wanglab/gogpt-training-data huggingface dataset:
Protein: Subtilisin-like protease 2 (EC 3.4.21.62) (Merozoite surface sheddase) (MESH) (PfSUB2) (O97364)
Organism: Plasmodium falciparum
Function: Serine protease which plays an essential role in the shedding of AMA1, MSP1 and MSP7 from the surface of the invading merozoite; this step is essential for productive invasion and the release of the adhesion between the erythrocyte and the merozoite. May cleave TRAMP/PTTRAMP, thereby shedding TRAMP from the merozoite surface during erythrocyte invasion (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:10551362, ECO:0000269|PubMed:16322767}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle, microneme membrane {ECO:0000269|PubMed:16322767}; Single-pass type I membrane protein {ECO:0000305}. Note=In mature schizonts, localizes to micronemes at the merozoite apical region (PubMed:10551362, PubMed:16322767). Immediately after schizont rupture, secreted from the micronemes to the merozoite surface where it redistributes in an actin-dependent manner to accumulate at the posterior end of newly released merozoites (PubMed:16322767). {ECO:0000269|PubMed:10551362, ECO:0000269|PubMed:16322767}.
Interaction partners:
Sequence:
MLNIIYVVSLILIKFIFYKECNNNNNYYLSNIELYNYKLRKRNRILNNNINDRKSFLSDLEQNYKPLFDIYELSANFEKRRKELEKKTKGEENEIEKKKENDLEEKKENEIEKKKENDLEKEYNDVINLLELSLSSEYKELNADVSNNDNSGHEENNKHKLNKKNSSNYKNDKSLDELIKGAILKLKQNPNIKNKNMLDYDKIFKIIKEKLINKNLASNKIKGGDNEKLKEEKKQSDISTNVEVKKDIINDQLNKGIPTKIENKDDMINKESNKEDITNEGKSNSLNNLNTLNNDGNIITKVYDHYTIVTNSNDILNDISIDASDISKNSIGGINIPFNENDNSSFTHQRYIVLSNNGEKKYKIVLMTKNPKFMDMDGIYDEEEKKESLIELNQKVNKEENTNLYDGTGTLYYGKKSKKEKENTQQKGGNNPNVDINILNNNNNNNNNNNNNSNNNSNSMNDEEINYNNNNNKESPSMFRRFINFLSFSGNENETEDTLIYHNKNDNSYKNKKEGTGKNNDNNDPNNNNNKKILLNVDKLVDQYLLNLKNNHTSKQELILVLKGELDLHSKNMKNVINNAKKNLEKYFKEHFKEFDKISYDISTPINFLCIFIPTLFDMNNMDLLKQALLILHNDLHEYVENWSFSSTYHTYEADYIKEQDSVYDRSPKKKYIKASKKLYNNKYSFLNKFLNIEPLILFAKKLNSKRSNIEKEILNFLPKELRDYSTWNLSIIRVFNAWFLAGYGNKNVKVCVVDSGADIKHVDLNGNLYIPEYNEKYEMTQDFYNFMVKNPTDASGHGTHVTGIIGGVANDLGVVGVAPNITLISLRFIDGKKYGGSFHAIKALNVCILNKAPIINASWGSSHFDVNLHLAVERLKYTLNGKGSVLIAASGNKSNDNDISPLYPATFTFPHVYSVASISRNFEISPFSNYGHKSVHILAPGHHIYSTIPNNSYKIFTGTSMAAPHVCGVSALVYSVCYNQGFIPQAEEVLDILTRTSIKIISTKKRTINDSLVNAEGAVLTTLLGGLWMQMDCYFVKFNLEKGKKKHIPVVFSAYKKGVYETDIVIAIIPIDGKSKIYGEIHIPIKIVTDVNIPNFQESPRRGKNYTIDSNEAQHDEVLSYICENALYNLYEYDSHYLLASVILFFLALLSIFVGMIYMKSRKHSDKKCSKNLMKSNYIPEMDDGMEETQQLQQERRQYFRELFGENLEKNYDQHFVQDFGQDFRQDFKLGSTPDLKQYSDIDLQNKIQQPERKTVKIIINNFEDRKKETKRRLLKGLNYDGENAKKHDFTNESISNSRKNFKFSNNTEMKKNTIKSEDVKIASDDNVNKAMNQLDDMFMK
Protein: Mitochondrial carrier homolog 2 (Q9PUL9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00004374}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004374}.
Interaction partners:
- C1q and TNF-related 4.
Sequence:
MADTCGQVLLGSGLTVLSHPLMYIKVLVQVGHEPLAPTLGRNMFGRQVYQLPGLFAYAKHIIKIDGKAGLFKGLAPRLCAGTIGTIVHSKALQKCQEEKIEVLGSSLKSDEGSLQQVINETTKEMIARSCATVVTHPFHVITLRCMVQFIGREAKYSGVFDSIVTIYREEGILGFFAGLIPRLLGDVLSLWICNMLAHFINTYTIDESTSHTGEIKNCSQAVTGFFASMLTYPFVLVSNMMAVNNCGLAGGLPPYAAIYPNWLHCWSHLSREGNMSRGNSLFFRKLPAGKTYAIEQKRFF
Protein: Evasin P1243 (A0A0C9S461)
Organism: Amblyomma americanum (Lone star tick)
Function: Salivary chemokine-binding protein which has chemokine-neutralizing activity and binds to host chemokines CCL1, CCL3, CCL3L1, CCL4, CCL4L1, CCL5, CCL7, CCL8, CCL13, CCL14, CCL15, CCL16, CCL17, CCL18, CCL19, CCL20, CCL21, CCL22, CCL23, CCL24, CCL27, XCL1, CX3CL1, CXCL1, CXCL2, CXCL4, CXCL5, CXCL6, CXCL7, CXCL9, CXCL12 and CXCL14.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MHSTIAYVFVSALALFAALHGSTSARNHTEDNSTEYYDYEEARCACPARHLNNTNGTVLKLLGCHYFCNGTLCTAPDGYPCYNLTAQQVRTLTTYPNTSCAVGVCMKGTCVKNGTMEQCFKTP
Protein: Chaperone DnaJ-domain superfamily protein (F4JG06)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MGGEDDKDKKWNPPPPQQKPDSRPWEVLAAFVICATATTFAVHQLRRNFDWVYTQLTRTPSAGRGTFRTSFQEEAWRRYNKRMQEEYEDELERVARIRRMQSVFNRERNKFRRGYENWTENDPGAQQYHQQFQRHDWYWKTESSHRNQRTNHQEPSDQRRVYPLSHHYSVLGLSRSRATPYTEAEIKKAFREKALEFHPDQNQDNKIVAEAKFKEVLLSYEAIKQEIKEK
Protein: Zymogen granule membrane protein 16 (Zymogen granule protein 16) (Secretory lectin ZG16) (Q8K0C5)
Organism: Mus musculus (Mouse)
Function: May play a role in protein trafficking. May act as a linker molecule between the submembranous matrix on the luminal side of zymogen granule membrane (ZGM) and aggregated secretory proteins during granule formation in the TGN (By similarity).
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:O60844}. Zymogen granule lumen {ECO:0000250|UniProtKB:Q8CJD3}. Golgi apparatus lumen {ECO:0000250|UniProtKB:Q8CJD3}.
Interaction partners:
- Colipase
- Syncollin
- Mucin-2
- Mucin-2
- Calcium-activated chloride channel regulator 1
- Calcium-activated chloride channel regulator 3A-1
- HORMA domain-containing protein 1
- Anterior gradient protein 2 homolog
Sequence:
MLAVALLVLLCASASANSIQSRTSSYSGEYGGKGGKRFSHSGNQLDGPITAFRIRVNRYYIVGLQVRYGTVWSDYVGGTQGDLEEIFLHPGESVIQVSGKYKSYVKQMIFVTDKGRYLPFGKASGTSFNAVPLHPNTVLRFISGRSGSAIDSISLHWDTYPSHCNTC
Protein: Sterile alpha motif domain-containing protein 1 (SAM domain-containing protein 1) (Atherin) (Q6SPF0)
Organism: Homo sapiens (Human)
Function: Unmethylated CpG islands (CGIs)-binding protein which localizes to H3K4me3-decorated CGIs, where it acts as a transcriptional repressor. Tethers L3MBTL3 to chromatin and interacts with the KDM1A histone demethylase complex to modulate H3K4me2 and H3K4me3 levels at CGIs. Plays a role in atherogenesis by binding with LDL on cell surface and promoting LDL oxidation which leads to the formation of foam cell.
Subcellular location: Nucleus {ECO:0000269|PubMed:34006929}. Chromosome {ECO:0000269|PubMed:34006929}. Secreted {ECO:0000269|PubMed:16159594, ECO:0000269|PubMed:34006929}. Note=In atherosclerotic lesions, it is found in the extracellular compartment and in foam cells cytoplasm. {ECO:0000269|PubMed:16159594, ECO:0000269|PubMed:34006929}.
Interaction partners:
- Lethal
Sequence:
MAGPPALPPPETAAAATTAAAASSSAASPHYQEWILDTIDSLRSRKARPDLERICRMVRRRHGPEPERTRAELEKLIQQRAVLRVSYKGSISYRNAARVQPPRRGATPPAPPRAPRGAPAAAAAAAPPPTPAPPPPPAPVAAAAPARAPRAAAAAATAPPSPGPAQPGPRAQRAAPLAAPPPAPAAPPAVAPPAGPRRAPPPAVAAREPPLPPPPQPPAPPQQQQPPPPQPQPPPEGGAVRAGGAARPVSLREVVRYLGGSGGAGGRLTRGRVQGLLEEEAAARGRLERTRLGALALPRGDRPGRAPPAASARPSRSKRGGEERVLEKEEEEDDDEDEDEEDDVSEGSEVPESDRPAGAQHHQLNGERGPQSAKERVKEWTPCGPHQGQDEGRGPAPGSGTRQVFSMAAMNKEGGTASVATGPDSPSPVPLPPGKPALPGADGTPFGCPPGRKEKPSDPVEWTVMDVVEYFTEAGFPEQATAFQEQEIDGKSLLLMQRTDVLTGLSIRLGPALKIYEHHIKVLQQGHFEDDDPDGFLG
Protein: Putative pentatricopeptide repeat-containing protein At5g09950 (Q9FIB2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Phosphoglycerate mutase family protein
Sequence:
MTNCVPLSFVQSCVGHRGAARFFHSRLYKNRLDKDVYLCNNLINAYLETGDSVSARKVFDEMPLRNCVSWACIVSGYSRNGEHKEALVFLRDMVKEGIFSNQYAFVSVLRACQEIGSVGILFGRQIHGLMFKLSYAVDAVVSNVLISMYWKCIGSVGYALCAFGDIEVKNSVSWNSIISVYSQAGDQRSAFRIFSSMQYDGSRPTEYTFGSLVTTACSLTEPDVRLLEQIMCTIQKSGLLTDLFVGSGLVSAFAKSGSLSYARKVFNQMETRNAVTLNGLMVGLVRQKWGEEATKLFMDMNSMIDVSPESYVILLSSFPEYSLAEEVGLKKGREVHGHVITTGLVDFMVGIGNGLVNMYAKCGSIADARRVFYFMTDKDSVSWNSMITGLDQNGCFIEAVERYKSMRRHDILPGSFTLISSLSSCASLKWAKLGQQIHGESLKLGIDLNVSVSNALMTLYAETGYLNECRKIFSSMPEHDQVSWNSIIGALARSERSLPEAVVCFLNAQRAGQKLNRITFSSVLSAVSSLSFGELGKQIHGLALKNNIADEATTENALIACYGKCGEMDGCEKIFSRMAERRDNVTWNSMISGYIHNELLAKALDLVWFMLQTGQRLDSFMYATVLSAFASVATLERGMEVHACSVRACLESDVVVGSALVDMYSKCGRLDYALRFFNTMPVRNSYSWNSMISGYARHGQGEEALKLFETMKLDGQTPPDHVTFVGVLSACSHAGLLEEGFKHFESMSDSYGLAPRIEHFSCMADVLGRAGELDKLEDFIEKMPMKPNVLIWRTVLGACCRANGRKAELGKKAAEMLFQLEPENAVNYVLLGNMYAAGGRWEDLVKARKKMKDADVKKEAGYSWVTMKDGVHMFVAGDKSHPDADVIYKKLKELNRKMRDAGYVPQTGFALYDLEQENKEEILSYHSEKLAVAFVLAAQRSSTLPIRIMKNLRVCGDCHSAFKYISKIEGRQIILRDSNRFHHFQDGACSCSDFW
Protein: IQ domain-containing protein F1 (Q9D9K8)
Organism: Mus musculus (Mouse)
Function: Involved in sperm capacitation and acrosome reaction.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:25380116}.
Interaction partners:
- Coiled-coil domain-containing protein 83
Sequence:
MGEEQQKPEELNAPTDDAPQEKQQPADLSSETEKAKSKKKQELSEKDQVVKIQAWWRGTLVRRSLLHAALSAWIIQCWWRLILPKIMEKRRQSMLDTFQQEQWAVVRLQSWIRMWRIRRRYCRLLKAVRTIQSHWRGHTCSSRGVIKGQYRISTSQMHLELEVLLGSGPCIVTECIPLPIKQ
Protein: Bruno 1, isoform D (RE72594p) (Q8SYC0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLNKKLNENDVRKLFEVHGAIEECTVLRDQNGQSKGCAFVTFATKHAAISAIKVTLSQNKIMEGCTSPLVVKFADTQKEKEQKKIQQIQANLWNLASNINIPLGQTATSVTTPILPNPPQQPSPVLGADAITPASIQLLQQLQAVGLQHQLLQALTGLGAQQSSSATDTSAVAAAGLLTPMTVQNLAAIAAMTQPSLSNAAAAAAAATSPGSAQLTNTAALLWSDPNPMASAYMSTAAGLPQFGSASALSTSPLASVALSAAAAAAAGKQIEGPEGCNLFIYHLPQEFTDTDLASTFLPFGNVISAKVFIDKQTSLSKCFGFVSFDNPDSAQVAIKAMNGFQVGTKRLKVQLKKPKDSKPY
Protein: DNA-(apurinic or apyrimidinic site) lyase (EC 4.2.99.18) (E5KPM9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPARALLPRRMGHRTLASTPALWASIPCPRSELRLDLVLPSGQSFRWREQSPAHWSGVLADQVWTLTQTEEQLHCTVYRGDKSQASRPTPDELEAVRKYFQLDVTLAQLYHHWGSVDSHFQEVAQKFQGVRLLRQDPIECLFSFICSSNNNIARITGMVERLCQAFGPRLIQLDDVTYHGFPSLQALAGPEVEAHLRKLGLGYRARYVSASARAILEEQGGLAWLQQLRESSYEEAHKALCILPGVGTKVADCICLMALDKPQAVPVDVHMWHIAQRDYSWHPTTSQAKGPSPQTNKELGNFFRSLWGPYAGWAQAAGSDAS
Protein: Calponin-homology (CH) domain-containing protein (U4PBJ9)
Organism: Caenorhabditis elegans
Interaction partners:
- Actin
- FERM domain-containing protein
- Zyxin
- Vinculin
- Calponin-homology
- mitogen-activated protein kinase kinase
- mitogen-activated protein kinase kinase
- MAP kinase kinase mkk-4
- Ubiquitin-like domain-containing protein
- Calponin-homology
Sequence:
MAQPKRLDQEEEVVPAIRHDDAEWKIIQQNTFTRWVKNHLQKAGETIESLETDFSDGLKLIALAQVLSHKNVGKFNKKVAFRSQKLENVSLALNFFQNEENIKIINIDSTHIVDHNKKLILGLVWTLILHYSISMGWIQEKREDGDNKEETPKQKLLNWIRNRLPVSGMPISNFTSDWNDGVALGALVNSMAPGALEDWENWSPNDALENTEKAMKSAQDLLKVAPLIAPAEMIHPEIDEMSVMTYLSQFPATKPIIMKPKVQATISNLDKILQVNDPREFDLKLSRDGFKPKVSIRDEDGQDIHLSLKKVEDKENAYKVKFTPTKIGFIHVDVAANDVHTFETQTIPEASVICQVVPIARLLDYNKTAKVGDDVKFAVVDAIEGPVEAIVVDPTGKEHRMVILDGTSPGEHSFEYKIPCIGLHSVNVFHKKLPLTGSPFPLRGKPKNSFKVWGRGIAPEGIRKNDVVGVHVESLDPEENIANANISLEVLKPSDGSHLPVSVGYNDESQSMDFEYSPKQAPDDLEVLVKVAGEVIESHKIHVAPESSSKIRAFGAGLEGGIVNEPCVFDVEMNGESKDLSFAVEGPSKAEIGCQERPDGSAILSYTPTVAGVYKVGVLADGKHIQDSPFVLRVTEPIEGLKPSATRVTGIDESKVYNVGEKIPFRVDTRLCGVDLVPKVEILDPELNPISYGAREITPGLFEYTLIPDAPIKHKIDVSVAGVSVPGAPFSVKVKEPTDASKLKIFGPGVDGPVYSKEPTRFTIDATQAGPGAVEVALRDDQGENVDLDVLDNQDGSFTVKYTAQRPGAYQLNVVFAGEEISPIEINVKPNVDVSGIRVEGLENENLLIGSHLRPTINIGKLEPKSKGLQLIDEVNGKRYNVPMKINPDGTYSTDTPLMEVGEHKLQLLFDEIPVKEAVVEVIKGTDVNKCKAYGPGLEQAVVGEKAVFELDLDGAGEGALSMEMRGPAKAESRIQDRGNGKCSVEYVAKAPGDYEMAIKFGKDEQKEHVKGSPFKAVVDYKKDPSQITISGLDQPNYRLNQPINFVIDTSKTKDLPVKATVPSDFAQLQPVVSRSPSNPRHHNVRFVPSGKPNVSIPIEIIYDGLKIDEKLVKVLPEVEPQLIKILHDKKKDSLTTTPITTNASHEGHVPFDVRDCGNVKKIESRVFGPDGKERLNHVRSTEQNGIYDVSFPTDMAGEYCVVFYINGQEVAARVPVMAEKIGRKEDVIKEEIVFHPEIAEHSPTVLTYNHPIDAKKKKAHPAIQVLAAKPDAVRLEHIQELVDNGHRVADRIVFTATKLGTNTLDVFYGGEHVDHVEYEAIGKLEYERIQAERAKVVVEKEDDVDKYEKQYKDEPSSAPADPRVAPTNGKEPTTAQESKKNGNQQKLAPSAEIEHKPLEKYFTFQFNVRDLGYQPKDLEAIVMPPTQKKEVAEIIDNLDGTILVKYTPKVHGSHELSILQNGAQLQGTPIKFYVDAYGDGWATVYGPGLQNAVVGEPATFTVCAKGSQAKELSVSIEGPAKSQIKIHDNKDGTCSAAWVPPVPGEYKVHVKLGGKAVKDSPFRVLVMGEGQKRSHLSVGSTSEVALPITQQELKGISASIKSPGGIEEPCFVRLLDGGRLGVSFTPREAGEHLITVKRDGKLVPKAPFKIKVDKTQVGDASKVEVSGSGKAKGITLQANELLVDTSKAGYGGLSVSVQGPSKAELTCKEVKSGLIKVLYTPTEPGVYAIAIKFADHHVKDSPLTVQCTGKSAGRVIQTIQKDVEQHGICLPDQESHLFLKLLNTSPMDITARLMDPKGHTDDIEMRDLGQQYYQLKFTPKMEGIHTLSVMYKDAHVNGSPFQFTVGSFSEGGAHKVRAAGQGVVRGETGTFNAFNIYHREAGVGAVAVTIEGPSKATLEFKDHNDGNCHVDYKVATPGEYVVAVKFNDQHIPDSPFKVYIAPATGEVRKLELAQFHGQGIPAGKAFTFTVLTHRAKGHLEAKVVTPNNEVDTIDIVPIEDGESYAMRFVPKETGNHFIHVTLDGAPMRESPFRLRVGGKDLCDPTAISASGDGLVKGTTGQKCEFVINTANAGAGILTVQMDGPSKATLDAYELEKGYKVRYTPLAPGSYFASVKYNGIHAPGSPFKIPVEGKELGGNGYNETSHVKIDAVAKTSKGTVAVVPEYQGDAAKVTAKGAGLNKFFPGRPAAFQIDTGLAGTNLLMVGVVTTKGPCEEVVVRHQGSGHYVCSYRIPDRVKGFVFIKYGDKEIPGSPFAIEP
Protein: Set1/Ash2 histone methyltransferase complex subunit ASH2 (Absent, small, or homeotic discs protein 2) (Q94545)
Organism: Drosophila melanogaster (Fruit fly)
Function: Transcriptional regulator. Regulates a number of genes involved in wing development including activation of net and bs and repression of rho and kni and controls vein-intervein patterning during wing development. Required for correct expression of a number of homeotic genes including Scr in the first leg imaginal disk and Ubx in the third leg imaginal disk and haltere disks. Required for stabilization of the histone-lysine N-methyltransferase trr and for trimethylation of 'Lys-4' of histone H3. Plays a role in maintenance of transcriptionally active chromatin through down-regulation of histone H1 hyperphosphorylation.
Subcellular location: Nucleus {ECO:0000269|PubMed:17466076, ECO:0000269|PubMed:21694722, ECO:0000269|PubMed:23197473, ECO:0000269|PubMed:8889525}. Chromosome {ECO:0000269|PubMed:17466076, ECO:0000269|PubMed:21694722, ECO:0000269|PubMed:23197473, ECO:0000269|PubMed:8889525}. Note=Accumulates on salivary gland polytene chromosomes. {ECO:0000269|PubMed:17466076, ECO:0000269|PubMed:21694722, ECO:0000269|PubMed:23197473, ECO:0000269|PubMed:8889525}.
Interaction partners:
- Retinoblastoma-binding protein 5 homolog
- Histone-lysine N-methyltransferase SETD1
- Protein dpy-30 homolog
- Histone-lysine N-methyltransferase trithorax
- CXXC-type zinc finger protein 1
- Host cell factor
- Histone-lysine N-methyltransferase trr
- Protein will die slowly
- WD repeat-containing protein 82
- HL01030p
Sequence:
MEDSQMDTSSPTESSSEVNFTAEEDKSQETRSAAGVCYCGKERNLNIVELLCATCSRWVHETCVSYQLGKGKLLPFITNYVFVCKNCSASGLESFRKSQATISQMCHCAIANMQQAASRDGRRQIQFSKDKEIIPYIEQYWEAMTTMPRRLTQSWYSTVQRSLVKDVQTLFTYEEHAEHGAMYGLFHQDLRIIKPNYESMSKSGALRLTDDGYTQASLSKNNRQKRKFPGTDSGPTGKKGRPSSDITANVKLPPHGYPLEHPFNKDGYRYILAEPDPHAPFRQEFDESSDWAGKPIPGWLYRILVPHSVLLALHDRAPQLKISEDRLAVTGERGYCMVRATHSVNRGCWYFEVTIEEMPDGAATRLGWGREYGNLQAPLGYDKFGYSWRSRKGTKFTESHGKHYSDAYVEGDTLGFLIELPEEASLDYLPNTFKDRPLVKFKSHLYYEDKDKITETLKNLHILQGSRIEFFKNGQSQGVAFEDIYAGSYFPAISIHKSATVSVNFGPAFKYPEVLVEHKAKGMHDRVEELITEQCLADTLYLTEHDGRLRLDNMGL
Protein: Serine acetyltransferase 1, chloroplastic (AtSAT-1) (EC 2.3.1.30) (AtSERAT2;1) (SAT-p) (Q42588)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Serine acetyltransferase which catalyzes the formation of O-acetyl-L-serine from acetyl-CoA and L-serine. Also displays O-acetylserine (thio1)-lyase activity in vitro. May be involved in detoxification process by mediating the production of glutathione.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:9830017}. Cytoplasm {ECO:0000269|PubMed:9830017}. Note=First chloroplastic and progressively cytoplasmic during aging.
Interaction partners:
- Cysteine synthase 1
- Cysteine synthase, chloroplastic/chromoplastic
- S-sulfo-L-cysteine synthase
- Bifunctional cystathionine gamma-lyase/cysteine synthase
- Cysteine synthase, mitochondrial
- Phosphoserine phosphatase, chloroplastic
- Putative inactive cysteine synthase 2
- Bifunctional aspartokinase/homoserine dehydrogenase 1, chloroplastic
- Bifunctional aspartokinase/homoserine dehydrogenase 2, chloroplastic
- Serine racemase
Sequence:
MATCIDTCRTGNTQDDDSRFCCIKNFFRPGFSVNRKIHHTQIEDDDDVWIKMLEEAKSDVKQEPILSNYYYASITSHRSLESALAHILSVKLSNLNLPSNTLFELFISVLEESPEIIESTKQDLIAVKERDPACISYVHCFLGFKGFLACQAHRIAHTLWKQNRKIVALLIQNRVSESFAVDIHPGAKIGKGILLDHATGVVIGETAVVGDNVSILHGVTLGGTGKQSGDRHPKIGDGVLIGAGSCILGNITIGEGAKIGSGSVVVKDVPARTTAVGNPARLIGGKENPRKHDKIPCLTMDQTSYLTEWSDYVI
Protein: Baeyer-Villiger monooxygenase (BVMO) (EC 1.14.13.-) (Q9I3H5)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Catalyzes a Baeyer-Villiger oxidation reaction, i.e. the insertion of an oxygen atom into a carbon-carbon bond adjacent to a carbonyl, which converts ketones to esters or lactones using NADPH and/or NADH as an electron donor. Thus, can convert bicyclo[3.2.0]hept-2-en-6-one into the oxidative lactone products 2-oxabicyclo[3.3.0]oct-6-en-3-one and 3-oxabicyclo[3.3.0]oct-6-en-2-one. Is also able to catalyze the sulfoxidation of methyl phenyl sulfide (thioanisole).
Interaction partners:
- Probable short-chain dehydrogenase
- Probable acyl-CoA dehydrogenase
- Probable short-chain dehydrogenase
- Probable short-chain dehydrogenase
- Probable oxidoreductase
- Probable oxidoreductase
- Alkane 1-monooxygenase 2
- HTH tetR-type domain-containing protein
- Probable esterase/deacetylase
- Metal-dependent hydrolase
Sequence:
MYTPANNHNRSLAMSTQPTPAAARHCKVAIIGTGFSGLGMAIRLRQEGEDDFLIFEKDAGVGGTWRVNNYPGCACDVQSHVYSFSFEANPEWTRMFARQPEIRAYLEKCWEKYRLQEKTLLNTEIGKLAWDERQSLWHLHDAQGNHYTANAVVSGMGGLSTPAYPRLDGLENFQGKVFHSQQWDHDYDLKGKRVAVIGTGASAIQFVPEIQPLVAALDLYQRTPPWILPKPDRAISETERRRFRRFPLVQKLWRGGLYSLLEGRVLGFTFAPQVMKLVQRLAIRHIHKQIKDPELRRKVTPDYTIGCKRILMSHNYYPALAAANSTVITEGIRAVTANGIVDGNGREREVDAIIFGTGFTANDPIPRGVVFGRDGRDLLDSWSKGPEAYKGTTTAGFPNLFFLMGPNTGLGHNSMVYMIESQIAYVLDALKLMKRRELLSLEVKAPVQERYNEYLQRKLDRSVWSVGGCKSWYLHPVSGRNCTLWPGFTWRFRALTRQFDASAYHLTTTPLAALSNEARQQAEGVPA
Protein: Nucleoprotein (N) (Nucleocapsid protein) (NC) (Protein N) (P0DTC9)
Organism: Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) (SARS-CoV-2)
Function: Packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP) and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M. Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication (By similarity).
Subcellular location: Virion {ECO:0000255|HAMAP-Rule:MF_04096}. Host cytoplasm {ECO:0000269|PubMed:33060197, ECO:0000269|PubMed:34341353}. Secreted {ECO:0000269|PubMed:35921414}. Host extracellular space {ECO:0000269|PubMed:35921414}. Note=Probably associates with ER-derived membranes where it participates in viral RNA synthesis and virus budding. When located inside the virion, complexed with the viral RNA. Can be secreted by unconventional protein secretion (UPS) (PubMed:35921414). When secreted, can bind to host glycosaminoglycans on infected and non infected cells (PubMed:35921414). Found in host cytoplasmic stress granules (PubMed:34901782). {ECO:0000255|HAMAP-Rule:MF_04096, ECO:0000269|PubMed:34901782, ECO:0000269|PubMed:35921414}.
Interaction partners:
Sequence:
MSDNGPQNQRNAPRITFGGPSDSTGSNQNGERSGARSKQRRPQGLPNNTASWFTALTQHGKEDLKFPRGQGVPINTNSSPDDQIGYYRRATRRIRGGDGKMKDLSPRWYFYYLGTGPEAGLPYGANKDGIIWVATEGALNTPKDHIGTRNPANNAAIVLQLPQGTTLPKGFYAEGSRGGSQASSRSSSRSRNSSRNSTPGSSRGTSPARMAGNGGDAALALLLLDRLNQLESKMSGKGQQQQGQTVTKKSAAEASKKPRQKRTATKAYNVTQAFGRRGPEQTQGNFGDQELIRQGTDYKHWPQIAQFAPSASAFFGMSRIGMEVTPSGTWLTYTGAIKLDDKDPNFKDQVILLNKHIDAYKTFPPTEPKKDKKKKADETQALPQRQKKQQTVTLLPAADLDDFSKQLQQSMSSADSTQA
Protein: A kinase anchor protein 6 (E9Q9K8)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus membrane {ECO:0000256|ARBA:ARBA00004126}.
Interaction partners:
- Ryanodine receptor 2
- 3',5'-cyclic-AMP phosphodiesterase 4D
- A-kinase anchor protein 1, mitochondrial
- A-kinase anchor protein 7 isoform gamma
- Rap guanine nucleotide exchange factor 3
- A-kinase anchor protein 9
Sequence:
MLTMSVTLSPLRSQDPDPMATDASPMAINMTPTVEQEEGEGEEAVKDVGAEQQYGKPPPLHTAADWKIVLHLPEIETWLRMTSERVRDLTYSVQQDADSKHVDVHLVQLKDICEDISDHVEQIHALLETEFSLKLLSYSVNVIVDIHAVQLLWHQLRVSVLVLRERILQGLQDANGNYTRQTDILQAFSEETTEGRLDSLTEVDDSGQLTIKCSQNYLSLDCGITAFELSDYSPSEDLLGGLGDMTTSQAKTKSFDSWSYSEMEKEFPELIRSVGLLTVATEPVPSSCGAANEDSSQVILSEDHRGGHEEDGALEPGEQLGSTLETSSLGDTLTNAAEHPPETANQDSTSSPQLGAKKSQPGPCEMMTPKRSIRDCFNYNEDSPTQPTLPKRGLFLKETLKNERRGSDGKGRVVDLKPELSRSTPSLVEPPDRSKLCLVLQSSYPSSPSAASQSYECLHKVGIGNLENIVRSHIKEISSSLGRLTDCHKEKPRLKKPHKTLAEVSLCKIPKRGTGSGKQSENTRSSVVPTMVSPGAPKATARPATDSASTTSGDTCHQRNRGGKLPAQSKASSSSPCSHSSESSLGSDNIKSPLPLLSKSQKGSPPAPCHATQNGQVVEAWYGSDEYLALPSHLKQTEVLALKLENLTKLLPQKPRGETIQDIDDWELSEMNSDSEIYPTYHIKKKHTRLGTVSPSSSSDIASSLGESIESGPLSDILSDEDLCMPLSGMKKFTDEKSERPSSSEKNESHSATKSALIQKLMKDIQHQDNYEAIWERIEGFVNKLDEFIQWLNEAMETTENWTPPKAETDSLRLYLETHLSFKLNVDSHCALKEAVEEEGHQLLELIASHKAGLKDMLKMIASQWKELQRQIKRQHSWILRALDTIKAEILATDVSVEDEEGTGSPKAEAQLCYLEAQRDAVEQMSLKLYSEQYTSGSKRKEEFADMSKAHSVGSNGLLDFDSEYQELWDWLIDMESLVMDSHDLMMSEEQQQHLYKRYSVEMSIRHLKKTELLSKVEALKKGGLSLPNDILEKVDSINEKWELLGKTLREKIQDTMAGHSGSGPRDLLSPESGSLVRQLEVRIKELKRWLRDTELFIFNSCLRQEKEGTSAEKQLQYFKSLCHEIKQRRRGVASILRLCQHLLDDRDTCNLNADHQPMQLIIVNLERRWEAIVMQAVQWQTRLRKKMGKESETLNVIDPGLMDLNGMSEDALEWDETDISNKLISVHEESNDLDQDLEPMVPTVKLEETHHKDSGYEEEAGDCGGSQYTSNITAPSSPHIYQVYSLHNVEFHEDSHTQFLKSSPKFTGTVQPTVLTKSLSKDSSFSSTKSLPDLLGGSSLVRPYSCQSGDLSQNSGSESGIVSEGDNEMPTNSDMSLFSMVDGSPSNPETQHLDPQMGDAANVLEQKFKDEGECIKLSSVSQASVSPVGCVNGKAGDLNSITKHTTDCLGDELQGKHEVFTFYDYSYLQGSKLKFPMIMKQPQSEKAHLEDPLLRGFYFDKKSCKPKHQTSESQPDAPLHEKILASAPHEMGRSSYKSSDIEKALTGIQNARQLSLLSRSSSVESLSPGGDLFGLGIFKNGSDSLQRSTSLESWLTSYKSNEDLFSCHSSGDISVSSGSVGELSKRTLDLLNRLENIQSPSEQKIKRSVSDITLQSSSQKMSFSGQMSLDVASSINEDSPASLTELSSSDELSLCSEDIVLHKNKVPESNASFRKRLNRSVADESDVNVSMIVNVSCTSACTDDEDDSDLLSSSTLTLTEEELCLKDEDDDSSIATDDEIYEESNLMSGLDYIKNELQTWIRPKLSLSREKKRPSVTDEIKVNKDGGSTERANPSDTLDIEALLNCSIKRLSENNGNGKNPPRTHDLGTKGENKKNTYDVTKDPHVADMENGNVESTPEREKEKPEIPEASANLASNVKKISESKHDEYEALMDGSDDSSVTGKEFGPPNDRHPPQIGADPQHPERGDCTSVQNSCSGLLLETGGGSRQDSDGLKSLSNDAPSVARNAAGCCLLEQNETEESASISSSTSCCNCKPDVFHQKDDEDCSVHDFVKEIIDMASTALKSKSQPESEVAAPTSLTQIKEKVLEHSHRPIHLRKGDFYSYLSLSSHDSDCGEVTNYIDEKSNTPLPPDTVDSGLDDKEDVDCFFEACVEDEPADEEARLSSALPNESEVQDEAAKPEQMTASSSVFRDETDTVPLSGLSPQKGADDAKEGDGASHTSQGCVESAEPTTPPGKAKREGSSRKQSVSGTPEENAASAKPKIQAFSLNAKQPKGKAALYPSPQTLTCKEKLVSFHEDRHSNMHR
Protein: FMRFamide-like neuropeptides 13 [Cleaved into: SDRPTRAMDSPLIRF-amide; AMDSPLIRF-amide; AADGAPLIRF-amide 1; APEASPFIRF-amide 1; AADGAPLIRF-amide 2; APEASPFIRF-amide 2; ASPSAPLIRF-amide; SPSAVPLIRF-amide; SAAAPLIRF-amide; ASSAPLIRF-amide] (O44185)
Organism: Caenorhabditis elegans
Function: Probable FMRFamide-like neuropeptides. Binds to neuronal receptors such as dmsr-1 to promote sleep in response to cellular stress also known as stress-induced sleep (SIS). Plays a role in behaviors associated with SIS, acting in concert with the FMRFamide related peptide, flp-24 and neuropeptide-like protein nlp-8.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- FMRFamide-like neuropeptides 24
- FMRFamide-like neuropeptides 11
- Neuropeptide-like protein nlp-8
- FMRFamide-like neuropeptide 18
- FMRFamide-like neuropeptides 9
- FMRFamide-like neuropeptides 5
- FMRFamide-like neuropeptides 19
- FMRFamide-like neuropeptides 1
- G-protein coupled receptor dmsr-1
- FMRFamide-like neuropeptides 14
Sequence:
MMTSLLTISMFVVAIQAFDSSEIRMLDEQYDTKNPFFQFLENSKRSDRPTRAMDSPLIRFGKRAADGAPLIRFGRAPEASPFIRFGKRAADGAPLIRFGRAPEASPFIRFGKRASPSAPLIRFGRSPSAVPLIRFGRSAAAPLIRFGRASSAPLIRFGRK