTYKRLAIKLPDDKIQKSNCNVAVINVGAPAAGMNAAVRSAVRVGIADGHKMFAVYDGFDGFAKGQIKEIRWGDVGGWTGQGGSILGTKRILPGKYLEEIATQIRTHNINAILIIGGFEAYLGLLELSAAREKHEEFCVPMVMVPATVSNNVPGSDFSIGADTALNTITDTCDRIKQSASGTKRRVFIIETMGGYCGYLANMGGLAAGADAAYIFEEPFDIRDLQSNVEHLTEKMKTTIQRGLVLRNESCSENYTTDFIYQLYSEEGRGVFDCRKNVLGHMQQGGAPSPFDRNFGTKISARAMQWITTKLKESPGKGKRFVSDDSICVLGISKRNVLFQPVAELKNETDFEHRIPKEQWWLKLRPLMKILAKYKTSYDVSDSGQLVPVRHRGGPEEPAAI
Protein: Protein MID1-COMPLEMENTING ACTIVITY 1 (Q8L7E9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Calcium-permeable stretch-activated channel component. Involved in mechano-stimulated calcium uptake mechanism and in mechanosensing in the primary root.
Subcellular location: Cell membrane {ECO:0000269|PubMed:17360695}; Single-pass membrane protein {ECO:0000269|PubMed:17360695}.
Interaction partners:
- Mechanosensitive ion channel protein 10
- Mechanosensitive ion channel protein 9
- Hyperosmolality-gated Ca2+ permeable channel 1.1
- Protein high chlorophyll fluorescent 107
- Two pore calcium channel protein 1
- Receptor-like protein kinase THESEUS 1
- Mechanosensitive ion channel protein 8
- LRR receptor-like serine/threonine-protein kinase FEI 2
- Mechanosensitive ion channel protein 4
- Mechanosensitive ion channel protein 2, chloroplastic
Sequence:
MSHSWDGLGEIASVAQLTGLDAVKLIGLIVKAANTAWMHKKNCRQFAQHLKLIGNLLEQLKISEMKKYPETREPLEGLEDALRRSYLLVNSCRDRSYLYLLAMGWNIVYQFRKHQDEIDRFLKIIPLITLVDNARIRERFEYIDRDQREYTLDEEDRHVQDVILKQESTREAASVLKKTLSCSYPNLRFCEALKTENEKLQIELQRSQEHYDVAQCEVIQRLIGVTQAAAAVEPDSEKELTKKASKKSERSSSMKTEYSYDEDSPKKSSTRAASRSTSNVSSGHDLLSRRASQAQHHEEWHTDLLACCSEPSLCFKTFFFPCGTLAKIATAASNRHISSAEACNELMAYSLILSCCCYTCCVRRKLRKTLNITGGFIDDFLSHVMCCCCALVQELREVEIRGAYGTEKTKISPPSSQFMEH
Protein: Scavenger receptor (Q58SM2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
TCDRDGRLRGEKPFCASRGCARPEDPENGHVENLSLRADVVCHDGYVLVGGRTAYCDGERWSTQLGSCRRSNHTRDHSCDFESEDQCGWEAETTFRRPWKRVSTVSDIHSLRTGPRHDHTFKNESGGHYMRMETQMGAYGSYHLLSPIYPRSLTLKTACCFRFHYFMFGAGVDNLVVSVKPVSMPMATMWNRFRANCSKFEISGQQGTQWLEHTISIDEMQEDFQVIFTATDARSQFGDIAIDDVKLMTGSECGTNGFTTTTEPTAPTGSNEQPLVYDMMSCSGRCGTSISASNITNNGIVMGCGCNDECLSDETCCLNYLEECTKELLTTTEDDISSLPPTVTSTSTSTTRKSTTTTTTSTTSTSTTTTKRPTTTTTTTKATTTKRTTTTKKPTTTSTTPKPTTTTSTTPMTTTSTTFTTSTTSTRPTTTTTINVFTTKKTTIMIPTSSTEKTTGINTTMKTLKRITWNVDPQDIEGHMDTSGSTPNPALVVLYLLLGIVLVVVLANVVNRWIIPITGSKTSSEKAVRFKKAFDSLKKQRKRNSMDDQPLCDSDNDDVEYFEEMGVDIRHRTDL
Protein: Chelated iron transport system membrane protein YfeB (Q56953)
Organism: Yersinia pestis
Function: Part of an ATP-driven transport system YfeABCD for chelated iron.
Subcellular location: Cell inner membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- Chelated iron transport system membrane protein YfeC
- Iron-binding protein YfeA
- Chelated iron transport system membrane protein YfeD
- Similar to Escherichia coli high-affinity zinc uptake system membrane protein ZnuB SW:ZNUB_ECOLI
- High-affinity zinc uptake system protein ZnuA
Sequence:
MSHPVFVRPELVVDNVTVTYNNGHTAIYDASFSLTGGTICALVGVNGSGKSTLFKSIMGLVKPSVGKVELSHKPISHALKQNTIAYVPQTEDVDWNFPVLVEDVVMMGRYGKMNFLRIPSREDKAIVNKSIERVGLTALRSRQIGELSGGQKKRVFLARALAQQGTLLLLDEPFTGVDVKTENAIIELLQSLRDEGHLILVSTHNLGSVPEFCDHVILINQTVLAAGPIETTFTQKNLEMTFGGVLRHINLSGTALHDDNDPRTVTVITDDERPAVFYGHTKNDPPAQSQSKEQNS
Protein: Ent-kaurene synthase TSP4, chloroplastic (EC 4.2.3.19) (Terpene synthase 4) (VacTPS4) (A0A2K9RFY0)
Organism: Vitex agnus-castus (Chaste tree)
Function: Involved in the biosynthesis of labdane-type diterpenoid including cleroda-dienols, and peregrinol lactones and furan derivatives, dopaminergic diterpenoids that can bind to dopamine receptors in the human pituitary gland, have probably ability to lower prolactin levels, and are used to treat menstrual cycle disorders (e.g. premenstrual syndrome and mastodynia) (Probable). Terpene synthase that produces ent-kaurene from ent-copalyl diphosphate.
Subcellular location: Plastid, chloroplast membrane {ECO:0000305|PubMed:29315936}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MSLQLSNSLFFARKESHFRCFSHVSASLDTGVRRVTSAKIASTCFEETKERIADLIHKAELSVSTYDTAWVAMVPSPNSSQEPCFPDCLSWLLQNQCCDGSWACPHHHPLLKKDVLCSTLACVLALKKWGVGEEKINRGVHFIEHNFASAMEKCQISPMGFDIIFPAMLDYARDLLLNLRLEPTMLNDLIYKRGLELKRNQNHSAEREAYLAYVAEGMGKLQDLGSVMKHQRRNGSLFNSPSTTAAAFIAFPNSRCLTYLRSALKKFGSAVPAVYPLDIYLQLCTVDNLERLGISRYFQKEIQGVLDETYRCWLQGNEEIFMDAPTCALAFRVLRKNGYNVTSDPITKLLEECFSSSFCGNIKDINTTLGLYRASEFILYPDERDLEKQNLMLKNLLEQELSSDFIHSSQLGRNIDAEVKHALEYPFYADLDRIVNRRNIEHYNFDNTRILKTSYCSPNFGNKDFLFLSVKDYNECQAIHREELRELERWVIENRLDELRFARQKCAYCYFSAAATLFAPELSNARMSWAKNGVLTTVVDDFFDLGGSVEELKNLIQLVELWDVDVSTECSSQNVQIIFSALKCTICDIGDKGSKLQERSITNHIIDIWLDLLYSMMKETEWARDKYIPTMDEYISNAYVSFALGPIVLPALYLVGPKLSEEMVHHSEYHNLYKLMSTCGRLLNDIRGCERELKEGKLNAIPLYIINNGGEITKEAAASEMKSLIETHRRELLRLVLEGKNSVLPKSCKELFWHMSKVLHLFYSKDDGFTSQDLIKVVKAVIYEPIVLK
Protein: Spermidine-binding periplasmic protein SpuE (Q9I6J0)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Spermidine-binding protein probably required for its uptake into cells. Binds spermidine with high affinity (KD=14.3 nM). Does not bind putrescine, cadaverine or spermine. Spermidine binding induces large inter-domain conformational changes. Implicated in induction of type 3 secretion systems (T3SS), which play a role in virulence.
Subcellular location: Periplasm {ECO:0000255|PIRNR:PIRNR019574}.
Interaction partners:
- Polyamine transport protein PotH
- Spermidine/putrescine import ATP-binding protein PotA
- Putrescine transport system permease protein PotI
- Spermidine/putrescine transport system permease protein PotC
- Polyamine transport protein PotC
- Spermidine/putrescine transport system permease protein PotC
- Polyamine transport protein PotB
- Probable permease of ABC transporter
- Probable permease of ABC transporter
- Probable permease of ABC transporter
Sequence:
MQHSIGKTLLVAALATAIAGPVQAEKKSLHIYNWTDYIAPTTLKDFTKESGIDVSYDVFDSNETLEGKLVSGHSGYDIVVPSNNFLGKQIQAGAFQKLDKSKLPNWKNLDPALLKQLEVSDPGNQYAVPYLWGTNGIGYNVAKVKEVLGDQPIDSWAILFEPENMKKLAKCGVAFMDSGDEMLPAALNYLGLDPNTHDPKDYKKAEEVLTKVRPYVSYFHSSKYISDLANGNICVAFGYSGDVFQAAARAEEAGKGIDIQYVIPKEGANLWFDLMAIPADAKAADNAYAFIDYLLRPEVIAKVSDYVGYANAIPGARPLMDKSVSDSEEVYPPQAVLDKLYVSAVLPAKVLRLQTRTWTRIKTGK
Protein: Taste receptor type 1 member 3 (Sweet taste receptor T1R3) (Q7RTX0)
Organism: Homo sapiens (Human)
Function: Putative taste receptor. TAS1R1/TAS1R3 responds to the umami taste stimulus (the taste of monosodium glutamate). TAS1R2/TAS1R3 recognizes diverse natural and synthetic sweeteners. TAS1R3 is essential for the recognition and response to the disaccharide trehalose (By similarity). Sequence differences within and between species can significantly influence the selectivity and specificity of taste responses.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Taste receptor type 1 member 1
- Guanine nucleotide-binding protein G
- Taste receptor type 1 member 2
- Sodium/glucose cotransporter 1
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Taste receptor type 2 member 4
- Pro-glucagon
- Transient receptor potential cation channel subfamily M member 5
Sequence:
MLGPAVLGLSLWALLHPGTGAPLCLSQQLRMKGDYVLGGLFPLGEAEEAGLRSRTRPSSPVCTRFSSNGLLWALAMKMAVEEINNKSDLLPGLRLGYDLFDTCSEPVVAMKPSLMFLAKAGSRDIAAYCNYTQYQPRVLAVIGPHSSELAMVTGKFFSFFLMPQVSYGASMELLSARETFPSFFRTVPSDRVQLTAAAELLQEFGWNWVAALGSDDEYGRQGLSIFSALAAARGICIAHEGLVPLPRADDSRLGKVQDVLHQVNQSSVQVVLLFASVHAAHALFNYSISSRLSPKVWVASEAWLTSDLVMGLPGMAQMGTVLGFLQRGAQLHEFPQYVKTHLALATDPAFCSALGEREQGLEEDVVGQRCPQCDCITLQNVSAGLNHHQTFSVYAAVYSVAQALHNTLQCNASGCPAQDPVKPWQLLENMYNLTFHVGGLPLRFDSSGNVDMEYDLKLWVWQGSVPRLHDVGRFNGSLRTERLKIRWHTSDNQKPVSRCSRQCQEGQVRRVKGFHSCCYDCVDCEAGSYRQNPDDIACTFCGQDEWSPERSTRCFRRRSRFLAWGEPAVLLLLLLLSLALGLVLAALGLFVHHRDSPLVQASGGPLACFGLVCLGLVCLSVLLFPGQPSPARCLAQQPLSHLPLTGCLSTLFLQAAEIFVESELPLSWADRLSGCLRGPWAWLVVLLAMLVEVALCTWYLVAFPPEVVTDWHMLPTEALVHCRTRSWVSFGLAHATNATLAFLCFLGTFLVRSQPGCYNRARGLTFAMLAYFITWVSFVPLLANVQVVLRPAVQMGALLLCVLGILAAFHLPRCYLLMRQPGLNTPEFFLGGGPGDAQGQNDGNTGNQGKHE