wanglab/gogpt-training-data huggingface dataset:
Protein: E3 ubiquitin-protein ligase RNF126 (EC 2.3.2.27) (RING finger protein 126) (Q9BV68)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase that mediates ubiquitination oF target proteins. Depending on the associated E2 ligase, mediates 'Lys-48'- and 'Lys-63'-linked polyubiquitination of substrates (By similarity). Part of a BAG6-dependent quality control process ensuring that proteins of the secretory pathway that are mislocalized to the cytosol are degraded by the proteasome. Probably acts by providing the ubiquitin ligase activity associated with the BAG6 complex and be responsible for ubiquitination of the hydrophobic mislocalized proteins and their targeting to the proteasome. May also play a role in the endosomal recycling of IGF2R, the cation-independent mannose-6-phosphate receptor. May play a role in the endosomal sorting and degradation of several membrane receptors including EGFR, FLT3, MET and CXCR4, by mediating their ubiquitination. By ubiquitinating CDKN1A/p21 and targeting it for degradation, may also promote cell proliferation. May monoubiquitinate AICDA.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23026136}. Nucleus {ECO:0000269|PubMed:23026136}.
Interaction partners:
- Large proline-rich protein BAG6
- Golgi to ER traffic protein 4 homolog
- Ubiquitin-conjugating enzyme E2 D2
- ATPase GET3
- Ubiquitin-like protein 4A
- Ubiquitin-conjugating enzyme E2 D1
- E2 ubiquitin-conjugating enzyme
Sequence:
MAEASPHPGRYFCHCCSVEIVPRLPDYICPRCESGFIEELPEETRSTENGSAPSTAPTDQSRPPLEHVDQHLFTLPQGYGQFAFGIFDDSFEIPTFPPGAQADDGRDPESRRERDHPSRHRYGARQPRARLTTRRATGRHEGVPTLEGIIQQLVNGIITPATIPSLGPWGVLHSNPMDYAWGANGLDAIITQLLNQFENTGPPPADKEKIQALPTVPVTEEHVGSGLECPVCKDDYALGERVRQLPCNHLFHDGCIVPWLEQHDSCPVCRKSLTGQNTATNPPGLTGVSFSSSSSSSSSSSPSNENATSNS
Protein: Oligouridylate-binding protein 1C (AtUBP1c) (Polyuridylate-binding protein UBP1C) (Poly(U)-binding protein UBP1C) (Q9LJH8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Heterogeneous nuclear ribonucleoprotein (hnRNP)-like protein that acts as a component of the pre-mRNA processing machinery. Functions at multiple steps to facilitate the nuclear maturation of plant pre-mRNAs (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Ubiquitin carboxyl-terminal hydrolase 1
- Ribonuclease TUDOR 2
- Pumilio homolog 4
- La-related protein 1A
- mRNA-decapping enzyme-like protein
- Uncharacterized protein At2g23090
- Zinc finger A20 and AN1 domain-containing stress-associated protein 3
- Eukaryotic translation initiation factor 4E-1
- Eukaryotic translation initiation factor isoform 4G-2
Sequence:
MQNPRLKQHQQQQQQQAMMQQQALMQQHSLYHPGVLAPPQLEPVPSGNLPPGFDPSTCRSVYVGNIHTQVTEPLLQEIFTSTGPVESSKLIRKDKSSYGFVHYFDRRSAALAILSLNGRHLFGQPIKVNWAYATGQREDTSSHFNIFVGDLSPEVTDATLYQSFSVFSSCSDARVMWDQKTGRSRGFGFVSFRNQQDAQTAINEMNGKWLSSRQIRCNWATKGATSGDDKLSSDGKSVVELTTGSSEDGKETLNEETPENNSQFTTVYVGNLAPEVTQLDLHRYFHALGAGVIEEVRVQRDKGFGFVRYNTHPEAALAIQMGNTQPYLFNRQIKCSWGNKPTPPGTASNPLPPPAPAPVPGLSAADLLNYERQLALSKMASVNALMHQQGQHPLRQAHGINAAGATAAMYDGGFQNVAAAQQLMYYQ
Protein: Cinnamoyl-CoA reductase 2 (AtCCR2) (EC 1.2.1.44) (Q9SAH9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Cinnamoyl-CoA reductase probably involved in the formation of phenolic compounds associated with the hypersensitive response. Seems not to be involved in lignin biosynthesis.
Interaction partners:
- Cytochrome P450 84A1
- 4-coumarate--CoA ligase 4
- 4-coumarate--CoA ligase-like 7
- Caffeoyl-CoA O-methyltransferase 1
- Probable caffeoyl-CoA O-methyltransferase At4g26220
- Trans-cinnamate 4-monooxygenase
- Shikimate O-hydroxycinnamoyltransferase
- Putative caffeoyl-CoA O-methyltransferase At1g67980
- 4-coumarate--CoA ligase 1
- 4-coumarate--CoA ligase-like 6
Sequence:
MLVDGKLVCVTGAGGYIASWIVKLLLERGYTVRGTVRNPTDPKNNHLRELQGAKERLTLHSADLLDYEALCATIDGCDGVFHTASPMTDDPETMLEPAVNGAKFVIDAAAKAKVKRVVFTSSIGAVYMNPNRDTQAIVDENCWSDLDFCKNTKNWYCYGKMLAEQSAWETAKAKGVDLVVLNPVLVLGPPLQSAINASLVHILKYLTGSAKTYANLTQVYVDVRDVALGHVLVYEAPSASGRYILAETALHRGEVVEILAKFFPEYPLPTKCSDEKNPRAKPYKFTTQKIKDLGLEFKPIKQSLYESVKSLQEKGHLPLPQDSNQNEVIIES
Protein: Apidaecin +S [Cleaved into: Apidaecin -S] (C0HKX4)
Organism: Vespula maculifrons (Eastern yellow jacket) (Wasp)
Function: Antimicrobial peptide active against many Gram-negative enterobacterial and plant-associated bacterial species. Not active against other bacterial species like H.pylori, P.mirabilis, B.pertussis or N.gonorrhoeae.
Subcellular location: Secreted {ECO:0000269|PubMed:7929322}.
Interaction partners:
Sequence:
SNKPRPQQVPPRPPHPRL
Protein: At4g22730 (Leucine rich repeat receptor kinase-like protein) (Leucine-rich repeat protein kinase family protein) (Leucine-rich repeat receptor-like protein kinase) (O49654)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MVTLCATLLILLSIFLATPSNVRGNAELKALMELKSSLDPENKLLRSWTFNGDPCDGSFEGIACNQHLKVANISLQGKRLVGKLSPAVAELKCLSGLYLHYNSLSGEIPQEITNLTELSDLYLNVNNFSGEIPADIGSMAGLQVMDLCCNSLTGKIPKNIGSLKKLNVLSLQHNKLTGEVPWTLGNLSMLSRLDLSFNNLLGLIPKTLANIPQLDTLDLRNNTLSGFVPPGLKKLNGSFQFENNTGLCGIDFPSLRACSAFDNANNIEQFKQPPGEIDTDKSALHNIPESVYLQKHCNQTHCKKSSSKLPQVALISSVITVTITLIGAGILTFFRYRRRKQKISNTPEFSEGRLSTDQQKEFRASPLVSLAYTKEWDPLGDSRNGAEFSQEPHLFVVNSSFRFNLEDIESATQCFSEANLLSRNSFTSVFKGVLRDGSPVAIRSINISSCKNEEVEFMNGLKLLSSLSHENLVKLRGFCCSRGRGECFLIYDFASKGKLSNFLDLQERETNLVLAWSARISIIKGIAKGIAYLHGSDQQKKPTIVHRNISVEKILLDEQFNPLIADSGLHNLLADDMVFSALKTSAAMGYLAPEYVTTGKFTEKTDIFAFGVIILQILSGKLMLTSSLRNAAENGEHNGFIDEDLREEFDKPEATAMARIGISCTQEIPNNRPNIETLLENINCMKSE
Protein: Small capsomere-interacting protein (F5HEN7)
Organism: Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5)
Function: Participates in the assembly of the infectious particles by decorating the outer surface of the capsid shell and thus forming a layer between the capsid and the tegument. Complexes composed of the capsid protein VP5 and UL48A assemble together in the host cytoplasm and are translocated to the nucleus, where they accumulate and participate in capsid assembly.
Subcellular location: Virion {ECO:0000255|HAMAP-Rule:MF_04021, ECO:0000269|PubMed:11152518, ECO:0000269|PubMed:8764088}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04021}.
Interaction partners:
Sequence:
MSNTAPGPTVANKRDEKHRHVVNVVLELPTEISEATHPVLATMLSKYTRMSSLFNDKCAFKLDLLRMIAVSRTRR
Protein: Persulfide dioxygenase ETHE1, mitochondrial (EC 1.13.11.18) (Ethylmalonic encephalopathy protein 1 homolog) (Hepatoma subtracted clone one protein) (Sulfur dioxygenase ETHE1) (Q9DCM0)
Organism: Mus musculus (Mouse)
Function: First described as a protein that can shuttle between the nucleus and the cytoplasm and suppress p53-induced apoptosis by sequestering the transcription factor RELA/NFKB3 in the cytoplasm and preventing its accumulation in the nucleus (By similarity). Sulfur dioxygenase that plays an essential role in hydrogen sulfide catabolism in the mitochondrial matrix. Hydrogen sulfide (H(2)S) is first oxidized by SQRDL, giving rise to cysteine persulfide residues. ETHE1 consumes molecular oxygen to catalyze the oxidation of the persulfide, once it has been transferred to a thiophilic acceptor, such as glutathione (R-SSH). Plays an important role in metabolic homeostasis in mitochondria by metabolizing hydrogen sulfide and preventing the accumulation of supraphysiological H(2)S levels that have toxic effects, due to the inhibition of cytochrome c oxidase.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O95571}. Nucleus {ECO:0000250|UniProtKB:O95571}. Mitochondrion matrix {ECO:0000250|UniProtKB:O95571}.
Interaction partners:
- Sulfite oxidase, mitochondrial
- Sulfide:quinone oxidoreductase, mitochondrial
- Thiosulfate sulfurtransferase
- 3-mercaptopyruvate sulfurtransferase
Sequence:
MASAVVRVAGRRLSQQSASGAPVLLRQMFEPKSCTYTYLLGDRESREAVLIDPVLETAHRDAQLIKELGLKLLYAVNTHCHADHITGTGVLRSLLPGCQSVISRLSGAQADLHIGEGDSIRFGRFALETRASPGHTPGCVTFVLNDQSMAFTGDALLIRGCGRTDFQQGCAKTLYHSVHEKIFTLPGNCLIYPAHDYHGLTVSTVEEERTLNPRLTLSCEEFIKVMDNLNLPKPQQIDIAVPANMRCGVQTPPS
Protein: Arginine kinase (EC 2.7.3.3) (Q38EV1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Arginase, putative
- Arginine kinase
- Arginine kinase
Sequence:
MATRDVAAELEKAFAKLQAAKDCHSLLKKHLTSDVFKKLKDKKTKLGATLLDVIQSGVQNLDSGVGLYAPDAEAYTVFADLFDPVIEDYHNGFKVTDKQPPKDFGDLNTLVDVDPEGKYVISTRVRCGRSLAGYPFNPCLTKEQYEEMESRVREQLSTMTDDLQGTYYPLSGMTKETQQQLIDDHFLFKEGDRFLQAARACEYWPTGRGIYHNNDKTFLVWVNEEDHLRIISMQKGGNLKEVFSRLVKAVNIIEEKVEFSRDDRLGFLTFCPSNLGTTIRASVHIKLPKLGADRAKLEEVAAKYNLQVRGTAGEHSDSPDGIYDISNKRRLGLSEYEAVKEMQDGILELIKLENRAVVTDGAKPFVGSNL
Protein: Alpha terpineol synthase, chloroplastic (EC 4.2.3.111) (EC 4.2.3.112) ((-)-limonene synthase, chloroplastic) (EC 4.2.3.16) (Geraniol synthase, chloroplastic) (EC 3.1.7.11) (Terpene synthase alphaterp) (PbTPS-alphaterp) (Terpinolene synthase, chloroplastic) (EC 4.2.3.113) (R9QMR5)
Organism: Pinus banksiana (Jack pine) (Pinus divaricata)
Function: Monoterpene synthase (TPS) involved in the biosynthesis of monoterpene natural products included in conifer oleoresin secretions and volatile emissions; these compounds contribute to biotic and abiotic stress defense against herbivores and pathogens. Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) to (-)-alpha-terpineol, (+)-alpha-terpineol and terpin-4-ol, and, to a lower extent, to geraniol, terpinolene and (-)-limonene.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
Sequence:
MALLSVAPLASKSRLHKTLITSAHHLKPSPTTIPTLPVCTRRKTFTASITMCLTAPVSDDGVKRRIGNHHSNLWDHDFILSLSTPYEAPSYRERAARLISEVKEMFTEIEDGLSITPLNDLLSRLSMVDSIERLGVDRHFKMEIKSALDYVHRYWSEKGIGCGRESGVTDLNSTALGLRTLRLHGYPVSSSVLEQFKDEKGQFATSSIQTDPGEIRTIFNLFRASLVAFPNEKVMEDAQIFSTIYLKEYLEKIPLSSLSRQIEYVMEYGWHTNLPRLEARHYMDVFGDNEMPWMSYVNTEKLLELAKLEFNIFHSIQQRELKHISRWWKDSGFSQMNFVRHRHVEYYTLASCFAIDPEHSAFRVSFAKMCHLGTVLDDIYDTFGTMEELQLFTAAVKRWDPSATDSLPEYMKRVYTVLYETVNEMAQVAKKSQGRDTINYARHAWEAYLDSYMKEAEWISTGCLPTFEEYYENGKISFGYRICMLQPILSMDIPFPHHILQEIDYPSRFSSLAAGILRLKGDTRCYQADSARGEEASCISCYMKENPGLTEEDVVNHIHGMVDDLIKELNWELLKPDCNVPISSKKHAFDICRAFHHGYKYRDGYSVATNEIKDLVMITVLEPVPL
Protein: ATP-dependent Clp protease proteolytic subunit (EC 3.4.21.92) (Endopeptidase Clp) (Q8DST7)
Organism: Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00444}.
Interaction partners:
- ATP-dependent Clp protease ATP-binding subunit ClpX
- ATP-dependent protease ClpE
- Class III stress response-related ATP-dependent Clp protease, ATP-binding subunit
- Clp-like ATP-dependent protease, ATP-binding subunit
- Chaperone protein ClpB
- Co-chaperonin GroES
- Chaperonin GroEL
- Heat-inducible transcription repressor HrcA
- Chaperone protein DnaK
- Protein GrpE
Sequence:
MIPVVIEQTSRGERSYDIYSRLLKDRIIMLTGPVEDNMANSIIAQLLFLDAQDNTKDIYLYINSPGGSVSAGLAIVDTMNFIKSDVQTIVMGIAASMGTIIASSGAKGKRFMLPNAEYLIHQPMGGTGGGTQQSDMAIAAEQLLKTRKKLEKILSDNSGKTIKQIHKDAERDYWMDAKETLKYGFIDEIMENNELK
Protein: Importin subunit alpha-8 (Karyopherin subunit alpha-7) (A9QM74)
Organism: Homo sapiens (Human)
Function: Functions in nuclear protein import.
Subcellular location: Nucleus {ECO:0000269|PubMed:20701745, ECO:0000269|PubMed:36647821}.
Interaction partners:
- Importin subunit beta-1
- Interleukin-1 family member 10
- Butyrophilin subfamily 3 member A1
- GTP-binding nuclear protein Ran
- Mucin-3A
- Exportin-2
- Forkhead box protein P1
Sequence:
MPTLDAPEERRRKFKYRGKDVSLRRQQRMAVSLELRKAKKDEQTLKRRNITSFCPDTPSEKTAKGVAVSLTLGEIIKGVNSSDPVLCFQATQTARKMLSQEKNPPLKLVIEAGLIPRMVEFLKSSLYPCLQFEAAWALTNIASGTSEQTRAVVEGGAIQPLIELLSSSNVAVCEQAVWALGNIAGDGPEFRDNVITSNAIPHLLALISPTLPITFLRNITWTLSNLCRNKNPYPCDTAVKQILPALLHLLQHQDSEVLSDACWALSYLTDGSNKRIGQVVNTGVLPRLVVLMTSSELNVLTPSLRTVGNIVTGTDEQTQMAIDAGMLNVLPQLLQHNKPSIQKEAAWALSNVAAGPCHHIQQLLAYDVLPPLVALLKNGEFKVQKEAVWMVANFATGATMDQLIQLVHSGVLEPLVNLLTAPDVKIVLIILDVISCILQAAEKRSEKENLCLLIEELGGIDRIEALQLHENRQIGQSALNIIEKHFGEEEDESQTLLSQVIDQDYEFIDYECLAKK
Protein: RNA polymerase II C-terminal domain phosphatase-like 2 (FCP-like 2) (EC 3.1.3.16) (ASI1-immunoprecipitated protein 4) (Carboxyl-terminal phosphatase-like 2) (AtCPL2) (CTD phosphatase-like 2) (Q5YDB5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Processively dephosphorylates 'Ser-5' but not 'Ser-2' of the heptad repeats YSPTSPS in the C-terminal domain of the largest RNA polymerase II subunit (RPB1). This promotes the activity of RNA polymerase II. Together with CPL1, required for male gametes fertility. Multifunctional regulator that modulates plant growth, stress, and phytohormones responses. Positive transcription regulator of genes involved in high salinity resistance and auxin mediated signaling pathway.
Subcellular location: Nucleus {ECO:0000269|PubMed:15388846}. Cytoplasm {ECO:0000269|PubMed:15388846}.
Interaction partners:
- RNA-binding KH domain-containing protein RCF3
- Transcription initiation factor IIF subunit alpha
- Protein PARALOG OF AIPP2
- SCP1-like small phosphatase 4b
- Tryptophan/tyrosine permease
- Probable magnesium transporter NIPA4
- Double-stranded RNA-binding protein 1
- acylphosphatase
- DNA-directed RNA polymerase II subunit 4
- RNA polymerase II C-terminal domain phosphatase-like 5
Sequence:
MNRLGHKSVVYHGDLRLGELDVNHVSSSHEFRFPNDEIRIHHLSPAGERCPPLAILQTIASFAVRCKLESSAPVKSQELMHLHAVCFHELKTAVVMLGDEEIHLVAMPSKEKKFPCFWCFSVPSGLYDSCLRMLNTRCLSIVFDLDETLIVANTMKSFEDRIEALKSWISREMDPVRINGMSAELKRYMDDRMLLKQYIDNDYAFDNGVLLKAQPEEVRPTSDGQEKVCRPVIRLPEKNTVLTRIKPEIRDTSVLVKLRPAWEELRSYLTAKTRKRFEVYVCTMAERDYALEMWRLLDPEAHLISLKELRDRIVCVKPDAKKSLLSVFNGGICHPKMAMVIDDRMKVWEDKDQPRVHVVSAYLPYYAPQAETALVVPHLCVARNVACNVRGYFFKEFDESLMSSISLVYYEDDVENLPPSPDVSNYVVIEDPGFASNGNINAPPINEGMCGGEVERRLNQAAAADHSTLPATSNAEQKPETPKPQIAVIPNNASTATAAALLPSHKPSLLGAPRRDGFTFSDGGRPLMMRPGVDIRNQNFNQPPILAKIPMQPPSSSMHSPGGWLVDDENRPSFPGRPSGLYPSQFPHGTPGSAPVGPFAHPSHLRSEEVAMDDDLKRQNPSRQTTEGGISQNHLVSNGREHHTDGGKSNGGQSHLFVSALQEIGRRCGSKVEFRTVISTNKELQFSVEVLFTGEKIGIGMAKTKKDAHQQAAENALRSLAEKYVAHVAPLARETEKGPENDNGFLWESSEDVSNKGLEEEAPKENISEL
Protein: Origin recognition complex subunit 3 (Q9TVK9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDPTISVSKGCFVYKNGATRAGKKAASKRKRPAAESSSLLGKEVVQQPFYEEYRKAWNQINDHIADLQHRSYARTLEQLVDFVVGQAERDTPDEVLPTAALLTGINQPDHLSQFTALTQRLHAQRAAMVCVLQSRDCATLKAAVETLVFGLVEDNAEVEQMEDEDEDEDGAERDRKRLRRSQCTMKQLKSWYTNNFDSEQKRRQLVVILPDFECFNASVLQDLILILSAHCGSLPFVLVLGVATAMTAVHGTLPYHVSSKIRLRVFQTQAAPTGLNEVLDKVLLSPKYAFHLSGKTFKFLTHIFLYYDFSIHGFIQGFKYCLMEHFFGGNAFALCTDYSKALGRIKQLTHEDMETIRRLPSFRPYVEQINDCKRIIAVLTDDDYLKKKLPQLLRDCLLHFLLFRCSLEFLTELVGDLPRCPLGKLRRELYVNCLNRAIISTPEYKECQQMLSFLSKDEFVAKVNRALERTEQFLVEEIAPLELGEACTAVLRPKLEAIRLAVDEVVKATMATITTTSPNETSQATDHLTPVRSRQELKDQLLQRSKEDKMRHQLNTPTTQFGRALQKTLQLIETQIVQDHLRALQDAPPIHELFVFSDIATVRRNIIGAPRAALHTALNNPHFYMQCKCCELQDQSLLVGTLPDLSVVYKLHLECGRMINLFDWLQAFRSVVSGSDNEEVAQEQIDPQIQARFTRAVAELQFLGYIKMSKRKTDHATRLTW
Protein: Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1 (EC 2.1.1.57) (Cap1 2'O-ribose methyltransferase 1) (Q5T7F5)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU368012}.
Interaction partners:
Sequence:
MKRRTDPECTAPIKKQKKRVAELALSLSSTSDDEPPSSVSHGAKASTTSLSGSDSETEGKQHSSDSFDDAFKADSLVEGTSSRYSMYNSVSQKLMAKMGFREGEGLGKYSQGRKDIVEASSQKGRRGLGLTLRGFDQELNVDWRDEPEPSACEQVSWFPECTTEIPDTQEMSDWMVVGKRKMIIEDETEFCGEELLHSVLQCKKPLVKDREAELLYFADVCAGPGGFSEYVLWRKKWHAKGFGMTLKGPNDFKLEDFYSASSELFEPYYGEGGIDGDGDITRPENISAFRNFVLDNTDRKGVHFLMADGGFSVEGQENLQEILSKQLLLCQFLMALSIVRTGGHFICKTFDLFTPFSVGLVYLLYCCFERVC
Protein: Sesquiterpene alcohol synthase (MhTPS) (EC 2.5.1.-) (A0A343W969)
Organism: Murgantia histrionica (Harlequin bug)
Function: Sesquiterpene alcohol synthase that catalyzes the formation of (1S,6S,7R)-sesquipiperitol, a terpene intermediate in murgantiol biosynthesis, a male-released aggregation pheromone.
Interaction partners:
Sequence:
MVSIAAKSLPKLSGAVFGQFSRRKQLIQRHWLDTRTDQYYDVLRRIVVPECKNIASDVPEYPERIEKLLYYTNPAFSDAWNFTTELIYRTVADESHQTEENITKMYLIRATMDLLFTMSAVLDDISDRSEFRKGKKGWHMICQGGESTALYDGTQMGLFPLYLLKQYFKNDPGYSRLLETVVMTYIKLTIGQTIDVLGQFKKSPSMAEYKRINYYKAGQFVAAGSELAVIHAGITSQDLIDKTVEIFTIAGQIIQTWDDFNDYYSSSEQNGKLSCDFMNAGTTWVSAKAMEVFTPSQAVKFMECYGSDDQSKMKTVQELYDEIDMPKLYTEYVLENYNRCETLIKELPHDRLREACSSYMEWLVVRETPDEDSEHKVALCLNISG
Protein: Probable serine/threonine-protein kinase BSK3 (EC 2.7.11.1) (Brassinosteroid-signaling kinase 3) (OsBSK3) (Receptor-like cytoplasmic kinase 173) (OsRLCK173) (B9FDE0)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Probable serine/threonine kinase that acts as positive regulator of brassinosteroid (BR) signaling downstream of BRI1.
Subcellular location: Cell membrane {ECO:0000269|PubMed:26697897}; Lipid-anchor {ECO:0000305|PubMed:26697897}. Note=Plasma membrane localization is required for its function in the regulation of brassinosteroid signaling. {ECO:0000269|PubMed:26697897}.
Interaction partners:
- Brassinosteroid LRR receptor kinase BRI1
- 4-coumarate--CoA ligase
- Serine/threonine-protein phosphatase BSL1 homolog
- Os01g0296000 protein.
- non-specific serine/threonine protein kinase
- non-specific serine/threonine protein kinase
- Nuclear pore protein
- Os02g0732700 protein
- Mediator of RNA polymerase II transcription subunit 10
- Os06g0217500 protein
Sequence:
MGGRVSKAVACCCCRSQHHGVVVESSEKTAEEDHGESYELPAFQEFSFEQLRLATSGFAVENIVSEHGEKAPNVVYKGKLDAQRRIAVKRFNRSAWPDPRQFLEEAKSVGQLRSKRLANLLGCCCEGDERLLVAEYMPNDTLAKHLFHWEAQAMKWPMRLRVVLYLAEALEYCTSKGRALYHDLNAYRVLFDDDCNPRLSCFGLMKNSRDGKSYSTNLAFTPPEYMRTGRITPESVIYSFGTLLLDVLSGKHIPPSHALDLIRDRNFNMLTDSCLEGQFSNEEGTELVRLASRCLHYEPRERPNVRSLVQALAPLQKDLETPSYELMDIPRGGATSVQSLLLSPLAEACSRKDLTAIHEILEKTGYKDDEGTANELSFQMWTNQMQDTLNSKKKGDNAFRQKDFSSAIDCYSQFIEVGTMVSPTIYARRCLSYLMNDKAEQALSDAMQALVISPTWPTAFYLQAAALLSLGMENEAQEAIKDGCAHETSSSSGH
Protein: Protein trichome birefringence-like 33 (F4IH21)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable xylan acetyltransferase that plays a role in xylan acetylation and normal deposition of secondary cell walls. Required for 2-O-monoacetylation, 3-O-monoacetylation and 2,3-O-diacetylation of xylosyl residues in xylan. Required for the formation of 3-O-acetylated, 2-O-glucoronic acid-substituted xylosyl residues. May act as a bridging protein that binds pectin and other cell wall polysaccharides. Probably involved in maintaining esterification of pectins (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000305|PubMed:26745802}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
- Glucuronoxylan 4-O-methyltransferase 1
- Protein REDUCED WALL ACETYLATION 2
- UDP-glucuronate:xylan alpha-glucuronosyltransferase 1
- Protein SODIUM POTASSIUM ROOT DEFECTIVE 2
- UDP-glucuronate:xylan alpha-glucuronosyltransferase 2
- Protein REDUCED WALL ACETYLATION 3
- Beta-1,4-xylosyltransferase IRX9
Sequence:
MKPSSPISLTSSSIARKARFSPYLFTLLAFILFVSVLYGEDFMCIFGQLEPNFVLPPSRTPEKNKKSEKLAFAIGKTEESCDVFSGKWVRDEVSRPLYEEWECPYIQPQLTCQEHGRPDKDYQFWRWQPNHCDLPSFNASLMLETLRGKRMMYVGDSLNRGMFVSMICLLHRLIPEDQKSIKTNGSLTVFTAKEYNATIEFYWAPFLLESNSDDAIVHRISDRVVRKGSINKHGRHWKGVDIIIFNTYLWWMTGLKMNILQGSFDDKEKNIVEVSTEDAYRMGMKSMLRWVKNNMDRKKTRVFFTSMSPTHAKGIDWGGEPGQNCYNQTTLIEDPSYWGSDCRKSIMKVIGEVFGRSKTPITLLNITQMSNYRKDAHTSIYKKQWSPLTAEQLENPTSYADCVHWCLPGLQDTWNELLFAKLFYT
Protein: Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase (EC 2.4.1.102) (Core 2 beta-1,6-N-acetylglucosaminyltransferase) (C2GlcNAcT) (Core 2-branching enzyme) (Core2-GlcNAc-transferase) (C2GNT) (Core 2 GNT) (Leukocyte type core 2 beta-1,6-N-acetylglucosaminyltransferase) (C2GnT-L) (Q02742)
Organism: Homo sapiens (Human)
Function: Glycosyltransferase that catalyzes the transfer of an N-acetylglucosamine (GlcNAc) moiety in beta1-6 linkage from UDP-GlcNAc onto mucin-type core 1 O-glycan to form the branched mucin-type core 2 O-glycan. The catalysis is metal ion-independent and occurs with inversion of the anomeric configuration of sugar donor (By similarity). Selectively involved in synthesis of mucin-type core 2 O-glycans that serve as scaffolds for the display of selectin ligand sialyl Lewis X epitope by myeloid cells, with an impact on homeostasis and recruitment to inflammatory sites (By similarity). Can also act on glycolipid substrates. Transfers GlcNAc moiety to GalGb4Cer globosides in a reaction step to the synthesis of stage-specific embryonic antigen 1 (SSEA-1) determinant (By similarity). Can use Galbeta1-3GalNAcalpha1- and Galbeta1-3GalNAcbeta1- oligosaccharide derivatives as acceptor substrates (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:23027862}; Single-pass type II membrane protein {ECO:0000269|PubMed:23027862}. Note=Also detected in the trans-Golgi network.
Interaction partners:
- Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1
- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1
- Acetylgalactosaminyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase
- C1GALT1-specific chaperone 1
- Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 1
- Polypeptide N-acetylgalactosaminyltransferase 12
- Beta-1,4-galactosyltransferase 5
- Polypeptide N-acetylgalactosaminyltransferase 6
- Polypeptide N-acetylgalactosaminyltransferase 4
- Polypeptide N-acetylgalactosaminyltransferase 1
Sequence:
MLRTLLRRRLFSYPTKYYFMVLVLSLITFSVLRIHQKPEFVSVRHLELAGENPSSDINCTKVLQGDVNEIQKVKLEILTVKFKKRPRWTPDDYINMTSDCSSFIKRRKYIVEPLSKEEAEFPIAYSIVVHHKIEMLDRLLRAIYMPQNFYCIHVDTKSEDSYLAAVMGIASCFSNVFVASRLESVVYASWSRVQADLNCMKDLYAMSANWKYLINLCGMDFPIKTNLEIVRKLKLLMGENNLETERMPSHKEERWKKRYEVVNGKLTNTGTVKMLPPLETPLFSGSAYFVVSREYVGYVLQNEKIQKLMEWAQDTYSPDEYLWATIQRIPEVPGSLPASHKYDLSDMQAVARFVKWQYFEGDVSKGAPYPPCDGVHVRSVCIFGAGDLNWMLRKHHLFANKFDVDVDLFAIQCLDEHLRHKALETLKH
Protein: Phenylalanine dehydrogenase (PheDH) (EC 1.4.1.20) (Q59771)
Organism: Rhodococcus sp
Function: Catalyzes the reversible NAD(+)-dependent oxidative deamination of L-phenylalanine to phenylpyruvate.
Interaction partners:
Sequence:
MSIDSALNWDGEMTVTRFDRETGAHFVIRLDSTQLGPAAGGTRAAQYSQLADALTDAGKLAGAMTLKMAVSNLPMGGGKSVIALPAPRHSIDPSTWARILRIHAENIDKLSGNYWTGPDVNTNSADMDTLNDTTEFVFGRSLERGGAGSSAFTTAVGVFEAMKATVAHRGLGSLDGLTVLVQGLGAVGGSLASLAAEAGAQLLVADTDTERVAHAVALGHTAVALEDVLSTPCDVFAPCAMGGVITTEVARTLDCSVVAGAANNVIADEAASDILHARGILYAPDFVANAGGAIHLVGREVLGWSESVVHERAVAIGDTLNQVFEISDNDGVTPDEAARTLAGRRAREASTTTATA
Protein: PUF1 (Q962F5)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MSSDEETITTLYLRRQNILKQLSEVNNEIRTAEQQINEKSNNNETRRVEELVVKFGGDDDRESYLLDFCMRDANGLREAIRYVDALKALKECTSDDEVNRKKHLSRNTFVHAMIARSGELMVDANGSELIQHALGMLKSGGKVAPVLYSTDYIAASESDLSEFLLLLEVLKDKIPQICCDTNGSRAMQKVFDSLKSLEEVEFSAQCFSECIIELCKDIDGNHAVSRLLAAARGTPLWESGAAGDDSSSKLAHIHQLLYGKFPESCVDVCGNRHGCCVIQKCLQWAPEPYFSTLMDTIVHDTIKLVHDPFGNYVIQFILDHEQELSQRSSTGSEGADYTNRIIRQMLHNVAALSCNKFCSNVIEKCLKSATPDVRQLLVDELTDPQILPKLLTDSFANYVIQTAIVTSTEEKQFTQLRDSIMPLQRMLKNSPHGVKVESKLVRQQRELARKNGNQKNKKRWAQPAPQVMEKGMHEGFIGTHILPGMAGIPTIVGTDEFGGPALSLPGVAKEAVPIMTPTQYMPLMLPGQQTLIGLPQGYPQQQFPMDIMKGGNIWDPQQGFTLLHHPESKKGT
Protein: Phosphothreonine lyase OspF (EC 4.2.3.-) (Effector protein OspF) (Q8VSP9)
Organism: Shigella flexneri
Function: Catalyzes the removal of the phosphate group from the phosphothreonine in the mitogen-activated protein kinases such as MAPK2/ERK2, MAPK3/ERK1, MAPK8 and MAPK14 in an irreversible reaction, thus preventing the downstream phosphorylation of histone H3. This epigenetic modification results in inhibition of the transcription of a specific subset of pro-inflammatory genes, and ultimately to a reduced immune response against the invading pathogen. The diminished immune response enhances the bacterium's ability to disseminate and multiply within the host.
Subcellular location: Secreted {ECO:0000269|PubMed:11115111, ECO:0000269|PubMed:16988276, ECO:0000269|PubMed:17159983, ECO:0000269|PubMed:17305427}. Note=Secreted via the type III secretion system (T3SS). Localizes in the nucleus of the infected cell.
Interaction partners:
Sequence:
MPIKKPCLKLNLDSLNVVRSEIPQMLSANERLKNNFNILYNQIRQYPAYYFKVASNVPTYSDICQSFSVMYQGFQIVNHSGDVFIHACRENPQSKGDFVGDKFHISIAREQVPLAFQILSGLLFSEDSPIDKWKITDMNRVSQQSRVGIGAQFTLYVKSDQECSQYSALLLHKIRQFIMCLESNLLRSKIAPGEYPASDVRPEDWKYVSYRNELRSDRDGSERQEQMLREEPFYRLMIE