wanglab/gogpt-training-data huggingface dataset:
Protein: Homeobox-leucine zipper protein HDG7 (HD-ZIP protein HDG7) (Homeodomain GLABRA 2-like protein 7) (Homeodomain transcription factor HDG7) (Protein HOMEODOMAIN GLABROUS 7) (Q9LTK3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor that binds to the DNA sequence 5'-GCATTAAATGC-3'. Seems to promote cell differentiation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Nucleoid-associated protein At4g30620
- Transmembrane protein
- Probable long-chain-alcohol O-fatty-acyltransferase 6
- KIB1-4 beta-propeller domain-containing protein
- 60S ribosomal L18a-like protein
- At5g64430
- AT5g54630/MRB17_13
- Homeobox-leucine zipper protein ATHB-23
- At5g62770)
- Transcription factor bHLH154
Sequence:
MNGDLEVDMSRGDFNPSFFLGKLKDDEFESRSLSDDSFDAMSGDEDKQEQRPKKKKRKTKYHRHTSYQIQELESFFKECPHPNEKQRLELGKKLTLESKQIKFWFQNRRTQMKTQLERHENVILKQENEKLRLENSFLKESMRGSLCIDCGGAVIPGEVSFEQHQLRIENAKLKEELDRICALANRFIGGSISLEQPSNGGIGSQHLPIGHCVSGGTSLMFMDLAMEAMDELLKLAELETSLWSSKSEKGSMNHFPGSRETGLVLINSLALVETLMDTNKWAEMFECIVAVASTLEVISNGSDGSRNGSILLMQAEFQVMSPLVPIKQKKFLRYCKQHGDGLWAVVDVSYDINRGNENLKSYGGSKMFPSGCIIQDIGNGCSKVTWIEHSEYEESHTHSLYQPLLSSSVGLGATKWLATLQRQCESFTMLLSSEDHTGLSHAGTKSILKLAQRMKLNFYSGITASCIHKWEKLLAENVGQDTRILTRKSLEPSGIVLSAATSLWLPVTQQRLFEFLCDGKCRNQWDILSNGASMENTLLVPKGQQEGSCVSLLRAAGNDQNESSMLILQETWNDVSGALVVYAPVDIPSMNTVMSGGDSAYVALLPSGFSILPDGSSSSSDQFDTDGGLVNQESKGCLLTVGFQILVNSLPTAKLNVESVETVNNLIACTIHKIRAALRIPA
Protein: Methionine--tRNA ligase, mitochondrial (EC 6.1.1.10) (Methionyl-tRNA synthetase 2) (Mitochondrial methionyl-tRNA synthetase) (MtMetRS) (Q499X9)
Organism: Mus musculus (Mouse)
Subcellular location: Mitochondrion matrix {ECO:0000250}.
Interaction partners:
- Bifunctional glutamate/proline--tRNA ligase
- Isoleucine--tRNA ligase, cytoplasmic
- Isoleucine--tRNA ligase, mitochondrial
- Probable leucine--tRNA ligase, mitochondrial
- Leucine--tRNA ligase, cytoplasmic
- Lysine--tRNA ligase
- Probable arginine--tRNA ligase, mitochondrial
- Methionine--tRNA ligase, cytoplasmic
- Glutamine--tRNA ligase
- Tyrosine--tRNA ligase, cytoplasmic
Sequence:
MLRQCARWVLTRTRFGRGCRRYGSCSPSASGDAGEARAYFTTPIFYVNAAPHIGHLYSALLADALCRHRRLRVPGSASTRFSTGTDEHGLKIQQAAATAGLAPIELCDRVSAQFLQLFREADISSTDFIRTTEARHRVAVQHFWGVLEARGLLYKGIYEGWYCASDECFLPEAKVTRQVGPSGDPCPVSLESGHPVSWTKEENYIFKLSQFREPLQRWLGNNPQAITPEPFHQAVLQWLEEELPDLSVSRRSSHLHWGIPVPGDDSQTIYVWLDALVNYLTVVGYPDADFKSWWPATSHIIGKDILKFHAIYWPALLLGAGLRPPHRIYVHSHWTVSGQKMSKSLGNVVDPRTCLDRYTVDGFRYFLLRQGVPNWDCDYYDEKVVKLLDSELADALGGLLNRCTAYRINPSGTYPSFCAACFPSEPGLTGPSVRVQAEDYALVTAVATLPKLVAGYYNDFQIYKALEAVSSCVRQTNGFVQRHAPWKLNWESPEDAPWLGTVLHVALECLRVFGTLLQPVTPNLADKLLSRLGVSTTERGLGELYFLPRFYGHPCPFEGRKLGPDTGLLFPRLDQSRTRLVKAHRT
Protein: Probable functional amyloid protease FapD (EC 3.4.22.-) (Probable fibril-associated protease FapD) (Q9I2F1)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Periplasm {ECO:0000305|PubMed:23504942}.
Interaction partners:
- Functional amyloid transporter FapF
- Functional amyloid subunit FapC
- Functional amyloid subunit FapB
- Functional amyloid sbunit FapE
- Transporter
Sequence:
MRTLILSLLLLVDLTTQAATLGFPALPGGGLVYKQVQSIRERRFADLVEQKTDFSCGAAALATILEKAYGAPLDEQAVIQGMLAHADPEIVRTQGFSMLDMKRYVESMGMRARGYRIEAAQLEQLKIPAIVLMEIRGYKHFVVLQRTQGEYVYVGDPALGHKRYALTEFAKGWNGIVFAVIGQGYDRGNPLLTPPEPLTARNRLDRFKPVRDAELMEFGFIQSDFF
Protein: HLA class I histocompatibility antigen, B alpha chain (Human leukocyte antigen B) (HLA-B) (P01889)
Organism: Homo sapiens (Human)
Function: Antigen-presenting major histocompatibility complex class I (MHCI) molecule. In complex with B2M/beta 2 microglobulin displays primarily viral and tumor-derived peptides on antigen-presenting cells for recognition by alpha-beta T cell receptor (TCR) on HLA-B-restricted CD8-positive T cells, guiding antigen-specific T cell immune response to eliminate infected or transformed cells. May also present self-peptides derived from the signal sequence of secreted or membrane proteins, although T cells specific for these peptides are usually inactivated to prevent autoreactivity. Both the peptide and the MHC molecule are recognized by TCR, the peptide is responsible for the fine specificity of antigen recognition and MHC residues account for the MHC restriction of T cells. Typically presents intracellular peptide antigens of 8 to 13 amino acids that arise from cytosolic proteolysis via constitutive proteasome and IFNG-induced immunoproteasome. Can bind different peptides containing allele-specific binding motifs, which are mainly defined by anchor residues at position 2 and 9.
Subcellular location: Cell membrane {ECO:0000269|PubMed:25480565, ECO:0000269|PubMed:26439010, ECO:0000269|PubMed:9620674}; Single-pass type I membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000305|PubMed:9620674}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Killer cell immunoglobulin-like receptor 3DL1
- HLA class I histocompatibility antigen, A alpha chain
- Beta-2-microglobulin
- Killer cell immunoglobulin-like receptor 3DL2
- HLA class I histocompatibility antigen, C alpha chain
- Tapasin
- T-cell surface glycoprotein CD8 alpha chain
- HLA class I histocompatibility antigen, alpha chain E
- Leukocyte immunoglobulin-like receptor subfamily B member 2
- Leukocyte immunoglobulin-like receptor subfamily B member 1
Sequence:
MLVMAPRTVLLLLSAALALTETWAGSHSMRYFYTSVSRPGRGEPRFISVGYVDDTQFVRFDSDAASPREEPRAPWIEQEGPEYWDRNTQIYKAQAQTDRESLRNLRGYYNQSEAGSHTLQSMYGCDVGPDGRLLRGHDQYAYDGKDYIALNEDLRSWTAADTAAQITQRKWEAAREAEQRRAYLEGECVEWLRRYLENGKDKLERADPPKTHVTHHPISDHEATLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDRTFQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRWEPSSQSTVPIVGIVAGLAVLAVVVIGAVVAAVMCRRKSSGGKGGSYSQAACSDSAQGSDVSLTA
Protein: NAC (No Apical Meristem) domain transcriptional regulator superfamily protein (T27C4.5 protein) (Q9M846)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MVNPVGFRFRPTKEEIVDHYLRPTNFDGDTSHVDRNIMFMQDNRNDYRPPNSLTGVFSDCSSDDNDSDLLSPKTVS
Protein: Galanin receptor 2-like protein (B3GRU6)
Organism: Gallus gallus (Chicken)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Spexin 1
- Galanin peptides
- RNA binding motif protein 27
- Mitochondrial translation release factor 1
Sequence:
MMEHEDFTSLAGYWNSSDSYQFSPASVIVPVVFSLIFLLGTVGNSLVLAVLLRNRQMGHNTTNLFILNLSLADFFFIVFCVPFQATIYSLEGWVFGSFICKAVHFFIYLTMYASSFTLAAVSVDRYLAIRYPLRSRELRTPYNAVAAMAVIWGLSVVFAGPYLSYYDLIEWESSYICMPGWEEWRRKVMDTSTFAFGYVIPVLVISLSYTRTIKYLWTAVEPLEDMSESKKAKRKVTKMIIIVTILFCLCWLPYHVVILRYLYGDFPFNQATYAFRLLSHCMAYANSCLNPIVYALVSKHFRKGFKRVFSCLLRKKHRNKVHVLHAAHTVPGFEAGSTEVSQVHEENNRCELNPDSLAVPSGSSKHLHLS
Protein: Large ribosomal subunit protein bL19m (39S ribosomal protein L15, mitochondrial) (L15mt) (MRP-L15) (39S ribosomal protein L19, mitochondrial) (L19mt) (MRP-L19) (P49406)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:10600119, ECO:0000269|PubMed:11543634, ECO:0000269|PubMed:25278503, ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042}.
Interaction partners:
- Large ribosomal subunit protein uL22m
- Large ribosomal subunit protein bL20m
- Large ribosomal subunit protein uL29m
- Small ribosomal subunit protein uS15m
- Small ribosomal subunit protein uS17
- Large ribosomal subunit protein bL9m
- Large ribosomal subunit protein bL27m
- Small ribosomal subunit protein uS10m
- Large ribosomal subunit protein bL12m
- Large ribosomal subunit protein bL21m
Sequence:
MAACIAAGHWAAMGLGRSFQAARTLLPPPASIACRVHAGPVRQQSTGPSEPGAFQPPPKPVIVDKHRPVEPERRFLSPEFIPRRGRTDPLKFQIERKDMLERRKVLHIPEFYVGSILRVTTADPYASGKISQFLGICIQRSGRGLGATFILRNVIEGQGVEICFELYNPRVQEIQVVKLEKRLDDSLLYLRDALPEYSTFDVNMKPVVQEPNQKVPVNELKVKMKPKPWSKRWERPNFNIKGIRFDLCLTEQQMKEAQKWNQPWLEFDMMREYDTSKIEAAIWKEIEASKRS
Protein: Candida glabrata strain CBS138 chromosome J complete sequence (Q6FNU0)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- L23
- Small ribosomal subunit protein eS6
- 60S ribosomal protein L36
- Candida glabrata strain CBS138 chromosome M complete sequence
- Large ribosomal subunit protein eL32
- Small ribosomal subunit protein uS5
- L21
- 60S acidic ribosomal protein P0
- Large ribosomal subunit protein uL23
- RP41
Sequence:
MAGVKAYELRTKSKEQLENQLLSLKKELAELQVQKLSRPSLPKIHTVRKDIARVLTIINEQQREAVRQLYKGKKYQPKDMRAKKTRALRRALTKFEATRVTEKQKKKQIAFPQRKYAIKA
Protein: GPI-anchor transamidase (Phosphatidylinositol-glycan biosynthesis class K protein) (Q6IQM5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Phosphatidylinositol glycan anchor biosynthesis, class T.
- Phosphatidylinositol glycan anchor biosynthesis, class S.
- Glycosylphosphatidylinositol anchor attachment 1.
- Phosphatidylinositol glycan anchor biosynthesis, class U.
- GPI inositol-deacylase
- GPI ethanolamine phosphate transferase 3
- Phosphatidylinositol glycan anchor biosynthesis, class F
- GPI alpha-1,4-mannosyltransferase I, catalytic subunit
- Phosphatidylinositol glycan anchor biosynthesis, class L.
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit C
Sequence:
MDYSNLFTVYSCLLLFVSIPCAYSNYVETKAGQFFSSGHTNNWAVLVCTSRFWFNYRHVANTLSVYRSVKRLGIPDSHIVLMLADDMACNYRNPKPATVFSHKNMELNVYGDDVEVDYRGYEVTVENFLRVLTGRLPLSTPRSKRLLSDDRSNILIYLTGHGGNGFLKFQDSEEISNMELADAFEQMWQKRRYNELLFIIDTCQGASMYERFYSPNIMALASSQVGEDSLSHQPDLAIGVHLMDKYTFYLLEFLEEVHPASQANMNDLFKVCPQSQCVSTPGHRTDLFQRDPGSVLITDFFGSVRKVEITKDTISLTCPVESPMQRSGSGDLQVETFTYVDQLPVAEIIHQKPKQKDWHPPDGFILGLWTLILLVFFQTYGIKHLKHIF
Protein: Transcription factor VHR1 (VHT1 regulator 1) (P40522)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Transcription factor that binds to the VHRE consensus sequence in promoters of VHT1 and BIO5, and regulates their biotin-dependent expression.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16533810}.
Interaction partners:
- Vitamin H transporter
- Anaphase-promoting complex subunit 4
- 7-keto 8-aminopelargonic acid transporter
- Mitotic spindle checkpoint component MAD2
- Anaphase-promoting complex subunit CDC16
- Anaphase-promoting complex subunit 1
- Anaphase-promoting complex subunit 5
- Anaphase-promoting complex subunit 2
- Anaphase-promoting complex subunit DOC1
Sequence:
MNGPPTFTQYRINKFSGNGATHKIRELLNFNDEKKWKQFSSRRLELIDKFQLSQYKASEQDQNIKQIATILRTEFGYPVSCSKEFEKLVTAAVQSVRRNRKRSKKRYALSIANGSGGNVNNSISSNSTSDDEISPSIYQRSNSDFLPSSNYAADFQFSNKFQPLMSHQSHNGTIFPTVGTQNDSSPSVTSTQQKYNDIVTMLVHDLVTNVVPLSEQALKDPYTGPNLSHFATSSLSQQPNITTNIPIDSTVPFFLREKLLLQIQRSRTCQDISQAAGSIDIYANLEILGEMSIRMSIAFVIERFFSNLVSSSMKYITAKTCSPENLALLSQRLFGAATRHNLSHFPAAQVQLRLLYLVIGGIVKDFGFDPTLYPLSEIIHHIVMVQYPLASSCASEPPSSSPNKRVKRSPPVVSSDVMLNNNNTLSNRATLLTTLPMKPQSANKDVNRRVIIRFNDREQAFTFHQLSNGPPTVSEVLENCKNLFNIINKNKNFGIFHNDNLLNDESLAKLFDSFSTSEIHLVIKDISTIPLQDAKIPVPITLPKMSCIGENPSMPSIPLVPQEKDDPKKSSLTAFDNILNRISKSPMNEENSNTTLNTGTSTSNTNNNDHNESVPAPYVTKNKNSFQNGNLPQPVFQPLL
Protein: Peptidyl-prolyl cis-trans isomerase CYP20-3, chloroplastic (PPIase CYP20-3) (EC 5.2.1.8) (Cyclophilin of 20 kDa 3) (Cyclosporin A-binding protein) (Rotamase CYP20-3) (Rotamase cyclophilin-4) (P34791)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Required for the light-induced increase of thiol accumulation. Assists the folding or assembly of SAT1 enzyme to form the cysteine synthase complex. Links light and redox signals to the regulation of cysteine biosynthesis in response to stress.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:11719511, ECO:0000269|PubMed:8132503}. Note=Probably associated to membranes.
Interaction partners:
- UPF0235 protein At5g63440
- 2-Cys peroxiredoxin BAS1, chloroplastic
- Protein TORMOZ EMBRYO DEFECTIVE
- Serine acetyltransferase 1, chloroplastic
- Peptidyl-prolyl cis-trans isomerase FKBP13, chloroplastic
- Putative WD-repeat membrane protein
- rRNA 2'-O-methyltransferase fibrillarin 1
- Putative rRNA 2'-O-methyltransferase fibrillarin 3
- rRNA 2'-O-methyltransferase fibrillarin 2
- At4g28200
Sequence:
MASSSSMQMVHTSRSIAQIGFGVKSQLVSANRTTQSVCFGARSSGIALSSRLHYASPIKQFSGVYATTKHQRTACVKSMAAEEEEVIEPQAKVTNKVYFDVEIGGEVAGRIVMGLFGEVVPKTVENFRALCTGEKKYGYKGSSFHRIIKDFMIQGGDFTEGNGTGGISIYGAKFEDENFTLKHTGPGILSMANAGPNTNGSQFFICTVKTSWLDNKHVVFGQVIEGMKLVRTLESQETRAFDVPKKGCRIYACGELPLDA
Protein: GATA zinc finger domain-containing protein 3 (Q75JZ1)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MNHQYIPSPIYSDQNSGVHNVNKSLHNLNINNGNNNYNYSNNNYNNNINNNNNINNNINNNNNNNNNNNNNNINQYHQNHYDQYSDNNCNNSNSNNINNNNNINNNINNNNINNNNNNINSNNNNNNNNNNNNNNNLLKIPQLNISPNGVGGGNGISNGNGVNKIFSKLDLSKVPNSYQLAHNSSMPNSPTSSNISPSTPTSMALNLSSLKSILDSPPAAPAHSASSSHNNDHRTLNINGNHHNNNNNINNNINNNVNNNINNGNGNGNGNGNNNNNNNIGVNGSGSSNSSSPSIGFSIPLLQLKQIGINNQTSPSQQSQQQQQQQQQQQQSQHNGIPLINTTEIHQRSNPSSATNSPRALYYGNESSVENSPFTTPLSSPRGPISPRATINSSMSNLQSNIRVEEQWKKIEYYVNDLSHFIYESIRNKDYSNLSELKEKIDEVVNTSKEIEIIHSIAKSLPPQTRARKKRSTKAEKLQKDLIGIKRSYVTTPKSKGTYCIFCGTMETPEWRKGPGGHKTLCNACGLHYAKNIKKENQNNGGSPNPQQNNVTTTTTTTTSTSTNSPNSNGNNFSPESAMSVSKLISD
Protein: RING-box protein 1B (Regulator of cullins 1b) (Q9NHX0)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Through the RING-type zinc finger, seems to recruit the E2 ubiquitination enzyme to the complex and brings it into close proximity to the substrate (By similarity).
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- Cullin 3, isoform F
- Cullin homolog 1
- Cullin 6
- GEO01111p1
- Cullin-5
- Cullin-2
- AT19737p
- S-phase kinase-associated protein 2
- GEO01805p1
- LP10147p
Sequence:
MAEEIEVEETEDFHDMDFNDEEPSCSGGAVQARTERFVVKKWVAHAMWGWDVAVDNCAICRNHIMNLCIECQADPNANQDECTVAWGECNHAFHYHCIARWLKTRLVCPLDNKEWVYQKYGR
Protein: Cementoblastoma-derived protein 1 (Cementum protein 1) (Cementum protein 23) (CP-23) (Q6PRD7)
Organism: Homo sapiens (Human)
Function: May play a role in development of the periodontium which surrounds and supports the teeth by promoting the differentiation of multi-potent cells from the periodontal ligament into cementoblasts to form the cementum. Binds hydroxyapatite and may promote the biomineralization of the cementum. Also promotes cell proliferation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16263347, ECO:0000269|PubMed:21465469}. Nucleus {ECO:0000269|PubMed:21465469}. Note=Localizes to the nucleus of some cementoblasts. {ECO:0000269|PubMed:21465469}.
Interaction partners:
- Very-long-chain
Sequence:
MGTSSTDSQQAGHRRCSTSNTSAENLTCLSLPGSPGKTAPLPGPAQAGAGQPLPKGCAAVKAEVGIPAPHTSQEVRIHIRRLLSWAAPGACGLRSTPCALPQALPQARPCPGRWFFPGCSLPTGGAQTILSLWTWRHFLNWALQQREENSGRARRVPPVPRTAPVSKGEGSHPPQNSNGEKVKTITPDVGLHQSLTSDPTVAVLRAKRAPEAHPPRSCSGSLTARVCHMGVCQGQGDTEDGRMTLMG
Protein: Outer kinetochore KNL1 complex subunit ZWINT (SNAP25-interacting protein 30) (Scoilin) (ZW10 interactor) (ZW10-interacting protein 1) (Zwint-1) (Q8VIL3)
Organism: Rattus norvegicus (Rat)
Function: Part of the MIS12 complex, which is required for kinetochore formation and spindle checkpoint activity. Required to target ZW10 to the kinetochore at prometaphase (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O95229}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:O95229}. Note=Localizes to kinetochores from late prophase to anaphase (By similarity). Localizes to kinetochores both during mitosis and meiosis (By similarity). {ECO:0000250|UniProtKB:O95229, ECO:0000250|UniProtKB:Q9CQU5}.
Interaction partners:
- Kinetochore protein NDC80
- DSN1, MIND kinetochore complex component, homolog
- Mitotic checkpoint serine/threonine-protein kinase BUB1 beta
- Cell division cycle protein 20 homolog
- Kinetochore protein Nuf2
- Mitotic checkpoint serine/threonine-protein kinase BUB1
- Kinetochore protein Spc24
- NSL1 component of MIS12 kinetochore complex
- Protein zwilch
- Centromere/kinetochore protein zw10 homolog
Sequence:
MADAEKNAVAEKNAVAEENAVAEENAVADKNATKEVLAEAASVLEPVGLPEEAELPAKIMEEFMRNSRKKDKLLCSQLQVVNFLQTFLAQEDNTDQNPDALASEDTSRQKATETKEQWKELKATYMDHVDVIKCALSEALPQVKEAHRKYTELQKAFEQLEAKKRVLEEKLQLAQKQWVLQQKRLQNLTKISAEVKRRRKRALEKLDGSHQELETLKQQAGQEQEKLQRNQSYLQLLCSLQNKLVISESKADDKDVKGPALPPKSP
Protein: Phosphoenolpyruvate synthase regulatory protein (PEP synthase regulatory protein) (PSRP) (EC 2.7.11.33) (EC 2.7.4.28) (Pyruvate, water dikinase regulatory protein) (P0A8A4)
Organism: Escherichia coli (strain K12)
Function: Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the phosphoenolpyruvate synthase (PEPS) by catalyzing its phosphorylation/dephosphorylation.
Interaction partners:
- Phosphoenolpyruvate synthase
- Phytase AppA
- Putative general secretion pathway protein B
- Arabinose 5-phosphate isomerase KdsD
Sequence:
MDNAVDRHVFYISDGTAITAEVLGHAVMSQFPVTISSITLPFVENESRARAVKDQIDAIYHQTGVRPLVFYSIVLPEIRAIILQSEGFCQDIVQALVAPLQQEMKLDPTPIAHRTHGLNPNNLNKYDARIAAIDYTLAHDDGISLRNLDQAQVILLGVSRCGKTPTSLYLAMQFGIRAANYPFIADDMDNLVLPASLKPLQHKLFGLTIDPERLAAIREERRENSRYASLRQCRMEVAEVEALYRKNQIPWINSTNYSVEEIATKILDIMGLSRRMY
Protein: Glycine hydroxymethyltransferase (Serine methylase) (J3KRZ5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTMPVNGAHKDADLWSSHDKMLAQPLKDSDVEVYNIIKKESNRQRVGLELIASENFASRAVLEALGSCLNNKYSEGYPGQRYYGGTEFIDELETLCQKRALQAYKLDPQCWGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTDKKKISATSIFF
Protein: Protein translocase subunit SecA (F4HY36)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
Interaction partners:
Sequence:
MEEPECPVCLQSYDGESTVPRVLACGHTACEECLTNLPKKFPDTIRCPACTVLVKFPPQGPSALPKNIDLLRLFPSISKLKLEPGRNFEKVVEFVTRSWSDDFYATWKDRILVHDAVSVEIRESESSDFDSSSRLCGSLRDDSKVSLLRVASFEHGDCDSVLKYSYVQRMMSCLWGMREEERDELDAIISVKQRGVSKVFGLWGDLKNGVLYLVGEKLIGFSLEEFDSLEDETLRLGIIGMQICEALLNLHKEGLITGCLSVSCVKFDEYENAYVDLIELIETGRNVYRIIAEETSSLRKPVGASEMGLIFVGLQQKGIFISSEVLFEFLKEQNMLIKNTSSKSFVSHNSDVWPVCFLLLKLRLGKRCTEEFIESVNCVDGKGCEEGIEDILVLYTGITEKLSLESELQGKFKSMVEILRQCCCLDPQARPVLTDLWKCIRELVMKPRFNSMSRLHKTIYGKRKQFCLAQSELCRLVEVESKEVDKELPGMKIGDEAEEGKVDIDFPGRVSEGKVRSKDMRGHQDSVTGLAVGGGFLFSSSYDRTILIWSLKDFSHVHTFKGHQDKVMALIHIEGTEPVCVSGDGGGGIFVWSTTFPLEEQPLRKWYEPKDWRYTGIHALAYSEYGHVYTGSGDNTIKAWSLQDGSLLCTMSGHKSVVSTLVVVNGVLYSGSWDGTVRLWSLSDNSLLTVLGEETPGIVRSILSLAADDQTLVAAYQNGDIQIWRDDTLMKSMKIQNGAILSIAVNGKWLFTGGWDKTINVQELSGDEISVNCAHVGSIPGSSVITSLLYWEGKLFAGFADKTIKGNLGRLKRNVQDFTSMNYWVVRDYYRLVESVNSLEPQIQSLSDEQVKLSLKAKTAEFRERLARGESLADMQAEAFAVVREAAKRTIGMRHFDVQIIGGGVLHDGSIAEMKTGEGKTLVSTLAAYLNALTGEGVHVVTVNDYLAQRDAEWMGRVHRFLGLSVGLIQRGMKAEERKFNYSCDITYTNNSELGFDYLRDNLTSNREQLVMRWPKPFHFAIVDEVDSVLIDEGRNPLLISGEANENAARYPVAAKVAELLVKDSHYKVELKENSVELTEEGISLAEMALETGDLWDENDPWARFVMNALKAKEFYKRDVQYIVRDGKALIINELTGRVEDKRRWSEGVHQAVEAKEGLEIQADSIVVAQITYQSLFKLYPKLSGMTGTAKTEEKEFLKMFQIPVIEVPTNLSNIRIDLPIQAFATARGKWEHVRREVEDMFGQGRPVLVGTTSVENSEYLSELLKEWGIPHNVLNARPKYAAREADFIAQAGRKYAITISTNMAGRGTDIILGGNPKMLAREIIEDSILSYLTSEVLADNIDDDELSQKVLSKIKVGPSSLALLARASLMAKYVGKSESKSWTRKKAKSVVTESLEKSQTMDPMELQNLINEQSEMYPLGPAIALAYLSVLKDCEAHCLHEGSEVKRLGGLHVIGTSLHESRRIDNQLRGRAGRQGDPGSTRFMISLQDEMFQKFNFDTEWAVRLISKITNDEDLPIEGDTIVKQLLALQINAEKYFFGIRKSLVEFDEVLEVQRKHVYDLRQLLLTGENESCSQHIFQYMQAVVDEIVVGNSNPQKHPRYWSLAKLLKEFMAISGNLLDESFSGITEETMLQSLENLHEGSSIEMEDLSLPHLPKPPNAFRGIRRKNSSLRRWLDICSDNLTGSGSYRTLINLLRKFLGDYLIASYLNVVQESGFDDGYIKEIERAVLLKTLDCYWRDHLVNMNKLSSAVNVRSFAHRNPLEEYKIDGCRFFISMLSATRRLTVESILQYWSSPMESQELFIS
Protein: UDP-D-apiose/UDP-D-xylose synthase 1 (EC 4.1.1.35) (Q9ZUY6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the conversion of UDP-D-glucuronate to a mixture of UDP-D-apiose and UDP-D-xylose. D-Apiose (3-C-hydroxymethyl-d-erythrose) is the only plant cell wall monosaccharide with a branched carbon skeleton and is found in rhamnogalacturonan II (RG-II), apiogalacturonan, and several apioglycosides.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:32662159}.
Interaction partners:
- UDP-glucose 6-dehydrogenase 3
- UDP-glucose 6-dehydrogenase 4
- UDP-glucose 6-dehydrogenase 2
- UDP-glucose 6-dehydrogenase 1
- UDP-glucuronate 4-epimerase 3
- UDP-glucuronate 4-epimerase 5
- UDP-glucuronate 4-epimerase 6
- UDP-glucuronate 4-epimerase 1
- Probable UDP-arabinose 4-epimerase 3
- Putative UDP-arabinose 4-epimerase 2
Sequence:
MANGANRVDLDGKPIQPLTICMIGAGGFIGSHLCEKLLTETPHKVLALDVYNDKIKHLLEPDTVEWSGRIQFHRINIKHDSRLEGLVKMADLIINLAAICTPADYNTRPLDTIYSNFIDALPVVKYCSENNKRLIHFSTCEVYGKTIGSFLPKDHPLRDDPAFYVLKEDISPCIFGSIEKQRWSYACAKQLIERLVYAEGAENGLEFTIVRPFNWIGPRMDFIPGIDGPSEGVPRVLACFSNNLLRREPLKLVDGGESQRTFVYINDAIEAVLLMIENPERANGHIFNVGNPNNEVTVRQLAEMMTEVYAKVSGEGAIESPTVDVSSKEFYGEGYDDSDKRIPDMTIINRQLGWNPKTSLWDLLESTLTYQHRTYAEAVKKATSKPVAS
Protein: Glycylpeptide N-tetradecanoyltransferase 1 (EC 2.3.1.97) (Myristoyl-CoA:protein N-myristoyltransferase 1) (NMT 1) (Type I N-myristoyltransferase) (Peptide N-myristoyltransferase 1) (Q8K1Q0)
Organism: Rattus norvegicus (Rat)
Function: Adds a myristoyl group to the N-terminal glycine residue of certain cellular and viral proteins. Also able to mediate N-terminal lysine myristoylation of proteins: catalyzes myristoylation of ARF6 on both 'Gly-2' and 'Lys-3'. Lysine myristoylation is required to maintain ARF6 on membranes during the GTPase cycle.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P30419}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P30419}. Membrane {ECO:0000250|UniProtKB:P30419}; Peripheral membrane protein {ECO:0000250|UniProtKB:P30419}. Note=Copurifies with ribosomes. {ECO:0000250|UniProtKB:P30419}.
Interaction partners:
- Dephospho-CoA kinase domain-containing protein
- BH3-interacting domain death agonist
- G protein subunit alpha transducin 1
Sequence:
MADESETAVKLPAPSLPLMMEGNGNGHEHCSDCENEEDISHNRGGLSPANDTGAKKKKKKQKKKKEKGNDMDSTQDQPVKMNSLPAERIQEIQKAIELFSVGQGPAKTMEEASKRSYQFWDTQPVPKLGEVVNTHGPVEPDKDNIRQEPYTLPQGFTWDALDLGDRGVLKELYTLLNENYVEDDDNMFRFDYSPEFLLWALRPPGWLPQWHCGVRVVSSRKLVGFISAIPANIHIYDTEKKMVEINFLCVHKKLRSKRVAPVLIREITRRVHLEGIFQAVYTAGVVLPKPVGTCRYWHRSLNPRKLIEVKFSHLSRNMTMQRTMKLYRLPETPKTAGLRPMEKKDIPVVHQLLSRYLKQFNLTPVMNQEEVEHWFYPQENIIDTFVVENANGEVTDFLSFYTLPSTIMNHPTHKSLKAAYSFYNVHTQTPLLDLMSDALVLAKMKGFDVFNALDLMENKTFLEKLKFGIGDGNLQYYLYNWKCPSMGAEKVGLVLQ
Protein: Exosome complex exonuclease RRP44p homologue (Q384R7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Exosome component CSL4
- Ribosomal RNA processing protein 45
- Telomerase-associated protein, putative
- RNasePH-like protein exosome-associated protein 1 Rrp42 homologue
- Ribosomal RNA-processing protein 43
- Exosome complex exonuclease RRP40
- Ribosomal RNA processing protein 4
- Elongation factor 1-alpha, putative
- Exosome complex exonuclease RRP41A
- Exosome-associated protein 4
Sequence:
MFTKKRLAVHQVRSSATRRTASGITRNDIGCGTVGCKLCASTACQNSGNSSSLVPTAPIMIPDAVTILHNMNAMEDARIQNIVLLSTVMSEVQERNKAIYARLQRLVGGERKQCYVFSNDRHEQTHCVMQSEETRSDFNDRCVRVAGRWYAQHLALAFPAVTGVAEIPSVVLVSHDKLLQSAPNSAQAEENISNLSCLTLRQFLEGCVTAGTDLLEMIQPDRPVEGKEQGSARALFSPHLAESALDLGVQNGTYLRGKLRVSETNCFFGEIRGQWKGHNFERVLLPGRTNLNRAIHGDIVTVELLPVASWRPLRGAKPTEEMNDTGAGGDDHENSGREGIGEESEGAALARGYTPVGRVVGITTMNRRPFCGSIDVEELNKLADTLDTLTGTVSVLFQPKDNRIPRIRITTAHLGALKDKRLSVIIDDWGEHSSFPVGHYVEVLGTIGDKDTEAKVILLENDIPHYDFSEAVYDCLPKGEWNVTEEELGNRLDLRDLCVVSVDPLGCRDIDDALHCRRVNGNHLEVGVHIADVTHFLKEGTAMDEEAAKRSTSVYLVDRRINMLPQLLTENLCSIVADEDRYAFSIMWEFDENYSVVREFFGKTVIRSRAALYYGDAQRMIDDPEDESEAAVSLRYLMQLSRHFRKRREKDGALFLCSQEFKFKVDNDHVNPTDMQAYQTFDSNSMIEEWMLFANAAAARRVYASFPRWTLLRRHQAPAENAFDTLNEAIRRKIGLKLDDTTSLALNESLEKCVDPSDPYFNRLIRTLVTRCLRQAQYFSSSEVSKDEFHHFGLAMPIYTHFTSPIRRYADVIVHRQLAAALGIMDVSEAHMVSVKMEALASNLNYRHEQAQKAGRDSQNLFTGFYLRNFANQEIPSEDGYVVKLSETHVFVLVPKYGQEGKIAKETLVRVPNLLDKVKVGIEVRQRGDVLRASLVFSIIGLTKGCEDVSEPVAIAGEDLPLKRQRLEEGQQ