wanglab/gogpt-training-data huggingface dataset:
Protein: tRNA pseudouridine synthase 1 (EC 5.4.99.-) (tRNA pseudouridylate synthase 1) (tRNA-uridine isomerase 1) (Q12211)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Formation of pseudouridine at positions 27 and 28 in the anticodon stem and loop of transfer RNAs; at positions 34 and 36 of intron-containing precursor tRNA(Ile) and at position 35 in the intron-containing tRNA(Tyr). Catalyzes pseudouridylation at position 44 in U2 snRNA. Also catalyzes pseudouridylation of mRNAs.
Subcellular location: Nucleus {ECO:0000269|PubMed:11502169}.
Interaction partners:
- tRNA pseudouridine synthase 4
- Multisubstrate pseudouridine synthase 7
- tRNA
- H/ACA ribonucleoprotein complex subunit CBF5
- tRNA pseudouridine
- tRNA-dihydrouridine
- tRNA pseudouridine
- tRNA
- tRNA
- Bifunctional protein RIB2
Sequence:
MSEENLRPAYDDQVNEDVYKRGAQSKLTKARKADFDDEKDKKKDNDKHIDKRPKSGPRLDENGNPLPKEPRLPKRKVAVMVGYCGTGYHGMQYNPPNPTIESALFKAFVEAGAISKDNSNDLKKNGFMRAARTDKGVHAGGNLISLKMIIEDPDIKQKINEKLPEGIRVWDIERVNKAFDCRKMCSSRWYEYLLPTYSLIGPKPGSILYRDIEESKTELPGVLDEDLESKEFWEEFKKDANEKFSTEEIEAILAYVPPARDEFDINEELYQKVKKYKQLENAHRRRYRISAAKLAKFRASTSQYLGAHNFHNFTLGKDFKEPSAIRFMKDIKVSDPFVIGDAQTEWISIKIHGQSFMLHQIRKMVSMATLITRCGCPVERISQAYGQQKINIPKAPALGLLLEAPVFEGYNKRLEQFGYKAIDFSKYQDEVDKFKMKHIYDKIYKEEVDENVFNAFFSYIDSFNKVTGAQGEETADKSGPAVQKSIFEFLTAKGIPGLTDAPESNKKIKQRKRMEEEEAASKKAEISSTTQSNEPEVQPEAAAN
Protein: At2g03640 (Nuclear transport factor 2 (NTF2) family protein with RNA binding (RRM-RBD-RNP motifs) domain-containing protein) (Q8GW56)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MTPESNAPSVDPQFVGNGFVQEYYNHLYDSTSEVHKFYLEDSMISRPGLDGEIVTIKSLKGINDQIMSIDYKSSRIEILTADSQSTLKNGVVTLVTGLVIGNDGGRRKFSQSFFLVSRNGSYFVLNDTFRYVSDEFVEPEATKEVEESQSTNAITEPANESVEAVIVPTEAKTTVTKPASAIPNGHAKVPEEKVVNENSSLPKAAEAKLQEEVPKKSFALIVQSLAQSAGTLQVKASPVKRKPVEKPVAAPERKAPSPIRKQASAESIKPQAQGSSIFVANLPMDATIEQLYETFKSFGAIRKDGIQVRSYPEKKNCIGFVAFENGEAVKNVFQAHRESPIRIGNRRASIEEKRGGNNQNGNRVSTRNNSGYKNEDGFRRDGYKPRGSGVNGGRGYGRRNSESNGDGKAYQNNGHGNTEAKN
Protein: Protein 4.1 (Band 4.1) (Erythrocyte membrane protein band 4.1) (A0A2R8Y570)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cell cortex {ECO:0000256|ARBA:ARBA00004544}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MTTEKSLVTEAENSQHQQKEEGEEAINSGQQEPQQEESCQTAAEGDNWCEQKLKASNGDTPTHEDLTKNKERTSESRGLSRLFSSFLKRPKSQVSEEEGKEVESDKEKGEGGQKEIEFGTSLDEEIILKAPIAAPEPELKTDPSLDLHSLSSAETQPAQEELREDPDFEIKEGEGLEECSKIEVKEESPQSKAETELKASQKPIRKHRNMHCKVSLLDDTVYECVVEKHAKGQDLLKRVCEHLNLLEEDYFGLAIWDNATSKTWLDSAKEIKKQVRGVPWNFTFNVKFYPPDPAQLTEDITRYYLCLQLRQDIVAGRLPCSFATLALLGSYTIQSELGDYDPELHGVDYVSDFKLAPNQTKELEEKVMELHKSYRSMTPAQADLEFLENAKKLSMYGVDLHKAKDLEGVDIILGVCSSGLLVYKDKLRINRFPWPKVLKISYKRSSFFIKIRPGEQEQYESTIGFKLPSYRAAKKLWKVCVEHHTFFRLTSTDTIPKSKFLALGSKFRYSGRTQAQTRQASALIDRPAPHFERTASKRASRSLDGAAAVDSADRSPRPTSAPAITQGQVAEGGVLDASAKKTVVPKAQKETVKAEVKKEDEPPEQAEPEPTEAWKVEKTHIEVTVPTSNGDQTQKLAEKTEDLIRMRKDLDKSQEEIKKHHASISELKKNFMESVPEPRPSEWDKRLSTHSPFRTLNINGQIPTGEGVKKTSVLPSERKVGGPESPSYFLPDTYHLGVCKEPVLNFQTDQRRLAQLRELRAKFFLS
Protein: Gustatory and pheromone receptor 39a, isoform A (P58959)
Organism: Drosophila melanogaster (Fruit fly)
Function: Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates. Plays a role in sustaining courtship behavior in males, possibly through the reception of a stimulating arrestant pheromone.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MSKVCRDLRIYLRLLHIMGMMCWHFDSDHCQLVATSGSERYAVVYAGCILVSTTAGFIFALLHPSRFHIAIYNQTGNFYEAVIFRSTCVVLFLVYVILYAWRHRYRDLVQHILRLNRRCASSCTNQQFLHNIILYGMLTILCFGNYLHGYTRAGLATLPLALCMLVYIFAFLVLCLLLMFFVSLKQVMTAGLIHYNQQLCQGDLISGLRGRQQILKLCGGELNECFGLLMLPIVALVLLMAPSGPFFLISTVLEGKFRPDECLIMLLTSSTWDTPWMIMLVLMLRTNGISEEANKTAKMLTKVPRTGTGLDRMIEKFLLKNLRQKPILTAYGFFALDKSTLFKLFTAIFTYMVILVQFKEMENSTKSINKF
Protein: Potassium channel domain-containing protein (Q3TQ68)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
ELGTLREQLLQHSPCVAAHALDAFVERVLAAGRLGRAALANASGAANASDPAWDFASALFFASTLVTTVGYGYTTPLTDAGKAFSIVFALLGVPITMLLLTASAQRLSLLLTHAPLSWLSLHWGWPPQRAARWHLVALLMVIVAIFFLVPAAVFAYLEEAWSFLDAFYFCFISLSTIGLGDYVPGEAPGQPYRALYKVLVTAYLFLGLVAMVLVLQTFRRVSDLHGLTELILLPDPDPASLSQDEDDQVAVLDARTDLHQHLSAASHADYASIPR
Protein: Deoxyadenosine kinase (EC 2.7.1.76) (DddDAK) (DAK) (Q54YL2)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Specific kinase that phosphorylates deoxyadenosine but not any other deoxyribonucleoside, as part of the deoxyribonucleotide salvage pathway.
Interaction partners:
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH-ubiquinone oxidoreductase subunit 9
- NADH-ubiquinone oxidoreductase 23 kDa subunit
- NADH-ubiquinone oxidoreductase 49 kDa subunit
- Acyl carrier protein, mitochondrial
- Probable adenylate kinase B
- Adenylate kinase
- NADH-ubiquinone oxidoreductase 75 kDa subunit
- NADH dehydrogenase 1 alpha subcomplex subunit 6
- Cytosolic purine 5'-nucleotidase
Sequence:
MTTPILNSSVPGNIQKKSLEGTHIAISGLIGAGKTTLAVALGKVLNLPTYFEEVIDNLYLQDFYKDPKKYGFQLQIYLLNSRFQQQQQIIWQARGGVQDRTIYEDSVFAKMLNESGLLDDRDYNTYCKLFQNLSNFMRRPDLIIHLDVSPEKSLERIKLRNRDCEKDVSLEYLQNLYNAYHEFLQDISRYIPVIRINWSEFVDPEQLAQMIKAEYESMRFMNQINPPTFGNGPTTNKIISTPKDL
Protein: 60S ribosomal export protein nmd3 (Q09817)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Acts as an adapter for the XPO1/CRM1-mediated export of the 60S ribosomal subunit.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Note=Shuttles between the nucleus and the cytoplasm in a XPO1/CRM1-dependent manner. {ECO:0000250}.
Interaction partners:
- Probable metalloprotease arx1
- Eukaryotic translation initiation factor 6
- Probable nucleolar GTP-binding protein 1
- Ribosome biogenesis protein rlp24
- Zinc finger protein bud20
- Cytoplasmic 60S subunit biogenesis factor SPCC550.15c
- Large subunit GTPase 1
- Ribosome biogenesis protein nsa2
- Ribosome assembly factor mrt4
- GTPase grn1
Sequence:
MDMDSGSMGVAFQPSEPIASTILCCECGVPTPPNAAAMCMDCIKMTTDITSGIPRESTVNHCRECERYMQPPNNWMIAPLESRELMAICLKKLRGLNQVRLVDANFIWTEPHSRRIKVKLTVQKEAFTNTILQQSFQVEFYVNNTQCPDCARTYTPHIWKAVCQVRQKVLHKRTFLYLEQIILKHKAHMNTVNIKETKDGIDFYFGQRAHAIKMVEFLSAVVPIRYKGSEELISEDFKSNTANYKFTYSIEIVPICKDDLVCLPKTVAKAHGNIAQLVVCTKVGPTIRFLDPLTLQTCDMLPSIYWRTPFPALADIPELTEFIVADVDLLGPTNGKYALADVELIKSSDGSTHLTRTHLGGILNAGNTVLAYHLAVTNFNNEVYDTLREDSIPEVVIVKKTYPQTKKKNRNWRLKTIGMQKAEDVKKQDIERQERDYELFLQNLEEDPELRQGVNLYKAPVKAIAVADTDMDEEDEVDEDIPQISVDELLDDVEAMHI
Protein: Copal-8-ol diphosphate hydratase, chloroplastic (EC 4.2.1.133) (8-hydroxy-copalyl diphosphate synthase) (G3CCC0)
Organism: Nicotiana tabacum (Common tobacco)
Function: Class-II terpene synthase that synthesizes 8-hydroxy-copalyl diphosphate. Involved in the biosynthesis of cis-abienol, a labdane diterpene that can be used as synthesis precursor of ambergris substitution fragance products.
Subcellular location: Plastid, chloroplast {ECO:0000250}.
Interaction partners:
- Diphosphomevalonate decarboxylase
- Diphosphomevalonate decarboxylase
- Diphosphomevalonate decarboxylase
- Diphosphomevalonate decarboxylase
- Terpene cyclase/mutase family member
- isopentenyl-diphosphate Delta-isomerase
- isopentenyl-diphosphate Delta-isomerase
- isopentenyl-diphosphate Delta-isomerase
- isopentenyl-diphosphate Delta-isomerase
- isopentenyl-diphosphate Delta-isomerase
Sequence:
MQVIITSSHRFFCHHLHQLKSPTSLSAQKAEFKKHGPRNWLFQTEGSLLYKPVRLNCATSDASYLGNVNEYLESDHSKNSEEKDIQVSRTIQMKGLTEEIKHMLNSMEDGRLNVLAYDTAWVSFIPNTTNNGNDQRPMFPSCLQWIIDNQLSDGSWGEEIVFCIYDRLLNTLVCVIALTLWNTCLHKRNKGVMFIKENLSKLETGEVENMTSGFELVFPTLLEKAQQLDIDIPYDAPVLKDIYARREVKLTRIPKDVIHTIPTTVLFSLEGLRDDLDWQRLLKLQMPDGSFLISPASTAFAFMETNDEKCLAYLQNVVEKSNGGARQYPFDLVTRLWAIDRLQRLGISYYFAEEFKELLNHVFRYWDEENGIFSGRNSNVSDVDDTCMAIRLLRLHGYDVSPDALNNFKDGDQFVCFRGEVDGSPTHMFNLYRCSQVLFPGEKILEEAKNFTYNFLQQCLANNRCLDKWVIAKDIPGEIWYALEFPWYASLPRVEARYYIEQYGGADDIWIGKTLYRMPDVNNNVYLQAAKLDYNRCQSQHRFEWLIMQEWFEKCNFQQFGISKKYLLVSYFLAAASIFEVEKSRERLAWAKSRIICKMITSYYNDEATTWTTRNSLLMEFKVSHDPTRKNGNETKEILVLKNLRQFLRQLSEETFEDLGKDIHHQLQNAWETWLVFLREEKNACQEETELLVRTINLSGGYMTHDEILFDADYENLSNLTNKVCGKLNELQNDKVTGGSKNTNIELDMQALVKLVFGNTSSNINQDIKQTFFAVVKTFYYSAHVSEEIMNFHISKVLFQQV
Protein: Protein jagunal homolog 1 (Q8N5M9)
Organism: Homo sapiens (Human)
Function: Endoplasmic reticulum transmembrane protein involved in vesicle-mediated transport, which is required for neutrophil function. Required for vesicle-mediated transport; it is however unclear whether it is involved in early secretory pathway or intracellular protein transport. Acts as a regulator of neutrophil function, probably via its role in vesicle-mediated transport: required for defense against fungal pathogens and for granulocyte colony-stimulating factor (GM-CSF) signaling pathway; possibly by regulating glycosylation and/or targeting of proteins contributing to the viability and migration of neutrophils.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:25129144}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MASRAGPRAAGTDGSDFQHRERVAMHYQMSVTLKYEIKKLIYVHLVIWLLLVAKMSVGHLRLLSHDQVAMPYQWEYPYLLSILPSLLGLLSFPRNNISYLVLSMISMGLFSIAPLIYGSMEMFPAAQQLYRHGKAYRFLFGFSAVSIMYLVLVLAVQVHAWQLYYSKKLLDSWFTSTQEKKHK
Protein: Ferric uptake regulation protein (B5Z6G7)
Organism: Helicobacter pylori (strain G27)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MKRLETLESILERLRMSIKKNGLKNSKQREEVVSVLYRSGTHLSPEEITHSIRQKDKNTSISSVYRILNFLEKENFICVLETSKSGRRYEIAAKEHHDHIICLHCGKIIEFADPEIENRQNEVVKKYQAKLISHDMKMFVWCKECQESEY
Protein: PHISTb domain-containing RESA-like protein 1 (O96121)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKTYNRNNNCLSQNILDNKNIINCVNPMTMCSDNKYEEDEKRKGISLNISKCRYFLLPIVGILYIILLNILAFEGNLSTNIQFKNTFKRNLSSKEPSLDDFFKFYKKNSYKLSESFMDTKNMLTKKMKIEKSAFNKYSHLFTSLFNYDLWERFEISYYMLSGNSEYTNDLDLEINKKLVLLNNETNSELRIHTIWHNVMKSEKEKFNSWYMYFNNNFYLLRKKYKTPFNYAKPTCNQCNEFFALSKKYIENSFNKVFNKWFKNNVYLDVNEFRVIVMACRLLWRKTLATLKEEGMLYLQKPFEALHHERKKIHKRGGRALKFKAEEFYEKNPDLVTYKGCHFLNSLKNVNLEEKYDDDDEAENEKKKQEKIKDNKKEEEDAYEDNEDNEDYDDYDDYDDYDEEQYDKNGEVIVGANEDPSYEYNYHYEEPFILTPELIEAIERAVERDVEREVEKRSEKLIDDKWKKRLAKEIRDKPIKKVRFNL
Protein: Growth hormone secretagogue receptor type 1 (GH-releasing peptide receptor) (Ghrelin receptor) (A8CGH1)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MRSWPNRTDCLSPVNCSWEDNYWNYYFNGSYQGPVPPENLFPIPVLMGITITCTLLFLAGVAGNVMTILVVSKYRDMRTTTNLYLCSMAVSDLLIFLCMPPDVYRLWKYRPWIFGDTFCKLFQFVSECCTYSTILNITALSVERYLAICFPLRAKRLVTKRRVRALILFLWLVSLLSAGPVFVLVGVEHETRPAAGNSVTAGGAEGQTEIDTSECKPTQYAVESGLLAAMALVSSVFFFLPVFCLTVVYSLIGRRLWKRRRENNIGANVAHRDKSNRQTVKMLAVVVFAFVLCWLPFHLHRYLMSHSSEGSSPLWSLFTQYCSLVSTVLFYLSAAINPVLYNTMSRKYRSAAAQLFGLQETQPPRGRTASTVKGESSPAWTESTVSL
Protein: Pre-mRNA-splicing factor SYF1 (Q57VC9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- PRP8 protein homologue
- U5 small nuclear ribonucleoprotein component, putative
- Uncharacterized protein
- Pre-mRNA-splicing factor Syf1-like N-terminal HAT-repeats domain-containing protein
- Spliceosome-associated protein, putative
- G10 protein
- RNA helicase
- Pre-mRNA-processing factor 19
- Uncharacterized protein
- Cell division control protein, putative
Sequence:
MGTTSTDTLELEVLRNPSNVRGWLQFIRSILCSDYPNQVSKANAVNVAYERALRANGYSYKLWMGYISYRRENTRELTSPNEWFRSLRDIYDRAVEKLPMMPLLWTSFIEFAMDGSVAPRITLTRHVITRALEALPFTQHHRIWRLAKLWVSRPHVPMPTATYIWRLYLLYDPSTENQRNYFHMLWEKGNASDFLVECAAFLLRDSTSHGGLLRDIAFWETVRTALETKGLCFGGDISQVEKIVQMAADYCASPAEFRLSYAVFLANQGELSMARETLWAILNDVDNPAVFCRAFTAALAFESQIIDSLAMDSSIHALDEVKYQQLREKLCGDVPDPLYHLTRLTQQHPMLLNQLQLRADRHCTALWLKRIEILKEMECNGVATSSDVIALYRQAITQCTSGMPNVEAATAQLFESYACYLWENNLRTDAVTVADEGAWFVKFSSTTSNVLLMGLVVEFSQLTDPARTLDKLVSRLVKATNVSNSIRSKGLARQVVVKNLARDPRAWVLAVDVAFHRLLLKNTGESGGRSNEELKNLISLFCNSSGYTAEGACYVACRLWQSGDVSAAFQEFERALVAFAAAPLAVLHILQQYLSCLCVSFGTRLPLHRFREFSKLGLDVAQFTMRSSPVSTMEFLLNCVTLESRLGFSGSAVQIARECLHLALKHQAEYDSLLFGVLDAVLEVTFRLHGSQALRHYCAELLERQKLTPQLIQRLALWWAAVERRTGNADRAHTVMEACCKSQDPSSSHGAVFWSMWESICNTVKQFEGVHRRKQQAALKYSSGNNSADAAVDGVDGNKNNNVGASGNEAIEVVPVPALT
Protein: Inactive CLIP domain-containing serine protease A30 (Inactive CLIP domain-containing serine protease SPCLIP1) (A0A1S4HE51)
Organism: Anopheles gambiae (African malaria mosquito)
Function: Probable inactive serine protease which plays an essential role in the innate immune response against bacteria and protozoa infection by activating the melanization cascade. Binds to the surface of parasite P.berghei ookinetes and bacterium E.coli where it promotes the accumulation of mature TEP1 which leads to the melanization of the microbe.
Subcellular location: Secreted {ECO:0000269|PubMed:24039584, ECO:0000269|PubMed:33045027}. Note=Secreted into the hemolymph. {ECO:0000269|PubMed:24039584, ECO:0000269|PubMed:33045027}.
Interaction partners:
Sequence:
MAFSLRIGIRTTDSKRCLVLLVLVVLLTVLACLPPSVEGNFPVGKFRRCNNNKGICVSREQCLNGQINTVGHTQIEPRLLNDDDIDECDVYGMQCCNLPSTNVPADSDEEEQEEEEKEKKGGTVTTTTTEEPDDPDWSRQCGQRTDVTERADQDGETNRFEFPWSVALFSKAQFFGKVRKEFLCGGTLIDDYLVLTAARCVNQKDRNTLVVQLGRWNLDAGKESRMQEIAVEELIIHRGYVLSSHLHNVALLVLANGAQLGRAANRVCLPDHSVQFGPDTLCYVVGWSNSPSPNTSNRQLKLRSMVAPVQECTATIRRSTGAWDFRLLSENICTTYLDDTVPCERAPGSGFVCESPTLPGQYFLVGIASYAVRQCHKYRAHDVFVHVPDYIEWVDGHVVNQSRQTSFYRPDPISFD
Protein: Clavesin-2 (Retinaldehyde-binding protein 1-like 2) (A6JUQ6)
Organism: Rattus norvegicus (Rat)
Function: Required for normal morphology of late endosomes and/or lysosomes in neurons. Binds phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2).
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:19651769}; Peripheral membrane protein {ECO:0000269|PubMed:19651769}. Early endosome membrane {ECO:0000250|UniProtKB:Q8IUQ0}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8IUQ0}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:19651769}.
Interaction partners:
- von Willebrand factor C domain containing 2
- Coiled-coil domain-containing protein 175
Sequence:
MTHLQAGLSPETLEKARLELNENPDTLHQDIQEVRDMVITRPDIGFLRTDDAFILRFLRARKFHHFEAFRLLAQYFEYRQQNLDMFKSFKATDPGIKQALKDGFPGGLANLDHYGRKILVLFAANWDQSRYTLVDILRAILLSLEAMIEDPELQVNGFVLIIDWSNFTFKQASKLTPSMLRLAIEGLQDSFPARFGGIHFVNQPWYIHALYTVIRPFLKEKTRKRIFLHGNNLNSLHQLIHPEILPSEFGGMLPPYDMGTWARTLLDHEYDDDSEYNVDSYSMPVNEVDKELSPKSMKRSQSVVDPTALKRMDKSEEENMQPLLSLD
Protein: Palmitoyltransferase ZDHHC6 (EC 2.3.1.225) (Stearoyltransferase ZDHHC6) (EC 2.3.1.-) (Transmembrane protein H4) (Zinc finger DHHC domain-containing protein 6) (DHHC-6) (Zinc finger protein 376) (Q9H6R6)
Organism: Homo sapiens (Human)
Function: Endoplasmic reticulum palmitoyl acyltransferase that mediates palmitoylation of proteins such as AMFR, CALX, ITPR1 and TFRC. Palmitoylates calnexin (CALX), which is required for its association with the ribosome-translocon complex and efficient folding of glycosylated proteins. Mediates palmitoylation of AMFR, promoting AMFR distribution to the peripheral endoplasmic reticulum. Together with SELENOK, palmitoylates ITPR1 in immune cells, leading to regulate ITPR1 stability and function. Stearoyltransferase that mediates stearoylation of TFRC to inhibit TFRC-mediated activation of the JNK pathway and mitochondrial fragmentation.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21926431, ECO:0000269|PubMed:22314232, ECO:0000269|PubMed:28826475}; Multi-pass membrane protein {ECO:0000255}. Note=When not palmitoylated, accumulates to dot-like structures in the endoplasmic reticulum (PubMed:28826475). {ECO:0000269|PubMed:28826475}.
Interaction partners:
- Selenoprotein K
Sequence:
MGTFCSVIKFENLQELKRLCHWGPIIALGVIAICSTMAMIDSVLWYWPLHTTGGSVNFIMLINWTVMILYNYFNAMFVGPGFVPLGWKPEISQDTMYLQYCKVCQAYKAPRSHHCRKCNRCVMKMDHHCPWINNCCGYQNHASFTLFLLLAPLGCIHAAFIFVMTMYTQLYHRLSFGWNTVKIDMSAARRDPLPIVPFGLAAFATTLFALGLALGTTIAVGMLFFIQMKIILRNKTSIESWIEEKAKDRIQYYQLDEVFVFPYDMGSRWRNFKQVFTWSGVPEGDGLEWPVREGCHQYSLTIEQLKQKADKRVRSVRYKVIEDYSGACCPLNKGIKTFFTSPCTEEPRIQLQKGEFILATRGLRYWLYGDKILDDSFIEGVSRIRGWFPRKCVEKCPCDAETDQAPEGEKKNR
Protein: Glycosylphosphatidylinositol anchor attachment 1 (A0A8I5ZZA0)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MGLLSDPVRRRALARIVLRLNTPLWALPVAWLERAMRSVGLEVYTQSFSRKLPFPDETHERYMVSGTNVYGILRAPRAASTESLVLTVPCGPDTTNSQAVGLLLALAAHFRGQIYWAKDIIFLVTEHDLLGTEAWLEAYHDINVTGIQSSPLQGRAGAIQAAVALELSSDVVTSLDVTVEGLNGQLPNLDLLNLFQTFCQKGGLLCTLQGKLQPQDWTSLEGPLQGLQTLLLMVLRQASGRPHGPHGLFLRYGVEALTLRGINSFRQYKYDLVAVGKALEGMFRKLNHLLERLHQSFFFYLLPALSRFVSIGLYMPATGFLLLVLGLKALELWMQLHEAGVNPEEAGKAPGPGSPPLATQSVSLASLMAPLLISQAMGLALYFLPVLGQHVAAQHFPVAEAEAVVLTLLAIYVAGLALPHNTHRVVSSQVPDRGWMALKLVALIYLALQLGCIALLNFSLGFLLAATMVPAAALTKPHGPRTLYAALLVVTSPAVTLFGSLFLWRELQEVPLSLAEGWQLFLTALAQGVLEHYTYGALLFPILALGLYPCWLLFWNVLFWK
Protein: Rhomboid-like protein 11, chloroplastic (AtRBL11) (EC 3.4.21.-) (Q84MB5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Rhomboid-type serine protease that catalyzes intramembrane proteolysis. May be involved in TIC22 processing during its import.
Subcellular location: Plastid, chloroplast inner membrane {ECO:0000269|PubMed:18543065, ECO:0000269|PubMed:22738221}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- RHOMBOID-like protein 4
- RHOMBOID-like protein 10, chloroplastic
- RHOMBOID-like protein 9, chloroplastic
- RHOMBOID-like protein 12, mitochondrial
- Rhomboid-like protein 17, chloroplastic
- Rhomboid-like protein 15
- RHOMBOID-like protein 13
- RHOMBOID-like protein 1
- Rhomboid-like protein 16, chloroplastic
- Rhomboid-like protein 14, mitochondrial
Sequence:
MSQLLHLHRLSLPQSSLRFRFPPLHRRRAASSPTNSTQPPLQFRPLTVSRSQITCRFSQSDITPQFELDKAKDNRKPQKRANGIFWIILINLGIYLADHFFQVRGIKSLYLYHNFPAWYQFVTATFCHANWNHLSSNLFFLYIFGKLVEEEEGNFGLWLSYLFTGVGANLVSWLVLPRNAVSVGASGAVFGLFAISVLVKMSWDWRKILEVLILGQFVIERVMEAAQASAGLSGTIYGGYSLQTVNHIAHLSGALVGVVLVWLLSKFPSASMDQDVKKSS
Protein: Scm-like with four MBT domains protein 2 (Scm-like with 4 MBT domains protein 2) (Q5VUG0)
Organism: Homo sapiens (Human)
Function: Transcriptional repressor of HOXB13 gene.
Subcellular location: Nucleus {ECO:0000269|PubMed:23385818}.
Interaction partners:
- Sodium-coupled neutral amino acid transporter 4
Sequence:
MESTLSASNMQDPSSSPLEKCLGSANGNGDLDSEEGSSLEETGFNWGEYLEETGASAAPHTSFKHVEISIQSNFQPGMKLEVANKNNPDTYWVATIITTCGQLLLLRYCGYGEDRRADFWCDVVIADLHPVGWCTQNNKVLMPPDAIKEKYTDWTEFLIRDLTGSRTAPANLLEGPLRGKGPIDLITVGSLIELQDSQNPFQYWIVSVIENVGGRLRLRYVGLEDTESYDQWLFYLDYRLRPVGWCQENKYRMDPPSEIYPLKMASEWKCTLEKSLIDAAKFPLPMEVFKDHADLRSHFFTVGMKLETVNMCEPFYISPASVTKVFNNHFFQVTIDDLRPEPSKLSMLCHADSLGILPVQWCLKNGVSLTPPKGYSGQDFDWADYHKQHGAQEAPPFCFRNTSFSRGFTKNMKLEAVNPRNPGELCVASVVSVKGRLMWLHLEGLQTPVPEVIVDVESMDIFPVGWCEANSYPLTAPHKTVSQKKRKIAVVQPEKQLPPTVPVKKIPHDLCLFPHLDTTGTVNGKYCCPQLFINHRCFSGPYLNKGRIAELPQSVGPGKCVLVLKEVLSMIINAAYKPGRVLRELQLVEDPHWNFQEETLKAKYRGKTYRAVVKIVRTSDQVANFCRRVCAKLECCPNLFSPVLISENCPENCSIHTKTKYTYYYGKRKKISKPPIGESNPDSGHPKPARRRKRRKSIFVQKKRRSSAVDFTAGSGEESEEEDADAMDDDTASEETGSELRDDQTDTSSAEVPSARPRRAVTLRSGSEPVRRPPPERTRRGRGAPAASSAEEGEKCPPTKPEGTEDTKQEEEERLVLESNPLEWTVTDVVRFIKLTDCAPLAKIFQEQDIDGQALLLLTLPTVQECMELKLGPAIKLCHQIERVKVAFYAQYAN
Protein: Nucleoside permease NupC (Nucleoside-transport system protein NupC) (P0AFF2)
Organism: Escherichia coli (strain K12)
Function: Nucleoside transport protein that can transport adenosine, uridine, thymidine, cytidine and deoxycytidine. Shows weak activity with inosine and xanthosine. Transport is driven by a proton motive force. Does not transport guanosine, deoxyguanosine, hypoxanthine or uracil. Also shows activity with the chemotherapeutic drugs 3'-azido-3'-deoxythymidine (AZT), 2',3'- dideoxycytidine (ddC) and 2'-deoxy-2',2'-difluorocytidine (gemcitabine).
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:8022285}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Nucleoside permease NupG
- Nucleoside-specific channel-forming protein Tsx
- Xanthosine permease
Sequence:
MDRVLHFVLALAVVAILALLVSSDRKKIRIRYVIQLLVIEVLLAWFFLNSDVGLGFVKGFSEMFEKLLGFANEGTNFVFGSMNDQGLAFFFLKVLCPIVFISALIGILQHIRVLPVIIRAIGFLLSKVNGMGKLESFNAVSSLILGQSENFIAYKDILGKISRNRMYTMAATAMSTVSMSIVGAYMTMLEPKYVVAALVLNMFSTFIVLSLINPYRVDASEENIQMSNLHEGQSFFEMLGEYILAGFKVAIIVAAMLIGFIALIAALNALFATVTGWFGYSISFQGILGYIFYPIAWVMGVPSSEALQVGSIMATKLVSNEFVAMMDLQKIASTLSPRAEGIISVFLVSFANFSSIGIIAGAVKGLNEEQGNVVSRFGLKLVYGSTLVSVLSASIAALVL
Protein: Choriogonadotropin subunit beta variant 1 (A6NKQ9)
Organism: Homo sapiens (Human)
Subcellular location: Secreted.
Interaction partners:
Sequence:
MSTFPVLAEDIPLRERHVKGRVDPHFRAPKMEMFQRLLLLLLLSMGGTWASKEPLRPRCRPINATLAVEKEGCPVCITVNTTICAGYCPTMTRVLQGVLPALPQVVCNYRDVRFESIRLPGCPRGVNPVVSYAVALSCQCALCRRSTTDCGGPKDHPLTCDDPRFQDSSSSKAPPPSLPSPSRLPGP
Protein: DNA-binding protein SATB (Special AT-rich sequence-binding protein) (D3ZJ19)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
- T-box brain transcription factor 1
- BCL11 transcription factor B
- Homeobox protein cut-like 1
- Zinc finger protein 312
- Paired box protein Pax-6
- Transcription factor SOX-5
- Homeobox protein cut-like
- Neurogenic differentiation factor.
- Empty spiracles homeobox 1
- POU domain, class 3, transcription factor 2
Sequence:
MERRSESPCLRDSPDRRSGSPDVKGPPPVKVARLEQNGSPMGARGRPNGAVAKAVGGLMIPVFCVVEQLDGSLEYDNREEHAEFVLVRKDVLFSQLVETALLALGYSHSSAAQAQVERVERENLSDYCVLGQRPMHLPNMNQLASLGKTNEQSPHSQIHHSTPIRNQVPALQPIMSPGLLSPQLSPQLVRQQIAMAHLINQQIAVSRLLAHQHPQAINQQFLNHPPIPRAVKPEPTNSSVEVSPDIYQQVRDELKRASVSQAVFARVAFNRTQGLLSEILRKEEDPRTASQSLLVNLRAMQNFLNLPEVERDRIYQDERERSMNPNVSMVSSASSSPSSSRTPQAKTSTPTTDLPIKVDGANVNITAAIYDEIQQEMKRAKVSQALFAKVAANKSQGWLCELLRWKENPSPENRTLWENLCTIRRFLNLPQHERDVIYEEESRHHHSERMQHVVQLPPEPVQVLHRQQSQPTKESSPPREEAPPPPPPTEDSCAKKPRSRTKISLEALGILQSFIHDVGLYPDQEAIHTLSAQLDLPKHTIIKFFQNQRYHVKHHGKLKEHLGSAVDVAEYKDEELLTESEENDSEEGSDEMYKVEAEEESAEKNKVAPAETDQR
Protein: Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL (RPnTP synthase subunit PhnL) (EC 2.7.8.37) (P16679)
Organism: Escherichia coli (strain K12)
Function: Together with PhnG, PhnH and PhnI is required for the transfer of the ribose triphosphate moiety from ATP to methyl phosphonate.
Interaction partners:
- Alpha-D-ribose 1-methylphosphonate 5-phosphate C-P lyase
- Alpha-D-ribose 1-methylphosphonate 5-triphosphate diphosphatase
- Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnH
- Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnI
- Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnG
- Putative phosphonates utilization ATP-binding protein PhnK
- Ribose 1,5-bisphosphate phosphokinase PhnN
- Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase
- Probable transcriptional regulator PhnF
- Phosphonates-binding periplasmic protein
Sequence:
MINVQNVSKTFILHQQNGVRLPVLNRASLTVNAGECVVLHGHSGSGKSTLLRSLYANYLPDEGQIQIKHGDEWVDLVTAPARKVVEIRKTTVGWVSQFLRVIPRISALEVVMQPLLDTGVPREACAAKAARLLTRLNVPERLWHLAPSTFSGGEQQRVNIARGFIVDYPILLLDEPTASLDAKNSAAVVELIREAKTRGAAIVGIFHDEAVRNDVADRLHPMGASS