wanglab/gogpt-training-data huggingface dataset:
Protein: Phosphatidylinositol 4,5-bisphosphate-binding protein SLM2 (Synthetic lethal with MSS4 protein 2) (TORC2 effector protein SLM2) (P53955)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Together with SLM1, effector of the TORC2- and calcineurin-signaling pathways. Phosphorylated and activated by TORC2 under favorable growth conditions. Mediates actin polarization via inhibition of calcineurin-dependent transcription. Upon nutrient limitation or environmental stress, gets dephosphorylated by calcineurin, inhibiting interaction with TORC2, thereby antagonizing TORC2 signaling and mediating calcineurin-dependent actin depolarization. Also functions in heat-induced, calcineurin-mediated uracil permease (FUR4) endocytosis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15023338, ECO:0000269|PubMed:15372071, ECO:0000269|PubMed:15689497}; Peripheral membrane protein {ECO:0000269|PubMed:15023338, ECO:0000269|PubMed:15372071, ECO:0000269|PubMed:15689497}; Cytoplasmic side {ECO:0000269|PubMed:15023338, ECO:0000269|PubMed:15372071, ECO:0000269|PubMed:15689497}.
Interaction partners:
- Phosphatidylinositol 4,5-bisphosphate-binding protein SLM1
- Target of rapamycin complex 2 subunit TSC11
- Target of rapamycin complex 2 subunit AVO2
- Serine/threonine-protein kinase TOR2
- Large ribosomal subunit protein uL15m
- Target of rapamycin complex 2 subunit BIT61
- Large ribosomal subunit protein uL22m
Sequence:
MSYQRNSARASLDLRSQYQQLEGRMRSEHFNPAYQQQQQKGQNIPLSLPSSLAQRNPIPYPIDAVTSDPTIPAQLNVYDHDRQNSIVDAAAGTNTTHSLNSNNIPSSQNNNINNNNINNVGSFTDPSMLTLPKMSLHSHQKQYDSNQNDPRSPLAILIPTSAQPTDVLSARFSAWRNVIRAILVYLSETASIQDEIVRQQLRLSHAVQFPFFSIENQYQPVSNEDKSMQKFFLPLGSGSVQDLPTMLTKYHDNLASLASKSSKELTSEIIPRLEDLRRDLLVKIKEIKALQSDFKNSCNKELQQTKHLMKLFNESLKECKLGTPKSDPFLIKLQLEKQIKRQLVEENYLHEAFDNLQNSGAQLESVIVMEIQNGLTSYARILGKEAQVVFDSVISKLDSTILNKNTNLEWDSFILRNISNFVPPNLPMRRFKEISYSNQNDPFTFEVKSGFLEKRSKFLKSYSRGFYVLTPSFLHEFKTPDKHKFSTPLMSIPLVECTVTEHSKKTKSNSEQGKNKFILRTNSNGLIHRGHNWVFKVDSYDDMIEWFGNIKALSSLPNYDDKCKYVSKVAKLSKEKAKSNENTTESVTPQVTNEQHTRYDDVSSSNFPLNSIPKLDNLTITNTTSSIPETNDSQIQNRVPEFYIENVDSPRKSNQL
Protein: Midnolin (Midbrain nucleolar protein) (Q3TPJ7)
Organism: Mus musculus (Mouse)
Function: Facilitates ubiquitin-independent proteasomal degradation of polycomb protein CBX4. Plays a role in inhibiting the activity of glucokinase GCK and both glucose-induced and basal insulin secretion (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:10974535, ECO:0000269|PubMed:24187134}. Cytoplasm, cytosol {ECO:0000269|PubMed:24187134}. Nucleus, nucleolus {ECO:0000269|PubMed:10974535}. Note=Detected in the nucleus and nucleolus with no expression in the cytoplasm (PubMed:10974535). However, a later study finds expression in the nucleus and cytoplasm with no expression in the nucleolus (PubMed:24187134). {ECO:0000269|PubMed:10974535, ECO:0000269|PubMed:24187134}.
Interaction partners:
Sequence:
MEPQPGGARSCRRGAPGGACELNTATESAAPMSLAIHSTTGTRYDLSVPHDETVEGLRKRLSQRLKVPKERLALLHKDTRLSSGKLQEFGVGDGSKLTLVPTVEAGLMSQASRPEQSVMQALESLTETQVSDFLSGRSPLTLALRVGDHMMFVQLQLAAQHAPLQHRHVLAAAAAAAAAARGDSSVATPVSSPCRPVSSAARVPPVSSSPSSPVSPSPVTAGSFRSHAASTTCPEQMDCSPPASSSSTSTPGSSPTPRSRKPGAVIESFVNHAPGVFSGTFSGTLHPNCQDSSGRPRRDIGTILQILNDLLSATRHYQGMPPSLTQLRCHAQCSPASPAPDLTPKTTSCEKLAATSSTSLLQGQSQIRMCKPPGDRLRQTENRATRCKVERLQLLLQQKRLRRKARRDARGPYHWTPSRKAGRSDSSSSGGGGGPSEATGLGLDFEDSVWKPEVNPDIQSEFVVA
Protein: U8 snoRNA-decapping enzyme (EC 3.6.1.62) (IDP phosphatase) (IDPase) (EC 3.6.1.64) (Inosine diphosphate phosphatase) (Nucleoside diphosphate-linked moiety X motif 16) (Nudix motif 16) (U8 snoRNA-binding protein X29) (m7GpppN-mRNA hydrolase) (Q6TEC1)
Organism: Xenopus laevis (African clawed frog)
Function: RNA-binding and decapping enzyme that catalyzes the cleavage of the cap structure of snoRNAs and mRNAs in a metal-dependent manner. Part of the U8 snoRNP complex that is required for the accumulation of mature 5.8S and 28S rRNA. Has diphosphatase activity and removes m7G and/or m227G caps from U8 snoRNA and leaves a 5'monophosphate on the RNA. Catalyzes also the cleavage of the cap structure on mRNAs. Does not hydrolyze cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG). Also hydrolysis m7G- and m227G U3-capped RNAs but with less efficiencies. Has broad substrate specificity with manganese or cobalt as cofactor and can act on various RNA species. Binds to the U8 snoRNA; metal is not required for RNA-binding. May play a role in the regulation of snoRNAs and mRNAs degradation. Acts also as a phosphatase; hydrolyzes the non-canonical purine nucleotides inosine diphosphate (IDP) and deoxyinosine diphosphate (dITP) as well as guanosine diphosphate (GDP), deoxyguanosine diphosphate (dGDP), xanthine diphosphate (XDP), inosine triphosphate (ITP) and deoxyinosine triphosphate (ITP) to their respective monophosphate derivatives and does not distinguish between the deoxy- and ribose forms. The order of activity with different substrates is IDP > dIDP >> GDP = dGDP > XDP = ITP = dITP. Binds strongly to GTP, ITP and XTP. Participates in the hydrolysis of dIDP/IDP and probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions (By similarity).Exhibits decapping activity towards NAD-capped RNAs and FAD-capped RNAs (By similarity). Exhibits decapping activity towards dpCoA-capped RNAs in vitro (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:15053875}. Nucleus, nucleolus {ECO:0000269|PubMed:15053875}. Nucleus, nucleoplasm {ECO:0000269|PubMed:15053875}. Cytoplasm {ECO:0000250|UniProtKB:Q96DE0}. Note=Predominantly localized in nucleolus, and in a minor proportion in distinct foci in the nucleoplasm. {ECO:0000269|PubMed:15053875}.
Interaction partners:
Sequence:
MAESRSPDRGAKEDKPRPRNISREESLQLEGYKHACHALLHAPSQAKLFDRVPIRRVLLMMMRFDGRLGFPGGFVDTRDISLEEGLKRELEEELGPALATVEVTEDDYRSSQVREHPQKCVTHFYIKELKLEEIERIEAEAVNAKDHGLEVMGLIRVPLYTLRDRVGGLPAFLCNNFIGNSKSQLLYALRSLKLLREDQIQEVLKASHRLQY
Protein: RB transcriptional corepressor like 1 (H0YE05)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XIFLDIFQNPYEEPPKLPRSRKQRQDLLNPSFKGLPSDFHTADFTASEEPPCIIAVLCELHDGLLVEAKGIKEHYFKPYISKLFDRKILKGECLLDLSSFTDNSKAVNKEYEEYVLTVGDFDERIFLGADAEEEIGTPRKFTRDTPLGKLTAQANVEYNLQQHFEKKRSFAPSTPLTGRRYLREKEAVITPVASATQSVSRLQSIVAGLKNAPSDQLINIFESCVRNPVENIMKILKGIGETFCQHYTQSTDEQ
Protein: Phosphoenolpyruvate carboxykinase [GTP], mitochondrial (PEPCK-M) (EC 4.1.1.32) (P21642)
Organism: Gallus gallus (Chicken)
Function: Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle. Facilitates the recycling of lactate carbon in the liver.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q16822}.
Interaction partners:
- Lipoyl-binding domain-containing protein.
- Alpha-enolase
- Citrate synthase, mitochondrial
- Malate dehydrogenase, cytoplasmic
- ATP-citrate synthase
- Gamma-enolase
- Enolase 4
- Malate dehydrogenase
- Pyruvate kinase PKM
- Pyruvate dehydrogenase E1 component subunit beta
Sequence:
MFWLRGGAQSCRGGETEDRMQRGMWGVGLARRRLSTSLSALPAAARDFVEEAVRLCRPREVLLCDGSEEEGKELLRGLQDDGVLHPLPKYDNCWLARTDPRDVARVESKTVLVTPEQSDAVPPPPPSGGPPQLGNWMSPNAFQAAVQERFPGCMAGRPLYVIPFSMGPPTSPLAKLGVQVTDSPYVVLSMRIMTRVGPAVLQRLDDDFVRCLHSVGRPLPLTEPLVSSWPCDRSPVLVAHIPSERRIVSFGSGYGGNSLLGKKCFALRIASRMAQQQGWLAEHMLILGVTSPSGEKRYMAAAFPSACGKTNLAMMTPSLPGWRIHCVGDDIAWMKFDDEGRLRAINPERGFFGVAPGTSSRTNPNAMATIARNTIFTNVGLRSDGGVYWDGLDEPTEPGVTYTSWLGKPWKHGDPEPCAHPNSRFCAPADQCPIMDPRWDDPEGVPIDAIIFGGRRPRGVPLVVEAFGWRHGVFMGSAMRSEATAAAEHKGGRLMHDPFAMRPFFGYNAGRYLEHWLSTGLRSNARLPRLFHVNWFLRDNEGRFVWPGFGHNARVLAWIFGRIQGRDTARPTPIGWVPKEGDLDLGGLPGVDYSQLFPMEKGFWEEECRQLREYYGENFGADLPRDVMAELEGLEERVRKM
Protein: Superoxide dismutase (EC 1.15.1.1) (Q967T0)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MTFSIPPLPWGYDGLAAKGISKEQVTFHYDKHHMGYVTKLNAVAACNAAVAAKSVEEIIRTEKGPIFNLAAQIFNHDFYWESISPNGGGEPSGKLADAIADSFGSFARFKEEFTNAAVGHFGSGWAWLVQDTTTKKLKVFQTHDAGCPLTEADLKPILACDVWEHAYYIDYKNDRPAYVQTFWNEVNWAHAEEQLLKS
Protein: Coiled-coil and C2 domain-containing protein 1A (Five prime repressor element under dual repression-binding protein 1) (FRE under dual repression-binding protein 1) (Freud-1) (Q8K1A6)
Organism: Mus musculus (Mouse)
Function: Transcription factor that binds specifically to the DRE (dual repressor element) and represses HTR1A gene transcription in neuronal cells. The combination of calcium and ATP specifically inactivates the binding with FRE. May play a role in the altered regulation of HTR1A associated with anxiety and major depression. Mediates HDAC-independent repression of HTR1A promoter in neuronal cell. Performs essential function in controlling functional maturation of synapses.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q6P1N0}. Nucleus {ECO:0000250|UniProtKB:Q66HA5}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q6P1N0}.
Interaction partners:
- Deformed epidermal autoregulatory factor 1 homolog
Sequence:
MHKRNGPQAPPGRGAVTARQLGLLVDFSPDGLMIPEDGINEEELEAEFLALVGGQPQALEKLKGQGPLPMEAIEKMARLCMRDLDEDEEGTDEDDVEADEDLLAELNEVLGEEQKAVEPLMPVAQPKPSGPNPGVEATLQERLTLYQSALESARQAGDSAKMRRYDRGLKTLENLLVSAKKGNIINEADIPPPVASGKGAAAGHSHTQATSQLASVSPPAPESSGTLEAPSTTTPTSAKPQLPPDPCSPLARLQSLQHEYKLAALRAKHQDDTATATRHLRIAKSFDPVLEALSRGELVDLSRLPPPPDQLSPEPPLPAAQPLTSASTLTRPEVPQPPRNLLEALEQRMERYHVAAAQAKAKGDQRKARMHERIVKQYQDAIRAHKAGRAVDVAELPVPPGFPPMQGLESAEPSQQSLVGVLETAMRLANHDEGSDDEEEETPKKQNTPAASTTQLKSSPSKAPPSGPAPAGKAAPKGTSNRAQQQLAFLEGRKKQLLQAALRAKQKNDVEGAKMHLRQAKGLEPMLEASRNGLPVDIAKVPPAPVNKDDFVLVQRPGPGLSQEAVRRYGELTKLLRQQHEMCLNHSTQFTHLGNIAETIKFEKLAEDCKRSMDTLKQAFARSLPTPAARFEQRTFSVIKVFPDLSNSDMLLFIVKGINLPTPTGLSPSDLDAFVRFDFPYPNVEEAQKDKTSVIKNTDSPEFKEQFKLCINRGHRGFRRAIQTKGIKFEVVHKGGLFKTDRVLGTAQLKLGTLETACEVHEILEVLDGRRPTGGRLEVMVRIREPLTAQQLETTTERWLVIDHIPAAMPTVTGPKAKAPLIPASSREAGNRSARPLHSLSVLAFDQERLERKILALRQARRPVPPEVAQQYQDVVQRSQWQRAQLEQGGAALRREYASHLERQLHFYTEAARRLGYDGSREAAKEALYRRNLVESELQRLRR
Protein: MLO-like protein 9 (AtMlo9) (Q94KB4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in modulation of pathogen defense and leaf cell death. Activity seems to be regulated by Ca(2+)-dependent calmodulin binding and seems not to require heterotrimeric G proteins (By similarity).
Subcellular location: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Defensin-like protein 267
- Defensin-like protein 219
- At5g58530
- Protein CANDIDATE G-PROTEIN COUPLED RECEPTOR 7
- Protein disulfide isomerase-like 1-6
- Thioredoxin-like 1-3, chloroplastic
- Probable disease resistance protein At5g66910
Sequence:
MAGGGGGGGGEGPRQLDQTPTWAVSTVCGVIILISIILELIIHKVGEVFERKKKKALFEALEKIKNELMVLGFISLLLTFGQNYIASICVPSRYGHAMSFCGPYDGPSEDDRKKLKKTDHAMRILYSVQRRSLADAPPVNCKKDYVALISLNALHQVHIFIFFLAVFHVIYSAITMMLGRAKIRGWKVWEQEVIHEQEMMNDPSRFRLTHETSFVREHVNSWASNKFFFYVMCFFRQILRSVRKSDYLTMRHGFISVHLAPGMKFDFQKYIKRSLEDDFKVVVGIRPELWAFVMLFLLFDVHGWYVTAVITMIPPLLTLAIGTKLQAIISYMALEIQERHAVIQGMPVVNVSDQHFWFEKPDLVLHMIHFVLFQNAFEITYFFWIWYEFGLRSCFHHHFGLIIIRVCLGVGVQFLCSYITLPLYALVTQMGSTMKRSVFDEQTSKALEQWHKKARKKNEK
Protein: DNA topoisomerase 2-binding protein 1 (DNA topoisomerase II-binding protein 1) (A0A2R8RVN3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- CDC45 cell division cycle 45 homolog
- Tumor protein p53-binding protein, 1.
- DNA 5'-3' helicase
- ATR-interacting protein
- ATR serine/threonine kinase
- Mediator of DNA damage checkpoint 1.
- DNA helicase
- Cell cycle checkpoint protein RAD17
- Cell cycle checkpoint control protein
- BRCA1-associated RING domain 1.
Sequence:
MSKASKDAYIVKFVESNGQKSDVALQAYKAIVELQSEKYVQMVDEEAALELDHNDKSLFVFSDFTSSAFDHCRRLGCRIVSPLVVLFCLQKQRCVPKAEQPVYNMSMADVTVSCTNLDKEARSEVMDLIQLMGGRVYRDLNVSVTHLVAGEVGSKKYLVAASLGKPILLPSWVKACWEKSQDSVFHHSELNTEDYRCPVLKGCTVCVTGLSTVERKEVQRLCDQNGATYTGQLKMNECTHLIVNEPTGQKYEFARKWNVYCVSLHWLFDSIEKGFCQDESRYAVERGDKRKTDDKSGRPNTSTPTGQSRSKEDGPSLLGLSHISNISLNVNETALTTAGISHIEMPDPVDSFDITVCRVDDLLDGCKLYLCGLSGKKLEKLRRMVNTAGGLRFNQPTQELTHIVMGEADQGIKAFLDNATHRPHIVTVQWLLESFSRGSLLPENGYFHPSFLPPAPAAVDIPALHKAAPRASRPSVAPPPAPSPARQSRAEEDLLSQYMGNDQTVELPQDTSSRHSVLHPEPLVEGKDSTLAEASEGGLFFGKRFILVGFGAEAEAQLSELVMENAGKILVGRSRAVAHYAIVPLLGCDVEATVDEVATDTWLAMCVEQQCVLPLASHPLFTPVAVREGFSPLKDCVLSVSQFTGAERDSLIQLAKHLGASVQDYFVRTANQRKGMLASTHLVLQTPEGTKYQAAQKWGLPAVTIRWVLESARTGKRADEGQYLVDLPPSPERTEDSFVGASQKDPPPLRLHQRSPELPLLGPQNSDAITPLDTARFQSRSVRSAVRKLKQGEEEQAEVTTPGQEEAKGAQQKDSSLHLDTPSRFLSRDKLFGPSFNTKDVFDHLQTPGNKSQQGQGAETPLSEVIERNLKAAVANSNRSHVTNLAAMTASPQLGKEPEPEVEQKAAAPLSGVVVCVSKKLSKKQSELNAVAASLGAEFRWSCDDSVTHYIYQGKVGDNSKEYRAVKERGLYIVSQHWLQACADEQKHVSESLYPFTFNPKMSLTMSQMADSTQRSPPSATPRTRLRAFAENEETRLGPDDDITDVSTPKQGSVGEPEKDQTISTEKKNLTETLEMRESLQRQLQEIMSATKLTSGRRGSSRLAKTGPGGLDSPHTPDSLGRMSRRSRNLEAIRMSRQVCVDLNTEPSQSEQIVWDDPTAREERAKLADNLQWPGSPSQHSEPLALVPPPHSDHTTNGRDSMTDSELVEMAAFEVIDAQLKPKGTSSRVDTLHNPKTPEAPSIAFPISKTAALPLPRIEDEEEELKKDPPRFLLSSLNPQERIDYSHLIEELGGVVLEKQSFDPSCTHVIVGHPLRNEKYLAAMAAGKWILHRSYLEACRAEGHFIQEDQYEWGSSSILEALPSINSQQKRLALAAMRWRKTLQGCSNKEPNVIVVQGAFGGWIVMLNIDQAREAGFRRLLQSGGAKVLPDPSPSLFKETTHLFVDFSRLKPGDVRVDISEASAHGVKCLKPEYIADYLMQEPSPSMDAYYLPGAAADETEKVVDASSRKRKASGDMSTLKKSRMR
Protein: Retinol dehydrogenase 12 (EC 1.1.1.300) (All-trans and 9-cis retinol dehydrogenase) (Short chain dehydrogenase/reductase family 7C member 2) (Q96NR8)
Organism: Homo sapiens (Human)
Function: Retinoids dehydrogenase/reductase with a clear preference for NADP. Displays high activity towards 9-cis, 11-cis and all-trans-retinal. Shows very weak activity towards 13-cis-retinol. Also exhibits activity, albeit with lower affinity than for retinaldehydes, towards lipid peroxidation products (C9 aldehydes) such as 4-hydroxynonenal and trans-2-nonenal. May play an important function in photoreceptor cells to detoxify 4-hydroxynonenal and potentially other toxic aldehyde products resulting from lipid peroxidation. Has no dehydrogenase activity towards steroids.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15865448}.
Interaction partners:
- Lecithin retinol acyltransferase
- Retinaldehyde dehydrogenase 3
- Aldehyde dehydrogenase 1A1
- Retinal dehydrogenase 2
- Beta,beta-carotene 15,15'-dioxygenase
- Cytochrome P450 26A1
- Retinol dehydrogenase 5
- All-trans-retinol 13,14-reductase
- Retinoid isomerohydrolase
- Diacylglycerol O-acyltransferase 1
Sequence:
MLVTLGLLTSFFSFLYMVAPSIRKFFAGGVCRTNVQLPGKVVVITGANTGIGKETARELASRGARVYIACRDVLKGESAASEIRVDTKNSQVLVRKLDLSDTKSIRAFAEGFLAEEKQLHILINNAGVMMCPYSKTADGFETHLGVNHLGHFLLTYLLLERLKVSAPARVVNVSSVAHHIGKIPFHDLQSEKRYSRGFAYCHSKLANVLFTRELAKRLQGTGVTTYAVHPGVVRSELVRHSSLLCLLWRLFSPFVKTAREGAQTSLHCALAEGLEPLSGKYFSDCKRTWVSPRARNNKTAERLWNVSCELLGIRWE
Protein: Thylakoid lumenal 17.4 kDa protein, chloroplastic (P17.4) (P81760)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast thylakoid lumen {ECO:0000269|PubMed:11719511, ECO:0000269|PubMed:18431481}.
Interaction partners:
- Peptidyl-prolyl cis-trans isomerase CYP38, chloroplastic
- Peptidyl-prolyl cis-trans isomerase FKBP13, chloroplastic
- Thylakoid lumenal 15 kDa protein 1, chloroplastic
- Oxygen-evolving enhancer protein 1-2, chloroplastic
- Peptidyl-prolyl cis-trans isomerase FKBP20-2, chloroplastic
- UPF0603 protein At1g54780, chloroplastic
- PsbP domain-containing protein 4, chloroplastic
- PsbP domain-containing protein 5, chloroplastic
- At2g23670/F26B6.32
- Protease Do-like 5, chloroplastic
Sequence:
MASLPVQFTRNQISSPFFSVNLRREPRSLVTVHCSAGENRENGEGVKKSLFPLKELGSIACAALCACTLTIASPVIAANQRLPPLSTEPDRCEKAFVGNTIGQANGVYDKPLDLRFCDYTNDQTNLKGKTLSAALMVGAKFDGADMTEVVMSKAYAVEASFKGVNFTNAVIDRVNFGKSNLKGAVFRNTVLSGSTFEEANLEDVVFEDTIIGYIDLQKICRNESINEEGRLVLGCR
Protein: Spermatogenesis-associated protein 22 (S6C2T2)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MKRNLNESSTRSTAGCLPVPLFNQKKRNRQPLTSNPLQSDPGIGTVSDSYGFPSLPTDWAWEAVNPVVAPLKKTVNTGQIPASASYPLRIEDPVCKSIESNAKRSQGGGGYRGNNRNTSSRTWDRNDFRPQHKTVSPAANSEFSSGPVNLGAQRQKQFQTPEFPNLPGHKEAEVPRQTYLSKLPGSTMKGPDRASALQAFKPSFQQNPFNKTVLGDVPRENSLKETTLYQLKEKDNSLRIISAVIESMKYWQAQVKKTVLLFEVLAVLDSAVTPGPHYSKTFLMRDGKNILPCVFYEIDRELPRLIRGRVHRCVGHYDPHKNIFKCVSVRPASASEQKTFQAFVTIVDAEMKYHTKVMNEM
Protein: RNA exonuclease 4 (EC 3.1.-.-) (Q08237)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Exoribonuclease involved in ribosome biosynthesis. Involved in the processing of ITS1, the internal transcribed spacer localized between the 18S and 5.8S rRNAs.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Ribosome biogenesis protein NOP53
- Nucleolar protein 16
- Ribosome biogenesis protein SSF1
- Ribosome biogenesis protein MAK21
- ATP-dependent RNA helicase DBP3
- ATP-dependent rRNA helicase SPB4
- Nucleolar protein 12
- Ribosome biogenesis protein RLP7
- Nucleolar protein 4
- Suppressor protein SRP40
Sequence:
MALSSNWQALLASESNPTSNGKNKQSNRKIRNVKKVSKTVNVSSTTQYAPRKRKNGSKIMDMVYNMNKEISKHEKDKLEGKVFEFNPNKANTSTTIKEPVKVGISEDTRINSNKSKEIGKYIAMDCEFVGVGPEGKESALARISIVNYFGHVVLDEFVKPREKVVEWRTWVSGIKPEHMKNAITFKEAQKKTADILEGRILVGHALKHDLEALMLSHPKSLLRDTSRHLPFRKLYAKGKTPSLKKLTREVLKISIQEGEHSSVEDARATMLLYKKEKTEFEKIHRNTFN
Protein: Protein FIP1 (FRIGIDA-interacting protein 1) (Q8S8K9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Pentatricopeptide repeat-containing protein At2g06000
- Probable LRR receptor-like serine/threonine-protein kinase RFK1
- Polyadenylate-binding protein 1
- Pre-mRNA cleavage factor Im 25 kDa subunit 1
- Cleavage stimulation factor subunit 77
- Formin-like protein 18
Sequence:
MSTERRASSNPMTNEENAMFLDILHEAPLFGHRKSRSLVGSYLYMLLLAGYAILAAGAPWMFHRVQQLTPSLLCCCDVALLVVTGVFQQYFVYQVQKIRLQGYYSFSQKLKHVVRLPFAIAAYGTAAMLLVIVWRPQIHILSISSLQRIIMLVEAVGAGFFMGLYIGYVHQYNSVNSRPDVLKSLYSPLQPSSSMEGLRYYEGRLSDQQTALLQYQRENLHFLSEEILCLQEKLSKYEQSDDGSTPQVDLAHLLAARDQELRTLSAEMNQLQSELRLARSLIAERDAEVQRVNSTNNQYIEENERLRAILSEWSMRAANLERALEVERMSNSELQKEVASTRRKQMLETTTSEQP
Protein: Olfactory receptor 52A1 (HPFH1OR) (Odorant receptor HOR3'beta4) (Olfactory receptor OR11-319) (Q9UKL2)
Organism: Homo sapiens (Human)
Function: Odorant receptor.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
Sequence:
MSISNITVYMPSVLTLVGIPGLESVQCWIGIPFCAIYLIAMIGNSLLLSIIKSERSLHEPLYIFLGMLGATDIALASSIMPKMLGIFWFNVPEIYFDSCLLQMWFIHTLQGIESGILVAMALDRYVAICYPLRHANIFTHQLVIQIGTMVVLRAAILVAPCLVLIKCRFQFYHTTVISHSYCEHMAIVKLAAANVQVNKIYGLFVAFTVAGFDLTFITLSYIQIFITVFRLPQKEARFKAFNTCIAHICVFLQFYLLAFFSFFTHRFGSHISPYIHILFSSIYLLVPPFLNPLVYGAKTTQIRIHVVKMFCS
Protein: Heat shock protein beta-1 (Heat shock 27 kDa protein) (A4VAK4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm, cytoskeleton, spindle {ECO:0000256|ARBA:ARBA00004186}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- non-specific serine/threonine protein kinase
- Heat shock cognate 71 kDa protein
- non-specific serine/threonine protein kinase
- MAPK-activated protein kinase 3
- MAP kinase-activated protein kinase 5
- Heat shock cognate 71 kDa protein
- Heat shock protein HSP 90-alpha 1
- Heat shock cognate 71 kDa protein
- BCL2-associated athanogene 3.
- Cytochrome c
Sequence:
MAERRIPFSFMRSPSWDPFRDWYQGSRLFDQSFGMPALSEEMLTFPSTHWPGYMRPFGHPEFASLMQGPPVMPPMMTPSYGRALSRQLSSGMSEVKQTGDSWKISLDVNHFSPEELNVKTKDGVLEITGKHEERKDEHGFISRCFTRKYTLPPGVDSEKISSCLSPEGVLTVEAPLPKPAIQAPEVNIPVNKTTVSTTK
Protein: Ezrin (Cytovillin) (Villin-2) (p81) (P31977)
Organism: Rattus norvegicus (Rat)
Function: Probably involved in connections of major cytoskeletal structures to the plasma membrane. In epithelial cells, required for the formation of microvilli and membrane ruffles on the apical pole. Along with PLEKHG6, required for normal macropinocytosis (By similarity).
Subcellular location: Apical cell membrane {ECO:0000250|UniProtKB:P15311}; Peripheral membrane protein {ECO:0000250|UniProtKB:P15311}; Cytoplasmic side {ECO:0000250|UniProtKB:P15311}. Cell projection {ECO:0000250|UniProtKB:P15311}. Cell projection, microvillus membrane {ECO:0000250|UniProtKB:P15311}; Peripheral membrane protein {ECO:0000250|UniProtKB:P15311}; Cytoplasmic side {ECO:0000250|UniProtKB:P15311}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:P15311}; Peripheral membrane protein {ECO:0000250|UniProtKB:P15311}; Cytoplasmic side {ECO:0000250|UniProtKB:P15311}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:P15311}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P15311}. Cell projection, microvillus {ECO:0000250|UniProtKB:P26040}. Note=Localization to the apical membrane of parietal cells depends on the interaction with PALS1. Microvillar peripheral membrane protein (cytoplasmic side) (By similarity). Localizes to cell extensions and peripheral processes of astrocytes. Colocalizes with EZR and NHERF2 at the apical cell membrane of glomerular epithelium cells. {ECO:0000250|UniProtKB:P15311, ECO:0000269|PubMed:11457882, ECO:0000269|PubMed:15797715}.
Interaction partners:
- Na
- Radixin
- Moesin
- Intercellular adhesion molecule 1
- CD44 antigen
- Sodium/hydrogen exchanger 1
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit alpha
- Vascular cell adhesion protein 1
- Na
Sequence:
MPKPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLQYVDNKGFPTWLKLDKKVSAQEVRKENPVQFKFRAKFYPEDVADELIQDITQKLFFLQVKEGILSDEIYCPPETAVLLGSYAVQAKFGDYNKEMHKSGYLSSERLIPQRVMDQHKLSRDQWEDRIQVWHAEHRGMLKDSAMLEYLKIAQDLEMYGINYFEIKNKKGTDLWLGVDALGLNIYEKDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILQLCMGNHELYMRRRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMLREKEELMLRLQDFEQKTKRAEKELSEQIEKALQLEEERRRAQEEAERLEADRMAALRAKEELERQAQDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQDDLVKTKEELHLVMTAPPPPPPPVYEPVNYHVQEGLQDEGAEPMGYSAELSSEGILDDRNEEKRITEAEKNERVQRQLLTLSNELSQARDENKRTHNDIIHNENMRQGRDKYKTLRQIRQGNTKQRIDEFEAM
Protein: Primary amine oxidase (EC 1.4.3.21) (2-phenylethylamine oxidase) (Copper amine oxidase) (Tyramine oxidase) (P46883)
Organism: Escherichia coli (strain K12)
Function: The enzyme prefers aromatic over aliphatic amines.
Subcellular location: Periplasm.
Interaction partners:
- Phenylacetaldehyde dehydrogenase
- Transcriptional activator FeaR
- Putrescine aminotransferase
- Protein/nucleic acid deglycase 1
- Bifunctional protein PaaZ
- Lactoylglutathione lyase
- Lactaldehyde dehydrogenase
- Glyoxylate/hydroxypyruvate reductase B
- Glyoxylate/hydroxypyruvate reductase A
Sequence:
MGSPSLYSARKTTLALAVALSFAWQAPVFAHGGEAHMVPMDKTLKEFGADVQWDDYAQLFTLIKDGAYVKVKPGAQTAIVNGQPLALQVPVVMKDNKAWVSDTFINDVFQSGLDQTFQVEKRPHPLNALTADEIKQAVEIVKASADFKPNTRFTEISLLPPDKEAVWAFALENKPVDQPRKADVIMLDGKHIIEAVVDLQNNKLLSWQPIKDAHGMVLLDDFASVQNIINNSEEFAAAVKKRGITDAKKVITTPLTVGYFDGKDGLKQDARLLKVISYLDVGDGNYWAHPIENLVAVVDLEQKKIVKIEEGPVVPVPMTARPFDGRDRVAPAVKPMQIIEPEGKNYTITGDMIHWRNWDFHLSMNSRVGPMISTVTYNDNGTKRKVMYEGSLGGMIVPYGDPDIGWYFKAYLDSGDYGMGTLTSPIARGKDAPSNAVLLNETIADYTGVPMEIPRAIAVFERYAGPEYKHQEMGQPNVSTERRELVVRWISTVGNYDYIFDWIFHENGTIGIDAGATGIEAVKGVKAKTMHDETAKDDTRYGTLIDHNIVGTTHQHIYNFRLDLDVDGENNSLVAMDPVVKPNTAGGPRTSTMQVNQYNIGNEQDAAQKFDPGTIRLLSNPNKENRMGNPVSYQIIPYAGGTHPVAKGAQFAPDEWIYHRLSFMDKQLWVTRYHPGERFPEGKYPNRSTHDTGLGQYSKDNESLDNTDAVVWMTTGTTHVARAEEWPIMPTEWVHTLLKPWNFFDETPTLGALKKDK
Protein: Prolactin releasing hormone (G3UWC3)
Organism: Mus musculus (Mouse)
Interaction partners:
- Prolactin-releasing peptide receptor
- Pro-FMRFamide-related neuropeptide FF
- Pro-FMRFamide-related neuropeptide VF
- Neuropeptide FF receptor 1
- Orexigenic neuropeptide QRFP
Sequence:
MAPRTWLLCLLLLGLVLPGASSRAHQHSMETRTPDINPAWYTGRGIRPVGRFGRRRAALRDVTGPGLRCRLSCFPLDGSAKFSHSS
Protein: Skn-1 dependent zygotic transcript 1 protein (P34259)
Organism: Caenorhabditis elegans
Function: May have a role in mesendoderm development during embryogenesis.
Interaction partners:
- MX region of TRA-2 Related
- Uncharacterized protein
- Conserved secreted protein
- Uncharacterized protein
Sequence:
MLRYIFFAAILFFVFPNTESAGFLKFELTADRDCLLHLEHSSTYSETVRLLAYESRPLEIYTQGSINEIPVHFQLLHHFSGKALSEAKFQIFQLKNNGLWDSKVIDTDKVILSVRSTFYCENGYFGPICDRRSRTFAPKSDIQTSTPGYQTQVLKFDFKISDDIIIYSSLAFFVLLLIIFNCILCCYRPKKSQKYLDVSLGSPKVFSICGYSADKSGNTTEYLDAPSRFFSSTKIECVV