wanglab/gogpt-training-data huggingface dataset:
Protein: receptor protein-tyrosine kinase (EC 2.7.10.1) (Q9ESE0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MRPSGTARTTLLVLLTALCAAGGALEEKKVCQGTSNRLTQLGTFEDHFLSLQRMYNNCEVVLGNLEITYVQRNYDLSFLKTIQEVAGYFLIALNTVERIPSEDLQIIRGNALYENTYALAILSNYGTNRTGLRELPMRNLQEILIGAVRFSNNPILCNMDTIQWRDIVQNVFMSNMSMDLQSHPSSCPKCDPSCPNGSCWGGGEENCQKLTKIICAQQCSHRCRGRSPSDCCHNQCAAGCTGPQKSDCLVCQKFQDEATCKDTCPPLMLYNPTTYQMDVNPEGKYSFGATCVKNCPRNYVVTDHGSCVRACGPDYYEVEEDGIRKCKKCDGPCRKVCNGIGIGEFKDTLSINATNIKHFKYCTAISGDLHILPVAFKGDSFTRTPPLDPRELEILKTVKEITGSLLIQAWPENWTDLHAFENLEIIRGRTKQHGQFSLAVVGLNITSLPWQVPSLSWQAVTRPLHPLAQNRVSWDTGP
Protein: Farnesyl pyrophosphate synthase vrtD (FPP synthase) (FPS) (EC 2.5.1.10) ((2E,6E)-farnesyl diphosphate synthase) (Dimethylallyltranstransferase) (EC 2.5.1.1) (Farnesyl diphosphate synthase) (Viridicatumtoxin synthesis protein D) (D7PHZ5)
Organism: Penicillium aethiopicum
Function: Farnesyl pyrophosphate synthase; part of the gene cluster that mediates the biosynthesis of viridicatumtoxin, a tetracycline-like fungal meroterpenoid with a unique, fused spirobicyclic ring system. The first step of the pathway is the production of the malonamoyl-CoA starter unit for the polyketide synthase vrtA. The aldolase vrtJ may be involved in the synthesis of the malonamate substrate for malonamoyl-CoA synthetase vrtB. The polyketide synthase vrtA then may utilize the malonamoyl-CoA starter unit, followed by sequential condensation of eight malonyl-CoA units to form the polyketide backbone. The cyclization of the last ring could be mediated by the lactamase-like protein vrtG. The proposed post-PKS tailoring steps are an hydroxylation at C5 catalyzed the cytochrome P450 monooxygenase vrtE, a hydroxylation at C12a catalyzed by VrtH and/or VrtI, and an O-methylation by the O-methyltransferase vrtF. VrtC is then proposed to catalyze the transfer of a geranyl group synthesized by vrtD to the aromatic C ring of the tetracyclic polyketide intermediate of viridicatumtoxin to yield previridicatumtoxin. Finally, the cytochrome P450 monooxygenase vrtK catalyzes the spirocyclization of the geranyl moiety of previridicatumtoxin to afford viridicatumtoxin.
Interaction partners:
Sequence:
MATSTTTSLKEFLSVFPQLVADLRALCLEEYQLPACVWDRFESTLNHNTLGGKCNRGLSVIDSVRLLRDGLELSPAEYFDAAVLGWLVELLQATMLVLDDIMDGSPTRRGKPSWYRVPGVGMAAVNDATMLESAIYMLLKKYFAGRAIYLPVVDLFHETALQIELGQAFDMLIANEGTPDLTTFVPATYSQIVTYKTAFYSFYLPVALALHAVDAATPTNLAAARAILVPMGEYFQVQDDYLDCFADPTVLGKVGTDIIEGKCSWLVVQALQRASTDQAQLLAENYGSASGESSVKALYSELDLESVYRTFEEQRVAELRTLITGLDESQGLRKSVFEELLGKIYQRRK
Protein: PH-sensitive chloride channel 1, isoform M (M9PFL8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MGCVFEAAKEQPHKPRSRQLRRNQCRGKAEKAAAGTRGKVAVRGNNDKPAEDIKIKDNYQQNHKTQTETQTEVAAVVAIATDAGAETETETEAEAQKEPATGPEHLKAAAQVLLTIRQARQENNKHSSSQVAETHKDEGEDALARQGSIVDTAAGRIGIDIAATTIQVAERHEDGQHWQQHNVRRRRRQPDPAAHPASITKLSAISLHFHALAALAKTLQKHEDLSPVQDRQPLAYRAWQEHPYAETQMPATMSAAIIANVGATAAATSAAAFQYLGQHYKHYSQSISFYAASSVLLMLCYLTTASTAAATQSETGALDKHPIFDESSSDKEILDLLLEKKRYDKRLLPPVNDEDFCCGLQSPDMATNQNARRPHNRGTLTVNVNVLLLSLASPDESSLKYEVEFLLNQQWNDPRLQYGNKSHYDFLNALHHHDSIWTPDTYFIMHGDFKDPIIPMHFALRIFRNGTITYAMRRHLILSCQGSLHIFPFDDPKCSFSMESISYEEAQIKYVWKNDEDTLRKSPSLTTLNAYLIKNQTTACDQNSWRGNYSCLQVELTFTRDRAYYFTTVFIPGIILVTSSFITFWLEWNAVPARVMIGVTTMLNFFTTSNGFRSTLPVVSNLTAMNVWDGVCMCFIYASLLEFVCVNYVGRKRPLHNVVYRPGENPVTQASAAATPAMSMMGGATPMSSGTPAASSSVATPGTPRITDPEEFFGGGMRWQEAHGGIIGAAVQNLRARSIKRKAARSPSTSISPHPSGRPTEHIYEEPGGSTSGVTSTKVKFKDELKEEQPEEAESSTKLRRSVATSTPALVVRIEAEIDPEAEDKPIQDMEMTERQLSLPLKPPRRKASRSNSPASVYSDAFENVEATPGEKRQNAGAPNEIVACTTCGGSNSPCTHSANNGCATETCFVQVRKKEPPHPIRVAKTIDVIARITFPTAYAIFLIFFFVHYKGFS
Protein: Protein arginine N-methyltransferase 3 (EC 2.1.1.319) (Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 3) (O70467)
Organism: Rattus norvegicus (Rat)
Function: Protein-arginine N-methyltransferase that catalyzes both the monomethylation and asymmetric dimethylation of the guanidino nitrogens of arginine residues in target proteins, and therefore falls into the group of type I methyltransferases. May regulate retinoic acid synthesis and signaling by inhibiting ALDH1A1 retinal dehydrogenase activity (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:9642256}. Nucleus {ECO:0000250|UniProtKB:O60678}.
Interaction partners:
- Protein arginine N-methyltransferase 5
- Protein arginine N-methyltransferase 1
- Small ribosomal subunit protein uS5
- Programmed cell death 2-like
- Small ribosomal subunit protein uS5
- 40S ribosomal protein S2
- Histone-lysine N-methyltransferase SETD7
Sequence:
MCSLAAGNGQGAELGPEPLELSDSGDDAGWEDEDADAEPAQGRQHTPCLFCDRLFRSAEETFSHCKLEHQFNIDGMVHKHGLEFYGYIKLINFIRLKNPTVEYMNSIYNPVPWDKDEYLKPVLEDDLLLQFDVEDLYEPVSAPFTYPNGLSENTSAVEKLKLMEARALSAEAALARAREDLQKMKQFAQDFVMNVDVRTCSSTTTIADLQEDEDGVYFSSYGHYGIHEEMLKDKVRTESYRDFIYQNPHIFKDKVVLDVGCGTGILSMFAAKAGAKKVIAVDQSEILYQAMDIIRLNKLEDTIVLIKGKIEEVSLPVEKVDVIISEWMGYFLLFESMLDSVLYAKSKYLAKGGSVYPDICTISLVAVSDVSKHADRIAFWDDVYGFNMSCMKKAVIPEAVVEVVDHKTLISDPCDIKHIDCHTTSISDLEFSSDFTLRTTKTAMCTAVAGYFDIYFEKNCHNRVVFSTGPQSTKTHWKQTIFLLEKPFPVKAGEALKGKITVHKNKKDPRSLIVTLTLNSSTQTYSLQ
Protein: Protein-L-isoaspartate O-methyltransferase (PIMT) (EC 2.1.1.77) (L-isoaspartyl protein carboxyl methyltransferase) (Protein L-isoaspartyl methyltransferase) (Protein-beta-aspartate methyltransferase) (Q27873)
Organism: Caenorhabditis elegans
Function: Initiates the repair of damaged proteins by catalyzing methyl esterification of L-isoaspartyl and D-aspartyl residues produced by spontaneous isomerization and racemization of L-aspartyl and L-asparaginyl residues in aging peptides and proteins.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P22061}.
Interaction partners:
- Protein yippee-like B0546.4
Sequence:
MAWRSSGSTNSELIDNLRNNRVFASQRAYDAMKSVDRGDFAPRAPYEDAPQRIGYNATVSAPHMHAAALDYLQNHLVAGAKALDVGSGSGYLTVCMAMMVGRNGTVVGIEHMPQLVELSEKNIRKHHSEQLERGNVIIIEGDGRQGFAEKAPYNAIHVGAASKGVPKALTDQLAEGGRMMIPVEQVDGNQVFMQIDKINGKIEQKIVEHVIYVPLTSREEQWNRN
Protein: Paired box protein Pax-6 (E9PKM0)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MQNSHSGVNQLGGVFVNGRPLPDSTRQKIVELAHSGARPCDISRILQVSNGCVSKILGRYYETGSIRPRAIGGSKPRVATPEVVSKIAQYKRECPSIFAWEIRDRLLSEGVCTNDNIPSVSSINRVLRNLASEKQQMGADGMYDKLRMLNGQTGSWGTRPGWYPGTSVPGQPTQDGCQQQEGGGENTNSISSNGEDSDEAQMRLQLKRKLQRNRTSFTQEQIEALEKEFERTHYPDVFARERLAAKIDLPEARIQVWFSNRRAKWRREEKLRNQRRQASNTPSHIPISSSFSTSVYQPIPQPTTPVSSFTSGSMLGRTDTALTNTYSALPPMPSFTMANNLPMQPPVPSQTSSYSCMLPTSPSVNGRSYDTYTPPHMQTHMNSQPMGTSGTTSTGLISPGVSVPVQVPGSEPDMSQY
Protein: RAB33A, member RAS oncogene family (Ras-related protein Rab-33A) (Zgc:153710) (Q0P3Y1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00037868}; Lipid-anchor {ECO:0000256|ARBA:ARBA00037868}.
Interaction partners:
- TBC1 domain family member 25
- RAB33B, member RAS oncogene family a
- Rab proteins geranylgeranyltransferase component A
- WD repeat domain 41
Sequence:
MANEFSENRDGTANSRHANLTSSLDLSTSLDHSVQTRIFKIIVIGDSNVGKTCLTFRFTGGAFPCKTEATIGVDFREKAVEIEGEKIKVQVWDTAGQERFRKSMVEHYYRNVHAVVFVYDVTKMASFQNLKTWIQECNGHGVSSAVPRVLVGNKCDLVDQIQVPSNTALKFADAYNMLLFETSAKDPKESQNVDSIFMCLACRLKAQKSLIYRDVEREDGRVRLTHQPDPKSNCPC
Protein: Putative cystathionine beta-lyase (CBL) (EC 4.4.1.13) (Beta-cystathionase) (Cysteine lyase) (Cysteine-S-conjugate beta-lyase) (Increased recombination centers protein 7) (P43623)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Cystathionine beta-synthase
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
- Putative mitochondrial cysteine synthase
- Homocysteine/cysteine synthase
- Putative cystathionine gamma-synthase YML082W
- Homocysteine S-methyltransferase 2
- Homocysteine S-methyltransferase 1
- Thiosulfate sulfurtransferase TUM1
- Regulation of enolase protein 1
- Adenosylhomocysteinase
Sequence:
MIDRTELSKFGITTQLSVIGRNPDEQSGFVNPPLYKGSTIILKKLSDLEQRKGRFYGTAGSPTIDNLENAWTHLTGGAGTVLSASGLGSISLALLALSKAGDHILMTDSVYVPTRMLCDGLLAKFGVETDYYDPSIGKDIEKLVKPNTTVIFLESPGSGTMEVQDIPALVSVAKKHGIKTILDNTWATPLFFDAHAHGIDISVEAGTKYLGGHSDLLIGLASANEECWPLLRSTYDAMAMLPGAEDCQLALRGMRTLHLRLKEVERKALDLAAWLGNRDEVEKVLHPAFEDCPGHEYWVRDYKGSSGLFSIVLKNGFTRAGLEKMVEGMKVLQLGFSWGG
Protein: Multidrug transporter MdfA (Chloramphenicol resistance pump Cmr) (P0AEY8)
Organism: Escherichia coli (strain K12)
Function: Efflux pump driven by the proton motive force. Confers resistance to a broad spectrum of chemically unrelated drugs. Confers resistance to a diverse group of cationic or zwitterionic lipophilic compounds such as ethidium bromide, tetraphenylphosphonium, rhodamine, daunomycin, benzalkonium, rifampicin, tetracycline, puromycin, and to chemically unrelated, clinically important antibiotics such as chloramphenicol, erythromycin, and certain aminoglycosides and fluoroquinolones. Overexpression results in isopropyl-beta-D-thiogalactopyranoside (IPTG) exclusion and spectinomycin sensitivity. Transport of neutral substrates is electrogenic, whereas transport of cationic substrates is electroneutral. In addition to its role in multidrug resistance, confers extreme alkaline pH resistance, allowing the growth under conditions that are close to those used normally by alkaliphiles. This activity requires Na(+) or K(+).
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Small ribosomal subunit protein uS12
- Multidrug resistance protein MdtK
- Multidrug export protein EmrB
- Outer membrane protein TolC
- DNA gyrase subunit A
- Beta-galactosidase
- Guanidinium exporter
- Cyclic di-GMP phosphodiesterase PdeR
- Beta-lactamase
- Probable aminoglycoside efflux pump
Sequence:
MQNKLASGARLGRQALLFPLCLVLYEFSTYIGNDMIQPGMLAVVEQYQAGIDWVPTSMTAYLAGGMFLQWLLGPLSDRIGRRPVMLAGVVWFIVTCLAILLAQNIEQFTLLRFLQGISLCFIGAVGYAAIQESFEEAVCIKITALMANVALIAPLLGPLVGAAWIHVLPWEGMFVLFAALAAISFFGLQRAMPETATRIGEKLSLKELGRDYKLVLKNGRFVAGALALGFVSLPLLAWIAQSPIIIITGEQLSSYEYGLLQVPIFGALIAGNLLLARLTSRRTVRSLIIMGGWPIMIGLLVAAAATVISSHAYLWMTAGLSIYAFGIGLANAGLVRLTLFASDMSKGTVSAAMGMLQMLIFTVGIEISKHAWLNGGNGLFNLFNLVNGILWLSLMVIFLKDKQMGNSHEG
Protein: Putative succinate-semialdehyde dehydrogenase [NADP(+)] 2 (SSADH 2) (SSDH 2) (EC 1.2.1.79) (P9WNX7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. Although it has succinate semialdehyde dehydrogenase activity, is likely to act physiologically on a different aldehyde(s). NAD(+) can substitute for NADP(+), but enzymatic activity is three times reduced.
Interaction partners:
- 4-aminobutyrate aminotransferase
- Succinate dehydrogenase flavoprotein subunit
- Probable succinate dehydrogenase [iron-sulfur subunit]
- Succinate-semialdehyde dehydrogenase [NADP
- succinate dehydrogenase
- Probable succinate dehydrogenase [iron-sulfur subunit]
- Probable succinate dehydrogenase SdhD
- Succinate dehydrogenase 2 membrane subunit SdhC
- 2-methylcitrate synthase
- Citrate synthase 1
Sequence:
MPAPSAEVFDRLRNLAAIKDVAARPTRTIDEVFTGKPLTTIPVGTAADVEAAFAEARAAQTDWAKRPVIERAAVIRRYRDLVIENREFLMDLLQAEAGKARWAAQEEIVDLIANANYYARVCVDLLKPRKAQPLLPGIGKTTVCYQPKGVVGVISPWNYPMTLTVSDSVPALVAGNAVVLKPDSQTPYCALACAELLYRAGLPRALYAIVPGPGSVVGTAITDNCDYLMFTGSSATGSRLAEHAGRRLIGFSAELGGKNPMIVARGANLDKVAKAATRACFSNAGQLCISIERIYVEKDIAEEFTRKFGDAVRNMKLGTAYDFSVDMGSLISEAQLKTVSGHVDDATAKGAKVIAGGKARPDIGPLFYEPTVLTNVAPEMECAANETFGPVVSIYPVADVDEAVEKANDTDYGLNASVWAGSTAEGQRIAARLRSGTVNVDEGYAFAWGSLSAPMGGMGLSGVGRRHGPEGLLKYTESQTIATARVFNLDPPFGIPATVWQKSLLPIVRTVMKLPGRR
Protein: Bifunctional nuclease 1 (AtBBD1) (EC 3.1.-.-) (Q9FWS6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Bifunctional nuclease with both RNase and DNase activities. Involved in basal defense response. Participates in abscisic acid-derived callose deposition following infection by a necrotrophic pathogen.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Endonuclease 1
- At2g01260
- Ribonuclease 3
- Metacaspase-9
- Endonuclease 4
- Cysteine protease XCP1
- NAC domain-containing protein 92
- Cysteine protease XCP2
- Protein SOMBRERO
- Endonuclease 2
Sequence:
MRSVQAPVVCPAIRPRQVGACASLVNYTGLKPRSQFWGNRTKGVKSQGTTTTITLRLCNKSIKCVFSSHSDGNGSTAENFNENDEEYVNSSVVEAVEVKSGADGFMVKMRDGRQLRCVHNNPQGGHLPDYAPHPAIVLKMEDGTGLLLPIIVLEMPSVLLMAAMTNVQIARPTMYQVVKEMVDKMGYEVRLVRVTKRVHEAYFAQLFLSKVGNASECVSFDLRPSDAINIAVRCKIPIQVNKYLAYSDGMRVIESGKISTPAPASDGLLFTEQDRPNGQACLDTKEFNILSKMMQAVDEERYDEAAEWRDKLGQFRAKRNLRKYT
Protein: FLYWCH-type zinc finger-containing protein 1 (Q4VC44)
Organism: Homo sapiens (Human)
Function: Transcription cofactor. Negatively regulates transcription activation by catenin beta-1 CTNNB1, perhaps acting by competing with TCF4 for CTNNB1 binding. May play a role in DNA-damage response signaling. Binds specifically to DNA sequences at peri-centromeric chromatin loci.
Subcellular location: Nucleus {ECO:0000269|PubMed:33924684}. Chromosome, centromere {ECO:0000269|PubMed:34408139}. Note=Localized to peri-centromeric, H3K9me3-marked heterochromatin. {ECO:0000269|PubMed:34408139}.
Interaction partners:
Sequence:
MPLPEPSEQEGESVKAGQEPSPKPGTDVIPAAPRKPREFSKLVLLTASDQDEDGVGSKPQEVHCVLSLEMAGPATLASTLQILPVEEQGGVVQPALEMPEQKCSKLDAAAPQSLEFLRTPFGGRLLVLESFLYKQEKAVGDKVYWKCRQHAELGCRGRAITRGLRATVMRGHCHAPDEQGLEARRQREKLPSLALPEGLGEPQGPEGPGGRVEEPLEGVGPWQCPEEPEPTPGLVLSKPALEEEEAPRALSLLSLPPKKRSILGLGQARPLEFLRTCYGGSFLVHESFLYKREKAVGDKVYWTCRDHALHGCRSRAITQGQRVTVMRGHCHQPDMEGLEARRQQEKAVETLQAGQDGPGSQVDTLLRGVDSLLYRRGPGPLTLTRPRPRKRAKVEDQELPTQPEAPDEHQDMDADPGGPEFLKTPLGGSFLVYESFLYRREKAAGEKVYWTCRDQARMGCRSRAITQGRRVTVMRGHCHPPDLGGLEALRQREKRPNTAQRGSPGGPEFLKTPLGGSFLVYESFLYRREKAAGEKVYWTCRDQARMGCRSRAITQGRRVMVMRRHCHPPDLGGLEALRQREHFPNLAQWDSPDPLRPLEFLRTSLGGRFLVHESFLYRKEKAAGEKVYWMCRDQARLGCRSRAITQGHRIMVMRSHCHQPDLAGLEALRQRERLPTTAQQEDPEKIQVQLCFKTCSPESQQIYGDIKDVRLDGESQ
Protein: Very long chain fatty acid elongase 5 (EC 2.3.1.199) (3-keto acyl-CoA synthase ELOVL5) (ELOVL fatty acid elongase 5) (ELOVL FA elongase 5) (Elongation of very long chain fatty acids protein 5) (Fatty acid elongase 1) (hELO1) (Very long chain 3-ketoacyl-CoA synthase 5) (Very long chain 3-oxoacyl-CoA synthase 5) (Q9NYP7)
Organism: Homo sapiens (Human)
Function: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme that acts specifically toward polyunsaturated acyl-CoA with the higher activity toward C18:3(n-6) acyl-CoA. May participate in the production of monounsaturated and of polyunsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators (By similarity). In conditions where the essential linoleic and alpha linoleic fatty acids are lacking it is also involved in the synthesis of Mead acid from oleic acid (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03205, ECO:0000269|PubMed:20937905}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03205}. Cell projection, dendrite {ECO:0000255|HAMAP-Rule:MF_03205, ECO:0000269|PubMed:25065913}. Note=In Purkinje cells, the protein localizes to the soma and proximal portion of the dendritic tree. {ECO:0000255|HAMAP-Rule:MF_03205, ECO:0000269|PubMed:25065913}.
Interaction partners:
- Acyl-CoA 6-desaturase
- Acyl-CoA
- Stearoyl-CoA desaturase
Sequence:
MEHFDASLSTYFKALLGPRDTRVKGWFLLDNYIPTFICSVIYLLIVWLGPKYMRNKQPFSCRGILVVYNLGLTLLSLYMFCELVTGVWEGKYNFFCQGTRTAGESDMKIIRVLWWYYFSKLIEFMDTFFFILRKNNHQITVLHVYHHASMLNIWWFVMNWVPCGHSYFGATLNSFIHVLMYSYYGLSSVPSMRPYLWWKKYITQGQLLQFVLTIIQTSCGVIWPCTFPLGWLYFQIGYMISLIALFTNFYIQTYNKKGASRRKDHLKDHQNGSMAAVNGHTNSFSPLENNVKPRKLRKD
Protein: Olfactory receptor 1A2 (Olfactory receptor 17-6) (OR17-6) (Olfactory receptor OR17-10) (Q9Y585)
Organism: Homo sapiens (Human)
Function: Odorant receptor.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
Sequence:
MKKENQSFNLDFILLGVTSQQEQNNVFFVIFLCIYPITLTGNLLIILAICADIRLHNPMYFLLANLSLVDIIFSSVTIPKVLANHLLGSKFISFGGCLMQMYFMIALAKADSYTLAAMAYDRAVAISCPLHYTTIMSPRSCILLIAGSWVIGNTSALPHTLLTASLSFCGNQEVANFYCDIMPLLKLSCSDVHFNVKMMYLGVGVFSLPLLCIIVSYVQVFSTVFQVPSTKSLFKAFCTCGSHLTVVFLYYGTTMGMYFRPLTSYSPKDAVITVMYVAVTPALNPFIYSLRNWDMKAALQKLFSKRISS
Protein: Protein phosphatase 1, regulatory subunit 13B (A0A8I6A8S6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MMPMILTVFLSNNEQILTEVPITPETTCRDVVEFCKEPGEGGCHLAEVWRGSERPIPCDHMMYEHLQKWGPRREEVKFFLRHEDSPTESSEQGARQSQEQRTQRNVMNVPGEKHTENGVGNPRVELTLSELQDMAARQQQQIESQQQMLVAKEQRLHFLKQQERRQQQSISENEKLQKLKERVEAQENKLKKIRAMRGQVDYSKIMNGNLSAEIERFSAMFQEKKQEVQTAILRVDQLSQQLEDLKKGKLNGFQSYNGRLTGPAAVELKRLYQELQIRNQLNQEQNSKLQQQKELLNKRNMEVAMMDKRISELRERLYGKKIQLNRVNGTSSPQSPLSTSGRVAAVGPYIQVPSTGGFPLPGDPVKPQSLTIASSAAHGRSKSDGYSRCRGTSTWTVSDLDIGPHCGSSGHSASPLVNSNDGNWPTLKQNSASVKSTQMAGGDWKDSGMEGTLKQGAISSQPLPLSALGATDKLGIEIGKGPPPIPGVGKPLPPSYGTYPSPGPLGPGSTSSLERRKEGSLPRPAAGPPSRQKPAPLPPAGSAPQPSSSQQIQQRISVPPSPTYPPAGPPAFPAGDGKPELPLTVAIRPFLADKGSRPQSPRKGPQTVNSSSIYSMYLQQATPPKNYQPPAHGTLNKSVKAVYGKPVLPSGSASPSPLPFLHGSLGTGTTQPQPPSECAEKEAEPEGPSVPGEGSTVESLPRPLSPTKLTPIVHSPLRYQSDADLEALRRKLANAPRPLKKRSSITEPEGPGGPNIQKLLYQRFNTLAGGMEGTPFYQPSPSQDFVGTLADVDNGNTNANGNLDESFPPRPTAPLPDELAPSSDANDNELPSPEPEELICPQTTHQTAEPTEDNNNNVATVPSTEQIPSPVAEAPSEEDQVPPAPLSPVVHPPTASASKRTNLKKPNSERTGHGLRVRFNPLALLLDASLEGEFDLVQRIIYEVEDPSKPNDEGITPLHNAVCAGHHHIVKFLLDFGVNVNAADSDGWTPLHCAASCNSVHLCKQLVESGAAIFASTISDIETAADKCEEMEEGYIQCSQFLYGVQEKLGVMNKGIVYALWDYEAQNNDELSFHEGDAITILRRKDENETEWWWARLGDREGYVPKNLLGLYPRIKPRQRTLA
Protein: Zinc finger protein 835 (Q9Y2P0)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MEGLLSVALQGAELEGNWKHEGQVEDLQENQESCPEPEAVACKGDPAGDSMQERDEFSRIPRTISSPAATQASVPDDSSSRRCSAPGESPKERHPDSRQRERGGGPKKPWKCGDCGKAFSYCSAFILHQRIHTGEKPFACPECGKAFSQSVHLTLHQRTHTGEKPYACHECGKAFSQGSYLASHWRTHTGEKPHRCADCGKAFTRVTHLTQHRRVHTGERPYACAQCAKAFRNRSSLIEHQRIHTGEKPYECSACAKAFRFSSALIRHQRIHTEEKPYRCGQCAKAFAQIAHLTQHRRVHTGEKPYTCQDCGALFSQSASLAEHRRIHTGEKPYACGQCAKAFTQVSHLTQHQRTHTGERPYPCHDCGKRFSNRSHLLQHRLVHTGERPYRCLQCGAAFSHVSSLIEHQKIHTGERPYKCGECGKAFSQGSSLALHQRTHTGERPYTCPECGKAFSNRSYLIQHHIVHTGEKPYECSGCGKAFSFSSALIRHQRTHADSSGRLCPAPTPDSTPGLSQGGETCQQGCPGRNPRGPAED
Protein: Retrotransposon hot spot (RHS) protein, putative (Q584M7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- E2 ubiquitin-conjugating enzyme
- ATP-dependent RNA helicase
Sequence:
MNQQVPIEGRGDIEGRRREREEAARNDAEPPAVQQRVENNNQPQWRLFSCIEAVLLNGRAHPENVSVNDYLRRNLLDDIDLDQRLLRASMFAFVQRCEEYINDVNALNRIFATTEYQVYKVFATAYPLLFREGILNLQRWQQADEVVKAGLQVNIRGQRDGGRLWIIVTNMLNDALDVALERAAQTAASAVEIKGVYDSIYDAKWSYVMSGYRREPLGMKVFNGKPQRIWTEAEVDITPDPANLDARVPERPNGLEIFVLTSEKGWPYDRFASRDVNIRKNNFKHVYIRREIMRVWYIIQRGLQTWWVEKTARRTPIHIVIGTPGIGKSYGVGSFLLHSLLHFNDGMLDVVAYFVGKIAYLIYNKKPGEEGRVERYKVPEDAVDAIAALVSKKKKGHIIVDIGKRLLTPPDELCHLSWGITVLTSPDTAHYEEWAKDTGGRRIIINCDDVRDMKAFVAWKKLCVLSEEVPRDKTRQQLKEELESEWKIVEERIDMVGPLPRFVFSAPDYDERLESVRKEARQLDSDNGKKYDKIISKSKGWQNDKVTHKLVKIVRVSSGTVNVESYRCRSLSVNIWNMLICTLFGILIVEMTSKEIIMSDESVGANAFERLALLSLLFPRVFKVIANNLKYLRRGREIADRRSILNDMAPQQLRLIGQKALPAAQQRPIERCEHMVLYLPATGNEPVVDGFFFVEGRLRRNRDGTAPPTTPNIAVLLQVTKSERHPTTTDKVQKFRENIASYFSDWNTFSGNMAWEMIYINSVNGGTITHRQLCGGPPDRDRGEDGGPLGPQTFWESIDQFQVTLKETMQAELIQAYRRESGMRDAPALMGLAGRRRAREEVVEGRGDVAMDDVEGGEDA
Protein: Signal recognition particle 54 kDa protein (SRP54) (EC 3.6.5.4) (Q57565)
Organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Function: Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00306}. Note=The SRP-RNC complex is targeted to the cytoplasmic membrane. {ECO:0000255|HAMAP-Rule:MF_00306}.
Interaction partners:
- Signal recognition particle receptor FtsY
- Signal recognition particle 19 kDa protein
- Large ribosomal subunit protein uL15
- Protein translocase subunit SecY
- Large ribosomal subunit protein uL2
- Small ribosomal subunit protein uS9
- Large ribosomal subunit protein uL3
- Small ribosomal subunit protein uS5
- Large ribosomal subunit protein uL13
- Large ribosomal subunit protein uL16
Sequence:
MLDKLGENLNKALNKLKAAAFVDKKLIKEVIKDIQRALIQADVNVKLVLKMSKEIERRALEEKTPKGLSKKEHIIKIVYEELVKLLGEEAKKLELNPKKQNVILLVGIQGSGKTTTAAKLARYIQKRGLKPALIAADTYRPAAYEQLKQLAEKIHVPIYGDETRTKSPVDIVKEGMEKFKKADVLIIDTAGRHKEEKGLLEEMKQIKEITNPDEIILVIDGTIGQQAGIQAKAFKEAVGEIGSIIVTKLDGSAKGGGALSAVAETKAPIKFIGIGEGIDDLEPFDPKKFISRLLGMGDLESLLEKAEDMVDEKTEESIDAIMRGKFTLNELMTQLEAIENMGSMKKILSMIPGFGGAMPKELSHLTEAKIKKYKVIISSMTKEERENPKIIKASRIRRIARGSGTTENDVREVLRYYETTKNAIDKLRKGKMLRIGGPLGQIMRQLMFKEG
Protein: Dihydrofolate reductase (EC 1.5.1.3) (P00374)
Organism: Homo sapiens (Human)
Function: Key enzyme in folate metabolism. Contributes to the de novo mitochondrial thymidylate biosynthesis pathway. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. Binds its own mRNA and that of DHFR2.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:P00375}. Cytoplasm {ECO:0000250|UniProtKB:P00375}.
Interaction partners:
- Thymidylate synthase
- Folylpolyglutamate synthase, mitochondrial
- Serine hydroxymethyltransferase, cytosolic
- Serine hydroxymethyltransferase, mitochondrial
- C-1-tetrahydrofolate synthase, cytoplasmic
- Trifunctional purine biosynthetic protein adenosine-3
- Bifunctional purine biosynthesis protein ATIC
- Sepiapterin reductase
- Dihydropteridine reductase
- Methionine synthase
Sequence:
MVGSLNCIVAVSQNMGIGKNGDLPWPPLRNEFRYFQRMTTTSSVEGKQNLVIMGKKTWFSIPEKNRPLKGRINLVLSRELKEPPQGAHFLSRSLDDALKLTEQPELANKVDMVWIVGGSSVYKEAMNHPGHLKLFVTRIMQDFESDTFFPEIDLEKYKLLPEYPGVLSDVQEEKGIKYKFEVYEKND
Protein: NADH-ubiquinone oxidoreductase chain 5 (EC 7.1.1.2) (Q8HCR3)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004448}.
Interaction partners:
- NADH dehydrogenase iron-sulfur protein 2
- NADH-ubiquinone oxidoreductase chain 1
- NADH-ubiquinone oxidoreductase chain 3
- NAD
- NADH dehydrogenase iron-sulfur protein 3
- NAD
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH dehydrogenase iron-sulfur protein 3
- NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial, putative, expressed
- NADH-ubiquinone oxidoreductase 23 kDa subunit, mitochondrial, putative, expressed
Sequence:
MYLLIVFLPLLGSSVAGFFGRFLGSEGTAIMTTTCVSFSSILSLIAFYEVALGASACYLRIAPWISSEMFDASWGFFFDSLTVVMLIVVTFISSLVHLYSISYMSEDPHSPRFMCYLSIFTFFMLMLVTGDNFLQLFLGWEGVGLASYLLIHFWFTRLQADKAAIKAMLVNRVGDFGLALGIFGCFTLFQTVDFSTIFACASAPRNEWIFCNMRLNAITLICILLFIGAVGKSAQIGLHTWLPDAMEGPTPVSALIHAATMVTAGVFMIARCSPLFEYSPTALIVITFAGAMTSFLAATTGILQNDLKRVIAYSTCSQLGYMIFACGISNYSVSVFHLMNHAFFKALLFLSAGSVIHAMSDEQDMRKMGGLASSFPLTYAMMLMGSLSLIGFPFLTGFYSKDVILELAYTKYTISGNFAFWLGSVSVLFTSYYSFRLLFLTFLVPTNSFGRDRLRCHDAPIPMAIPLILLALGSLFVGYLAKDMMIGLGTNFWANSLFVLPKNEILAESEFAAPTIIKLIPILFSTLGAFLAYNVNLVADQFQRAFQTSTFCNRLYSFFNKRWFFDQVLNDFLVRSFLRFGYSVSFEALDKGAIEILGPYGISYTFRRLAERISQLQSGFVYHYAFAMLLGLTLFVTFFCMWDSLSSWVDSRLSFILLVSSFLINKSSQE