wanglab/gogpt-training-data huggingface dataset:
Protein: Rifin (Q8I211)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKVHYINILLFALPLYILDHKQRNHNSTTYHASKTKSIKTHRSLCECELYAPSDYDNDAEMIRVMQQFHDRTTQRFQEYDERLQENRQIYKDTCDKEIQKIILKDKIEKELTEKFSALHTDIQSDGIPTCICEKSLADKVEKVCLRCGSILGAAMPEVGSIGGGLLYALNAWKTDAIAAATKAAMIEGAAQGAVAGEAAGRNAIIGALKRYFHIDNLNGTSLKSFFNSTSYSDVTTIASAIDTQMTASCDAFSGKIVNQAFCDVRKTLRIVADPGKSFVKQKDAITGAVTQLVEKAKDTASFKATEVSSATSSKIITKQNALIEAGFDSSTTSIYASIIVILIIVLIMVIIYLILRYRRKKKMKKKLQYIKLLEE
Protein: Neuroendocrine protein 7B2 (Secretogranin V) (Secretogranin-5) (Secretory granule endocrine protein I) [Cleaved into: N-terminal peptide; C-terminal peptide] (P27682)
Organism: Rattus norvegicus (Rat)
Function: Acts as a molecular chaperone for PCSK2/PC2, preventing its premature activation in the regulated secretory pathway. Binds to inactive PCSK2 in the endoplasmic reticulum and facilitates its transport from there to later compartments of the secretory pathway where it is proteolytically matured and activated. Also required for cleavage of PCSK2 but does not appear to be involved in its folding. Plays a role in regulating pituitary hormone secretion. The C-terminal peptide inhibits PCSK2 in vitro.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P01165}. Note=Neuroendocrine and endocrine secretory granules. {ECO:0000250|UniProtKB:P01165}.
Interaction partners:
- Neuroendocrine convertase 2
- Secretogranin-1
- Secretogranin-3
- Secretogranin-2
Sequence:
MTSRMAILSGLLFWLLLEWNPAFAYSPRTPDRVSETDIQRLLHGVMEQLGIARPRVEYPAHQAMNLVGPQSIEGGAHEGLQHLGPFGNIPNIVAELTGDNIPKDFSEDQGYPDPPNPCPLGKTADDGCLENAPDTAEFSREFQLDQHLFDPEHDYPGLGKWNKKLLYEKMKGGQRRKRRSVNPYLQGKRLDNVVAKKSVPHFSEEEKEPE
Protein: Vascular endothelial growth factor receptor 3 (VEGFR-3) (EC 2.7.10.1) (Fms-like tyrosine kinase 4) (FLT-4) (Tyrosine-protein kinase receptor FLT4) (Q91ZT1)
Organism: Rattus norvegicus (Rat)
Function: Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFC and VEGFD, and plays an essential role in adult lymphangiogenesis and in the development of the vascular network and the cardiovascular system during embryonic development. Promotes proliferation, survival and migration of endothelial cells, and regulates angiogenic sprouting. Signaling by activated FLT4 leads to enhanced production of VEGFC, and to a lesser degree VEGFA, thereby creating a positive feedback loop that enhances FLT4 signaling. Modulates KDR signaling by forming heterodimers. Mediates activation of the MAPK1/ERK2, MAPK3/ERK1 signaling pathway, of MAPK8 and the JUN signaling pathway, and of the AKT1 signaling pathway. Phosphorylates SHC1. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase. Promotes phosphorylation of MAPK8 at 'Thr-183' and 'Tyr-185', and of AKT1 at 'Ser-473' (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P35917}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P35917}. Cytoplasm {ECO:0000250|UniProtKB:P35917}. Nucleus {ECO:0000250|UniProtKB:P35916}. Note=Ligand-mediated autophosphorylation leads to rapid internalization. {ECO:0000250|UniProtKB:P35917}.
Interaction partners:
- Vascular endothelial growth factor D
- Vascular endothelial growth factor C
- Vascular endothelial growth factor B
- Placenta growth factor
- Platelet-derived growth factor C
- Vascular endothelial growth factor receptor 2
- Vascular endothelial growth factor A
- Neuropilin-2
- Growth factor receptor-bound protein 2
- Angiopoietin-2
Sequence:
MQPGAALNRRLWLCLGLLQGLANGYSMTPPTLNITEDSYVIDTGDSLSISCRGQHPLEWTWRGAQEVLTTGGKDSEDTQVVQDCEGTEARPYCKVLSLAQTHANNTGSYYCYYKYIKARIEGTTAASTYVFVRDFEQPFINKPDTLLVNRKDSMWVPCLVSIPGLNITLRSQSSVLHPDGQEVLWDDRRGMRVPTLLLRDALYLQCETTWGDQDFLSNPFLVHITGNELYDIQLYPKKSLELLVGEKLVLNCTVWAEFDSGVTFDWDYPGKQAERAKWVPERRSQQTHTELSSILTIHNVSQHDLGPYVCEANNGIQQFRESTEVIVHEKPFISVEWLKGPVLEATAGDEMVKLPVKLAAYPPPEFQWYKDRKAVTGRHNPHALVLKEVTEASAGVYTLALWNSAAGLRQNISLELVVNVPPHIHEKEASSPSIYSRHSRQTLTCTTYGVPQPLSVQWHWRPWTPCKTFAQRSLRRRQPRDGMPQCRDWKEVTTQDAVNPIESLDTWTESVEGKNKTVSKLVIQDANVSAMYKCVVFNKVGQDERLIYFYVTTIPDGFSIESEPSEDPLEGQSVRLSCRADNYTYEHLRWYRLNLSTLHDAQGNPLLLDCKNVHLFATPLEANLEEAEPGARHATLSLNIPRVAPEDEGDYVCEVQDRRSQDKHCHKKYLSVQALEAPRLTQNLTDLLVNVRTSLEMRCPVAGAHVPSIVWYKDERLLEKESGIDLADSNQRLSIQRVREEDAGRYLCSVCNAKGCVNSSASVAVEGSEDKGSMEIVILIGTGVIAVFFWVLLLLIFCNMKRPAHADIKTGYLSIIMDPGEVPLEEQCEYLSYDVSQWEFPRERLHLGRVLGHGAFGKVVEASAFGINKGSSCDTVAVKMLKEGATASEHRALMSELKILIHIGNHLNVVNLLGACTKPNGPLMVIVEFCKYGNLSNFLRVKRETFDPYAEKSPEQRRRFRAMVEGAKADRRRLGSTDRALFTRFLMGKGSARRAPFVQEAEDLWLSPLTMEDLVCYSFQVARGMEFLASRKCIHRDLAARNILLSESDIVKICDFGLARDIYKDPDYVRKGSARLPLKWMAPESIFDKVYTTQSDVWSFGVLLWEIFSLGASPYPGVQINEEFCQRLKDGTRMRAPELATPAIRHIMQSCWSGDPKARPAFSDLVEILGDLLQGGGWQEEEEECMALHSSQSSEEDGFMQASTTALHITEADAESSPPSMHCHSLAARYYNCVSFPGRLVRGTKAPGSSRMKTFEELPMTPTTYKASVDNQTDSGMVLASEEFEQIESRHRQEGSFSRKDPGQHMDISRGHPDLQGRRRRPTQGAQGGKVFYNNEYGEVSQPCTEGDCCPSAGSTFFADSNY
Protein: Pleckstrin homology domain-containing family O member 1 (PH domain-containing family O member 1) (Q9JIY0)
Organism: Mus musculus (Mouse)
Function: Plays a role in the regulation of the actin cytoskeleton through its interactions with actin capping protein (CP). May function to target CK2 to the plasma membrane thereby serving as an adapter to facilitate the phosphorylation of CP by protein kinase 2 (CK2). Appears to target ATM to the plasma membrane. Appears to also inhibit tumor cell growth by inhibiting AKT-mediated cell-survival. Also implicated in PI3K-regulated muscle differentiation, the regulation of AP-1 activity (plasma membrane bound AP-1 regulator that translocates to the nucleus) and the promotion of apoptosis induced by tumor necrosis factor TNF. When bound to PKB, it inhibits it probably by decreasing PKB level of phosphorylation (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q53GL0}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q53GL0}. Nucleus {ECO:0000250|UniProtKB:Q53GL0}. Cytoplasm {ECO:0000250|UniProtKB:Q53GL0}. Note=Predominantly localized to the plasma membrane through the binding to phosphatidylinositol 3-phosphate. In C2C12 cells, with the absence of growth factor, it is found in the nucleus. It rapidly translocates to the plasma membrane after insulin stimulation. In response to TNF, it translocates from the plasma membrane to the cytoplasm and then to the nucleus accompanied by cleavage by caspase-3. However, the subcellular location is highly dependent of the cell type, and this explains why it is found exclusively at the plasma membrane, in some type of cells. {ECO:0000250|UniProtKB:Q53GL0}.
Interaction partners:
Sequence:
MKKSGSGKRGPPDGNHQSAAPEKVGWVRKFCGKGIFREIWKNRYVVLKGDQLYVSEKEVKDEKNSQEVFDLSDYEKCEELRKSKSRSKKNHSKFTLARCRQPGTTAPNLIFLAVSPEEKESWINALSSAITRAKNRILDEVTVEEDSYLAHPTRDRAKIQHSRRPPTRGHLMAVASTSTSDGMLTLDLIQEEDPSPEEPASCAESFRVDLDKSVAQLAGSRRRADSDRIQPSSQRASSLSRPWEKPDKGAPYTPQALKKFPSTEKSRCASLEEILSQRDTAPARPLHLQAEESLPPVPAQPGQLSRIQDLVARKLEKTQELLAEVQGLGDGKRKAKDPPQSPPDSESEQLLLETERLLGEASSNWSQAKRVLQEVRELRDLYRQMDLQTPDSHLRQTSQHSQYRKSLM
Protein: Structural maintenance of chromosomes protein 6 (DNA repair protein RHC18) (Rad18 homolog) (Q12749)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acts in a DNA repair pathway for removal of UV-induced DNA damage that is distinct from classical nucleotide excision repair and in repair of ionizing radiation damage. Functions in homologous recombination repair of DNA double strand breaks and in recovery of stalled replication forks. Probably plays a role in structure.
Subcellular location: Nucleus. Chromosome.
Interaction partners:
- Non-structural maintenance of chromosome element 3
- E3 SUMO-protein ligase MMS21
- Structural maintenance of chromosomes protein 5
- Non-structural maintenance of chromosome element 4
- Non-structural maintenance of chromosomes element 1
- DNA repair protein KRE29
- Non-structural maintenance of chromosome element 5
- Regulator of Ty1 transposition protein 107
- Structural maintenance of chromosomes protein 3
- ATP-dependent helicase SGS1
Sequence:
MISTTISGKRPIEQVDDELLSLTAQQENEEQQQQRKRRRHQFAPMTQFNSNTLDEDSGFRSSSDVATADQDNFLEESPSGYIKKVILRNFMCHEHFELELGSRLNFIVGNNGSGKSAILTAITIGLGAKASETNRGSSLKDLIREGCYSAKIILHLDNSKYGAYQQGIFGNEIIVERIIKRDGPASFSLRSENGKEISNKKKDIQTVVDYFSVPVSNPMCFLSQDAARSFLTASTSQDKYSHFMKGTLLQEITENLLYASAIHDSAQENMALHLENLKSLKAEYEDAKKLLRELNQTSDLNERKMLLQAKSLWIDVAHNTDACKNLENEISGIQQKVDEVTEKIRNRQEKIERYTSDGTTIEAQIDAKVIYVNEKDSEHQNARELLRDVKSRFEKEKSNQAEAQSNIDQGRKKVDALNKTIAHLEEELTKEMGGDKDQMRQELEQLEKANEKLREVNNSLVVSLQDVKNEERDIQHERESELRTISRSIQNKKVELQNIAKGNDTFLMNFDRNMDRLLRTIEQRKNEFETPAIGPLGSLVTIRKGFEKWTRSIQRAISSSLNAFVVSNPKDNRLFRDIMRSCGIRSNIPIVTYCLSQFDYSKGRAHGNYPTIVDALEFSKPEIECLFVDLSRIERIVLIEDKNEARNFLQRNPVNVNMALSLRDRRSGFQLSGGYRLDTVTYQDKIRLKVNSSSDNGTQYLKDLIEQETKELQNIRDRYEEKLSEVRSRLKEIDGRLKSTKNEMRKTNFRMTELKMNVGKVVDTGILNSKINERKNQEQAIASYEAAKEELGLKIEQIAQEAQPIKEQYDSTKLALVEAQDELQQLKEDINSRQSKIQKYKDDTIYYEDKKKVYLENIKKIEVNVAALKEGIQRQIQNACAFCSKERIENVDLPDTQEEIKRELDKVSRMIQKAEKSLGLSQEEVIALFEKCRNKYKEGQKKYMEIDEALNRLHNSLKARDQNYKNAEKGTCFDADMDFRASLKVRKFSGNLSFIKDTKSLEIYILTTNDEKARNVDTLSGGEKSFSQMALLLATWKPMRSRIIALDEFDVFMDQVNRKIGTTLIVKKLKDIARTQTIIITPQDIGKIADIDSSGVSIHRMRDPERQNNSNFYN
Protein: Uncharacterized protein, isoform D (EC 2.3.1.225) (M9PFJ4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MHIGSLLSLATHVNLLIIDEQIRRQYVVLHFSRFFLFLKPMSCELIALNISFIINIYACILSLIMLGYQIPALYLNTTFYTPKDYRYNQGLLGNFMAFMGKRGLWTFISPSIRSPLPHDGTKWQTKQAPTTF
Protein: Noelin-2 (Olfactomedin-2) (Q8BM13)
Organism: Mus musculus (Mouse)
Function: Involved in transforming growth factor beta (TGF-beta)-induced smooth muscle differentiation (By similarity). TGF-beta induces expression and nuclear translocation of OLFM2 where it binds to SRF, causing its dissociation from the transcriptional repressor HEY2/HERP1 and facilitating binding of SRF to target genes (By similarity). Plays a role in AMPAR complex organization. Is a regulator of vascular smooth-muscle cell (SMC) phenotypic switching, that acts by promoting RUNX2 and inhibiting MYOCD binding to SRF. SMC phenotypic switching is the process through which vascular SMCs undergo transition between a quiescent contractile phenotype and a proliferative synthetic phenotype in response to pathological stimuli. SMC phenotypic plasticity is essential for vascular development and remodeling (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:O95897}. Synapse {ECO:0000269|PubMed:25218043, ECO:0000305|PubMed:22632720}. Membrane {ECO:0000269|PubMed:25218043}. Nucleus {ECO:0000250|UniProtKB:O95897}. Cytoplasm {ECO:0000250|UniProtKB:O95897}. Note=Nuclear localization is induced by TGF-beta. {ECO:0000250|UniProtKB:O95897}.
Interaction partners:
- Glutamate receptor 1
- Glutamate receptor 2
- Noelin
- Glutamate receptor 4
- Glutamate receptor 3
- Voltage-dependent calcium channel gamma-3 subunit
- Noelin-3
- Leucine-rich repeat transmembrane neuronal protein 4
- Neuritin
- Disks large homolog 4
Sequence:
MRKLRQTGTTIAGGQTLFQSPEEGWQLYTSAQAPDGKCVCTAVIPAQSTCARDGRSRELRQLMEKVQNVSQSMEVLELRTFRDLQYVRSMETLMRSLDARLRAADGSVSAKSFQELKDRMTELLPLSSVLEQYKADTRTIVRLREEVRNLSGNLAAIQEEMGAYGYEDLQQRVMALEARLHACAQKLGCGKLTGVSNPITIRAMGSRFGSWMTDTMAPSADSRVWYMDGYYKGRRVLEFRTLGDFIKGQNFIQHLLPQPWAGTGHVVYNGSLFYNKYQSNVVVKYHFRSRSVLVQRSLPGAGYNNTFPYSWGGFSDMDFMVDESGLWAVYTTNQNAGNIVVSRLDPHTLEVVRSWDTGYPKRSAGEAFMICGVLYVTNSHLAGAKVYFAYFTNTSSYEYTDVPFHNQYSHISMLDYNPRERALYTWNNGHQVLYNVTLFHVISTAGDP
Protein: Histone-lysine N-methyltransferase SET5 (EC 2.1.1.-) (SET domain-containing protein 5) (P38890)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Putative protein lysine methyltransferase that acts as a virus host factor involved in the replication of positive-strand RNA viruses like the MBV.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22343720}. Chromosome {ECO:0000269|PubMed:22343720}. Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22343720}.
Interaction partners:
- Histone-lysine N-methyltransferase, H3 lysine-4 specific
- Histone H4
- SET domain-containing protein 4
- Potential protein lysine methyltransferase SET6
- Histone-lysine N-methyltransferase, H3 lysine-36 specific
- Histone H3
- Pyrimidine pathway regulatory protein 1
- Ribosomal lysine N-methyltransferase 1
- COMPASS component BRE2
- COMPASS component SDC1
Sequence:
MTLTIKIGTLNDSDQSAVHNGTENGSDFRKITPTEEEICDDVVLLWKEEPGTEDATIQHLYDRITERNQSWKLSASRFRKILNEHHLYDTDLETVSLYKDKIHFPKALDSDAKVEVKFIDDEHGRGLFAKRDFSKGQIILKENKPIVYIPPLDKLFLISNGKACARCGKALYDLTQHKIMVHYLDCEVCKAIWCSEKCKKAHASLHELLYHSWRSNRIDILHAGNWKRFVNYCEKYCFTAAFSVGLIYGSMLLDTTGEVKEQWQKLASISQRERIKLRDASGIGSTFSLLNGTTVHTEEESDNGTKKGVEKNIDDETVWEKCYELFCGAFPKASEEIDFEKFLTMIGTFNINQYNGQVYHWISFINHDCEPNAYIEQVEEHEELRLHARKPIKKGEQIRITYVNPLHGVRLRRRELRVNWGFLCQCDRCQNELSTFERVPNLEKKNADANLGVEKIDSNDSSEDGSKKSTGNRKSSMREAQPDLKEILKNGKEFELDIPETVDTQGNVRKTSVRFDSNVSVAVDER
Protein: Cytochrome c oxidase subunit 1 (EC 7.1.1.9) (Cytochrome c oxidase polypeptide I) (P05503)
Organism: Rattus norvegicus (Rat)
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P00396}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P00396}.
Interaction partners:
- Cytochrome c oxidase subunit 3
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome c oxidase subunit 2
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome c oxidase subunit 7C, mitochondrial
- Cytochrome b
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome c oxidase subunit 6C-2
- NADH-ubiquinone oxidoreductase chain 4
- Cytochrome c oxidase subunit 4 isoform 1, mitochondrial
Sequence:
MLVNRWLFSTNHKDIGTLYLLFGAWAGMVGTALSILIRAELGQPGALLGDDQIYNVIVTAHAFVMIFFMVMPMMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMTQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGLDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFSGYTLNDTWAKAHFAIMFVGVNMTFFPQHFLGLAGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVLVMIFMIWEAFASKREVLSISYSSTNLEWLHGCPPPYHTFEEPSYVKVK
Protein: LIM domain binding 2 (E9PFI4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSSTPHDPFYSSPFGPFYRRHTPYMVQPEYRIYEMNKRLQSRTEDSDNLWWDAFATEFFEDDATLTLSFCLEDGPKRYTIGRTLIPRYFSTVFEGGVTDLYYILKHSKESYHNSSITVDCDQCTMVTQHGKPMFTKVCTEGRLILEFTFDDLMRIKTWHFTIRQYRELVPRSILAMHAQDPQVLDQLSKNITRMGLTNFTLNYLRLCVILEPMQELMSRHKTYNLSPRDCLKTCLFQKWQRMVAPPAEPTRQPTTKRRKRKNSTSSTSNSSAGNNANSTGSKKKTTAANLSLSSQVPIASIARSPVSGCALRT
Protein: Plastin-1 (Q3V0K9)
Organism: Mus musculus (Mouse)
Function: Actin-bundling protein. In the inner ear, it is required for stereocilia formation. Mediates liquid packing of actin filaments that is necessary for stereocilia to grow to their proper dimensions.
Subcellular location: Cytoplasm {ECO:0000250}. Cell projection, stereocilium {ECO:0000269|PubMed:25124451, ECO:0000269|PubMed:27811163}.
Interaction partners:
- Fascin-2
- Ezrin
- Twinfilin-1
- Xin actin-binding repeat-containing protein 2
- Espin
- Unconventional myosin-VIIa
- Radixin
- Chloride intracellular channel protein 5
- Moesin
- Myosin-9
Sequence:
MENSTTTISREELEELQEAFNKIDIDNSGYVSDYELQDLFKEASLPLPGYKVREIVEKILVVADNNKDGKISFEEFVSLMQELKSKDISKTFRKIINKREGITAIGGTSSISSEGTQHSYSEEEKVAFVNWINKALENDADCSHLLPMNPNDGSLFKSLADGILLCKMINLSEPDTIDERAINKKKLTPFTVSENLNLALNSASAIGCTVVNIGAQDLKEGKPHLVLGLLWQIIKVGLFADIEISRNEALIALLKDGEDLEELMKLSPEELLLRWVNYHLTNAGWRTINNFSQDIKDSKAYFHLLNQIAPKGDRDDGPAVAIDLSGFNEKNDLKRAGFMLQEADKLGCRQFVTPADVVSGNPKLNLAFVANLFNTYPCLHKPDNNDIDLNLLEGESKEERTFRNWMNSLGVNPYINHLYSDLADALVIFQLYEMIRVPVNWSQVNKPPYPALGGNMKKIENCNYAVELGKNEAKFSLVGIAGQDLNEGNATLTLALVWQLMRRYTLKVLSDLGEGEKVTDDIIIKWVNQTLKSANKSTSISSFKDKSISTSLPVLDLIDAIAPNAVRQEMIKREHLTDEDKLNNAKYAISVARKIGARIYALPDDLVEVKPKMVMTVFACLMGKGLNRLK
Protein: Nicotinate/nicotinamide mononucleotide adenyltransferase (F4K688)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MDVPLPVEKLSYGSNTEDKTCVVLVATGSFNPPTFMHLRMFELARDELRSKGFHVLGGYMSPVNDAYKKKIMCRAFYLQNIFSLVEQCVVYKNVEAVSTGISKQLPTNFDGFIKGQDFLNNKSTCTRGVACYVFIIRASHYANDKHKFILMLESLKVMLLCGSDLLLSFCTPGVWIPEQLRTICKDYGIVCIRREGQDVENMISGDEILNENCANVKIVDNTVPNQISSSRLRQCISRGLSVKYLTEDGVIDYIRQHQLYTELT
Protein: Acetyltransferase PA3944 (EC 2.3.1.-) (GCN5-related N-acetyltransferase) (GNAT) (Q9HX72)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Catalyzes the transfer of an acetyl group from acetyl coenzyme A (AcCoA) to an acceptor substrate and releases both CoA and the acetylated product. It prefers the peptide Asp-Phe methyl ester (or aspartame) and the peptide antibiotics polymyxin B and colistin. Other substrates like dopamine, serotonin, puromycin, chloramphenicol, D-glucosamine, glycine and N-alpha-acetyl-L-glutamine are used and displayed lower activity.
Interaction partners:
- HAD family hydrolase
- Acyl-CoA thioesterase 2
- N-acetyltransferase domain-containing protein
- Arylamine N-acetyltransferase
- N-acetyltransferase domain-containing protein
- [Ribosomal protein uS5]-alanine N-acetyltransferase
- N-acetyltransferase domain-containing protein
- Acetyltransferase PA2578
- SagB/ThcOx family dehydrogenase
Sequence:
MNANLPPSAISELHGPRLLLRAWRDSDREAFAEMCADPQVMEFFPSVLDRAQSDALVDRVQAHFAERGYGPWALELPGEAAFIGFTGLFDVTMDVHFAPTVEIGWRLAPAYWGRGLAREAAETALDFAFERLRLPEVVAFTTPPNRRSWGLMERLGMRRDPAEDFDHPLLAADHPMRRHILYRVDAARWAER
Protein: Tubulin beta-2B chain (T beta-15) (Q3KRE8)
Organism: Rattus norvegicus (Rat)
Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin. Plays a critical role in proper axon guidance in both central and peripheral axon tracts. Implicated in neuronal migration (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9BVA1}.
Interaction partners:
- Tubulin alpha-1B chain
- Microtubule-associated protein tau
- Tubulin alpha-1A chain
- Tubulin alpha-8 chain
- Tubulin alpha-1C chain
- Tubulin alpha-4A chain
- Tubulin alpha chain
- Tubulin alpha-3 chain
- Gap junction alpha-1 protein
- Cytoplasmic dynein 1 heavy chain 1
Sequence:
MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEATGNKYVPRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDSKNMMAACDPRHGRYLTVAAIFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATADEQGEFEEEEGEDEA
Protein: Fatty-acid and retinol-binding protein 1 (Antigen maltose-binding protein) (Ov-FAR-1) (Ov20) (OvMBP/11) (OvS1) (S1 protein) (Q25619)
Organism: Onchocerca volvulus
Function: Binds retinol. Also binds the fluorescent fatty acids 11-((5-dimethylaminonaphthalene-1-sulfonyl)amino)undecanoic acid (DAUDA), dansyl-DL-alpha-aminocaprylic acid (DACA) and parinaric acid. Binds long chain fatty acids, with highest affinity for arachidonic acid, linoleic acid and oleic acid. These long chain fatty acids can act competitively to displace bound fluorescent fatty acids and retinol. May compete with host albumin for fatty acid-binding.
Subcellular location: Secreted {ECO:0000269|PubMed:12106870, ECO:0000269|PubMed:7770083, ECO:0000269|PubMed:9223154}.
Interaction partners:
- Tudor domain-containing protein.
- Small nuclear ribonucleoprotein Sm D2.
- DNA polymerase.
- Small nuclear ribonucleoprotein E
- Sm domain-containing protein
- Small nuclear ribonucleoprotein G.
- Proliferating cell nuclear antigen
- Sm domain-containing protein.
- Small nuclear ribonucleoprotein Sm D1
- DNA_pol_D_N domain-containing protein.
Sequence:
MYHQLILMALIGVIMANVVPFSMSNIPEEYKEFIPEEVKNFYKNLTQEDRQILRELASKHATFTNEDAALEALKNKSDKLYQKAVELRNFVKAKIDSLKPDAKAFVDEIIAKVRSLRPEDGQKLDMEKLKQAARDIIAKYEALNEETKEELKATFPNTTKIITNEKFKRIANSFLQKN
Protein: Chaperonin 60 subunit alpha 1, chloroplastic (CPN-60 alpha 1) (Protein SCHLEPPERLESS) (RuBisCO large subunit-binding protein subunit alpha 1) (P21238)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds RuBisCO small and large subunits and is implicated in the assembly of the enzyme oligomer. Involved in protein assisted folding. Required for proper chloroplast development.
Subcellular location: Plastid, chloroplast.
Interaction partners:
- 20 kDa chaperonin, chloroplastic
- Heat shock protein 90-5, chloroplastic
- 10 kDa chaperonin 2, chloroplastic
- 10 kDa chaperonin 1
- Heat shock 70 kDa protein 6, chloroplastic
- Heat shock 70 kDa protein 4
- Heat shock 70 kDa protein 7, chloroplastic
- Chaperonin 60 subunit beta 1, chloroplastic
- Ribulose bisphosphate carboxylase large chain
- Heat shock 70 kDa protein 10, mitochondrial
Sequence:
MASANALSSASVLCSSRQSKLGGGNQQQGQRVSYNKRTIRRFSVRANVKEIAFDQHSRAALQAGIDKLADCVGLTLGPRGRNVVLDEFGSPKVVNDGVTIARAIELPNAMENAGAALIREVASKTNDSAGDGTTTASILAREIIKHGLLSVTSGANPVSLKRGIDKTVQGLIEELQKKARPVKGRDDIRAVASISAGNDDLIGSMIADAIDKVGPDGVLSIESSSSFETTVEVEEGMEIDRGYISPQFVTNPEKLLAEFENARVLITDQKITAIKDIIPILEKTTQLRAPLLIIAEDVTGEALATLVVNKLRGVLNVVAVKAPGFGERRKAMLQDIAILTGAEYLAMDMSLLVENATIDQLGIARKVTISKDSTTLIADAASKDELQARIAQLKKELFETDSVYDSEKLAERIAKLSGGVAVIKVGAATETELEDRKLRIEDAKNATFAAIEEGIVPGGGAALVHLSTVIPAIKETFEDADERLGADIVQKALLSPAALIAQNAGVEGEVVVEKIMFSDWENGYNAMTDTYENLFEAGVIDPAKVTRCALQNAASVAGMVLTTQAIVVDKPKPKAPAAAAPEGLMV
Protein: Trans-cinnamate 4-monooxygenase (EC 1.14.14.91) (Cinnamic acid 4-hydroxylase) (C4H) (CA4H) (Cinnamic acid 4-hydroxylase 1) (SbC4H1) (Cytochrome P450 73A33) (Cytochrome P450C4H) (Q94IP1)
Organism: Sorghum bicolor (Sorghum) (Sorghum vulgare)
Function: Catalyzes the first oxidative step of the phenylpropanoid pathway in higher plants by transforming trans-cinnamate into p-coumarate. The compounds formed by this pathway are essential components for lignification, pollination, and defense against ultraviolet light, predators and pathogens. Can also use 2-naphthoic acid as substrate.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Phenylalanine ammonia-lyase
- Phenylalanine ammonia-lyase
- Phenylalanine ammonia-lyase
- Phenylalanine ammonia-lyase
- Phenylalanine ammonia-lyase
- Phenylalanine ammonia-lyase
- Phenylalanine ammonia-lyase
- 4-coumarate--CoA ligase
- 4-coumarate--CoA ligase
- 4-coumarate--CoA ligase
Sequence:
MDLVLLEKALLGLFAAAVLAVAVAKLTGKRYRLPPGPAGAPVVGNWLQVGDDLNHRNLMSLAKRFGDIFLLRMGVRNLVVVSTPELAKEVLHTQGVEFGSRTRNVVFDIFTGKGQDMVFTVYGDHWRKMRRIMTVPFFTNKVVAQNRVGWEEEARLVVEDVRKDPRAAAEGVVIRRRLQLMMYNDMFRIMFDTRFESEQDPLFNKLKALNAERSRLSQSFEYNYGDFIPVLRPFLRGYLNRCHDLKTRRMKVFEDNFVQERKKVMAQTGEIRCAMDHILEAERKGEINHDNVLYIVENINVAAIETTLWSIEWGIAELVNHPAIQSKLREEMDSVLGAGVPVTEPDLERLPYLQAIVKETLRLRMAIPLLVPHMNLNDGKLAGYDIPAESKILVNAWFLANDPKRWVRPDEFRPERFLEEEKTVEAHGNDFRFVPFGVGRRSCPGIILALPIIGITLGRLVQNFQLLPPPGQDKIDTTEKPGQFSNQIAKHATIVCKPLEA