wanglab/gogpt-training-data huggingface dataset:
Protein: Involucrin (P07476)
Organism: Homo sapiens (Human)
Function: Part of the insoluble cornified cell envelope (CE) of stratified squamous epithelia.
Subcellular location: Cytoplasm. Note=Constituent of the scaffolding of the cornified envelope.
Interaction partners:
- Loricrin
- Filaggrin
- Filaggrin-2
- Protein-glutamine gamma-glutamyltransferase K
- Trichohyalin
- Cornifin-B
- Cornifin-A
- Small proline-rich protein 3
- Keratin, type I cytoskeletal 10
- Keratin, type II cytoskeletal 1
Sequence:
MSQQHTLPVTLSPALSQELLKTVPPPVNTHQEQMKQPTPLPPPCQKVPVELPVEVPSKQEEKHMTAVKGLPEQECEQQQKEPQEQELQQQHWEQHEEYQKAENPEQQLKQEKTQRDQQLNKQLEEEKKLLDQQLDQELVKRDEQLGMKKEQLLELPEQQEGHLKHLEQQEGQLKHPEQQEGQLELPEQQEGQLELPEQQEGQLELPEQQEGQLELPEQQEGQLELPEQQEGQLELPQQQEGQLELSEQQEGQLELSEQQEGQLKHLEHQEGQLEVPEEQMGQLKYLEQQEGQLKHLDQQEKQPELPEQQMGQLKHLEQQEGQPKHLEQQEGQLEQLEEQEGQLKHLEQQEGQLEHLEHQEGQLGLPEQQVLQLKQLEKQQGQPKHLEEEEGQLKHLVQQEGQLKHLVQQEGQLEQQERQVEHLEQQVGQLKHLEEQEGQLKHLEQQQGQLEVPEQQVGQPKNLEQEEKQLELPEQQEGQVKHLEKQEAQLELPEQQVGQPKHLEQQEKHLEHPEQQDGQLKHLEQQEGQLKDLEQQKGQLEQPVFAPAPGQVQDIQPALPTKGEVLLPVEHQQQKQEVQWPPKHK
Protein: Calcium/calmodulin-dependent protein kinase type IV (CaMK IV) (EC 2.7.11.17) (CaM kinase-GR) (Q16566)
Organism: Homo sapiens (Human)
Function: Calcium/calmodulin-dependent protein kinase that operates in the calcium-triggered CaMKK-CaMK4 signaling cascade and regulates, mainly by phosphorylation, the activity of several transcription activators, such as CREB1, MEF2D, JUN and RORA, which play pivotal roles in immune response, inflammation, and memory consolidation. In the thymus, regulates the CD4(+)/CD8(+) double positive thymocytes selection threshold during T-cell ontogeny. In CD4 memory T-cells, is required to link T-cell antigen receptor (TCR) signaling to the production of IL2, IFNG and IL4 (through the regulation of CREB and MEF2). Regulates the differentiation and survival phases of osteoclasts and dendritic cells (DCs). Mediates DCs survival by linking TLR4 and the regulation of temporal expression of BCL2. Phosphorylates the transcription activator CREB1 on 'Ser-133' in hippocampal neuron nuclei and contribute to memory consolidation and long term potentiation (LTP) in the hippocampus. Can activate the MAP kinases MAPK1/ERK2, MAPK8/JNK1 and MAPK14/p38 and stimulate transcription through the phosphorylation of ELK1 and ATF2. Can also phosphorylate in vitro CREBBP, PRM2, MEF2A and STMN1/OP18.
Subcellular location: Cytoplasm. Nucleus. Note=Localized in hippocampal neuron nuclei. In spermatids, associated with chromatin and nuclear matrix (By similarity). {ECO:0000250}.
Interaction partners:
- Calmodulin-like protein 4
- Calmodulin-like protein 5
- Calmodulin-like protein 3
- Calmodulin-like protein 6
- Calmodulin-1
- Cyclic AMP-responsive element-binding protein 1
- Histone deacetylase 4
- Calcium/calmodulin-dependent protein kinase kinase 1
- Calcium/calmodulin-dependent protein kinase kinase 2
- Histone deacetylase 5
Sequence:
MLKVTVPSCSASSCSSVTASAAPGTASLVPDYWIDGSNRDALSDFFEVESELGRGATSIVYRCKQKGTQKPYALKVLKKTVDKKIVRTEIGVLLRLSHPNIIKLKEIFETPTEISLVLELVTGGELFDRIVEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPAPDAPLKIADFGLSKIVEHQVLMKTVCGTPGYCAPEILRGCAYGPEVDMWSVGIITYILLCGFEPFYDERGDQFMFRRILNCEYYFISPWWDEVSLNAKDLVRKLIVLDPKKRLTTFQALQHPWVTGKAANFVHMDTAQKKLQEFNARRKLKAAVKAVVASSRLGSASSSHGSIQESHKASRDPSPIQDGNEDMKAIPEGEKIQGDGAQAAVKGAQAELMKVQALEKVKGADINAEEAPKMVPKAVEDGIKVADLELEEGLAEEKLKTVEEAAAPREGQGSSAVGFEVPQQDVILPEY
Protein: V-type proton ATPase proteolipid subunit (Q384Q8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Vacuole membrane {ECO:0000256|RuleBase:RU363060}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU363060}.
Interaction partners:
- H
- V-type proton ATPase subunit
- Vacuolar proton pump subunit B
- V-type proton ATPase subunit a
- V-type ATPase, C subunit, putative
- Vacuolar ATP synthase subunit D, putative
- ATP synthase, putative
- V-type proton ATPase subunit F
- ATP synthase alpha chain
- V-type proton ATPase subunit H
Sequence:
MLQEVLRLHPLFSASGSSRNLHLYHISSPLLSPLLSLYARTLLTLGCASFAAPMKYSFIGLLSVICVTTVFATVGDGNTTRKEACLARMYPQSAGFFGSLGVAVALIFANLGSAYGAAKSGVGLAQLGLLAPEKIMRGIVPVVMAGILGIYGLIVAVIINNNIKTELYSYSTFSANLHLGAGMAAGLASLAAGLSIGVVGDTTTRAYGKQDQVFVAMVLMLIFSEALGLYGLIIALLMNNQANRYTGLCDSS
Protein: Lipoyl amidotransferase LIPT1, mitochondrial (EC 2.3.1.200) (Lipoate biosynthesis protein) (Lipoate-protein ligase) (Lipoyl ligase) (Lipoyltransferase 1) (EC 2.3.1.-) (Q9Y234)
Organism: Homo sapiens (Human)
Function: Catalyzes the transfer of the lipoyl group from lipoyl-AMP to the specific lysine residue of lipoyl domains of lipoate-dependent enzymes.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:O46419}.
Interaction partners:
- Octanoyl-[acyl-carrier-protein]:protein N-octanoyltransferase LIPT2, mitochondrial
- Lipoyl synthase, mitochondrial
- Glycine cleavage system H protein, mitochondrial
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Acyl-coenzyme A synthetase ACSM1, mitochondrial
- Enoyl-[acyl-carrier-protein] reductase, mitochondrial
- 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial
- Ecto-ADP-ribosyltransferase 3
- U5 small nuclear ribonucleoprotein 40 kDa protein
- Potassium voltage-gated channel subfamily E member 3
Sequence:
MLIPFSMKNCFQLLCNCQVPAAGFKKTVKNGLILQSISNDVYQNLAVEDWIHDHMNLEGKPILFFWQNSPSVVIGRHQNPWQECNLNLMREEGIKLARRRSGGGTVYHDMGNINLTFFTTKKKYDRMENLKLIVRALNAVQPQLDVQATKRFDLLLDGQFKISGTASKIGRTTAYHHCTLLCSTDGTFLSSLLKSPYQGIRSNATASIPSLVKNLLEKDPTLTCEVLMNAVATEYAAYHQIDNHIHLINPTDETLFPGINSKAKELQTWEWIYGKTPKFSINTSFHVLYEQSHLEIKVFIDIKNGRIEICNIEAPDHWLPLEIRDKLNSSLIGSKFCPTETTMLTNILLRTCPQDHKLNSKWNILCEKIKGIM
Protein: Phosphoribosylaminoimidazolecarboxamide formyltransferase, putative (Q726E7)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- Phosphoribosylglycinamide formyltransferase
- IMP cyclohydrolase, putative
- Serine hydroxymethyltransferase
- Adenylosuccinate lyase
- Adenylosuccinate synthetase
- Inosine-5'-monophosphate dehydrogenase
- Formate-dependent phosphoribosylglycinamide formyltransferase
- Bifunctional protein FolD
- Amidophosphoribosyltransferase
- N5-carboxyaminoimidazole ribonucleotide mutase
Sequence:
MRGAGPGGARLRQSARAFKWKLPVVGHCATLSAFRERGARPCRGVVRSSFRRGVMPGLARTWARHGGIPRSASSSQPKSIPEPTMSSLKDMYRTLQQDDFPERMTISFGDRTLVYRKRTWVIDGEAKGLRYGENPDQPAALYELAEGGLELGGVTFRGPGQGLVSALTEEHMVQAGKHPGKTNLTDVDNGINMLQYLTARPAAIILKHNNPSGAAWSDAGIADALSKAFWSDRIAAFGGAVVLNRPLDKAAAELIAANYFEVVAAPDFEEGALDIIKARKNLRILRIPGLARLEEVLADAPFLDVKSLTDGGIVVQHSFRNRIRTVGDFLPATATSKEGVTVTARAPSKQEAEDLLFAWAVESGVTSNSVIFVKDGATVSIGTGEQDRVGCVELAIHKAYTKYADVLAFREQGCSLYELKQKAVADATAAAALADIDERTRAAKGGLIGTSLVSDGFFPFRDGVDCAVAQGVAAIAQPGGSMRDHEVIMALNEATPQVAMVFTGQRSFKH
Protein: Dipeptidyl aminopeptidase B (DPAP B) (EC 3.4.14.-) (YSCV) (P18962)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Vacuole membrane; Single-pass type II membrane protein. Note=Lysosome-like vacuoles.
Interaction partners:
- Carboxypeptidase Y
- Protein transport protein SEC61
- Repressible alkaline phosphatase
- Aminopeptidase Y
- Translocation protein SEC62
- Signal recognition particle subunit SEC65
- Carboxypeptidase S
- Protein transport protein SBH1
- Protein transport protein SBH2
- Signal recognition particle subunit SRP54
Sequence:
MEGGEEEVERIPDELFDTKKKHLLDKLIRVGIILVLLIWGTVLLLKSIPHHSNTPDYQEPNSNYTNDGKLKVSFSVVRNNTFQPKYHELQWISDNKIESNDLGLYVTFMNDSYVVKSVYDDSYNSVLLEGKTFIHNGQNLTVESITASPDLKRLLIRTNSVQNWRHSTFGSYFVYDKSSSSFEEIGNEVALAIWSPNSNDIAYVQDNNIYIYSAISKKTIRAVTNDGSSFLFNGKPDWVYEEEVFEDDKAAWWSPTGDYLAFLKIDESEVGEFIIPYYVQDEKDIYPEMRSIKYPKSGTPNPHAELWVYSMKDGTSFHPRISGNKKDGSLLITEVTWVGNGNVLVKTTDRSSDILTVFLIDTIAKTSNVVRNESSNGGWWEITHNTLFIPANETFDRPHNGYVDILPIGGYNHLAYFENSNSSHYKTLTEGKWEVVNGPLAFDSMENRLYFISTRKSSTERHVYYIDLRSPNEIIEVTDTSEDGVYDVSFSSGRRFGLLTYKGPKVPYQKIVDFHSRKAEKCDKGNVLGKSLYHLEKNEVLTKILEDYAVPRKSFRELNLGKDEFGKDILVNSYEILPNDFDETLSDHYPVFFFAYGGPNSQQVVKTFSVGFNEVVASQLNAIVVVVDGRGTGFKGQDFRSLVRDRLGDYEARDQISAASLYGSLTFVDPQKISLFGWSYGGYLTLKTLEKDGGRHFKYGMSVAPVTDWRFYDSVYTERYMHTPQENFDGYVESSVHNVTALAQANRFLLMHGTGDDNVHFQNSLKFLDLLDLNGVENYDVHVFPDSDHSIRYHNANVIVFDKLLDWAKRAFDGQFVK
Protein: Growth hormone-releasing peptides [Cleaved into: Growth hormone-releasing peptide (GH-releasing peptide) (fGRP); fGRP-related peptide 1; fGRP-related peptide 2; fGRP-related peptide 3] (Q8JIM3)
Organism: Aquarana catesbeiana (American bullfrog) (Rana catesbeiana)
Function: Primary role is to release GH from the pituitary. May act as an endogenous ligand in the bullfrog hypothalamo-hypophysial system.
Subcellular location: Secreted.
Interaction partners:
Sequence:
MHLKIGTLTIRTIMLFTLCTFLTLFAFSTCFDETKTINLESQEIYDDLFESKEDLQNERNGNSDEYRYMGSNSINDINRYNRLSMQPENEFLQERSLKPAANLPLRFGRTSDDKIAKSIPSFDKIAKSIPNLPQRFGRYLSGKTKVQSMANLPQRFGRAQYTNHFVHSLDTLPLRFGRTPHSDRLQYEMNSHPLELKNPEEDSDRKKRQAMTFRIRTDLQM
Protein: GPI-anchor transamidase (GPI transamidase) (EC 3.-.-.-) (Q9USP5)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Mediates GPI anchoring in the endoplasmic reticulum, by replacing a protein's C-terminal GPI attachment signal peptide with a pre-assembled GPI. During this transamidation reaction, the GPI transamidase forms a carbonyl intermediate with the substrate protein (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- GPI transamidase component gaa1
- GPI transamidase component PIG-T homolog
- GPI transamidase component GAB1 homolog
- GPI transamidase component PIG-S homolog
- GPI ethanolamine phosphate transferase 3
- GPI inositol-deacylase
- GPI mannosyltransferase 3
- GPI mannosyltransferase 4
- Probable N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
- Cell division control protein 45 homolog
Sequence:
MIVQFVALLLLNLLQIIAAESSHTNNWAVLISTSRFWFNYRHTANVLGIYRSVKRLGIPDSQIILMIADDYACNSRNLFPGTVFDNADRALDLYGEEIEIDYKGYEVTVEAFIRLLTERVPENTPASKRLLTNERSNILIYMTGHGGDGFIKFQDAEELSSEDLADAIEQIHQHKRYNEILFMVDTCQANSLYTKIYSPNVLAIGSSEVGTSSYSHHADIDIGVAVIDRFTFSNLEFLENRVDSKSKLTMQDLINSYNPYEIHSTPGVQPINLRRSPDDILITDFFGNVRDIELHSEKINWMLPGENTTKPSIKRNSFVFQAQNDMQDDGKGFGISNLKSFLPPTRELKYKKHPISRIISAVVCISFSIGFPYYASKYLK
Protein: Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial (EC 1.3.5.1) (Flavoprotein subunit of complex II) (Fp) (Malate dehydrogenase [quinone] flavoprotein subunit) (EC 1.1.5.-) (Q920L2)
Organism: Rattus norvegicus (Rat)
Function: Flavoprotein (FP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). Can act as a tumor suppressor.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q0QF01}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q0QF01}; Matrix side {ECO:0000250|UniProtKB:Q0QF01}.
Interaction partners:
- Succinate dehydrogenase cytochrome b560 subunit, mitochondrial
- Succinate dehydrogenase cytochrome b small subunit, mitochondrial
- Succinate--CoA ligase subunit alpha, mitochondrial
- Fumarate hydratase, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- NADH dehydrogenase iron-sulfur protein 2, mitochondrial
- NADH dehydrogenase flavoprotein 1, mitochondrial
- Succinate--CoA ligase subunit beta, mitochondrial
- NADH dehydrogenase iron-sulfur protein 8, mitochondrial
- Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial
Sequence:
MAGVGAVSRLLRGRRLALAGATRGFHFSVGESKKASAKVSDAISTQYPVVDHEFDAVVVGAGGAGLRAAFGLSEAGFNTACLTKLFPTRSHTVAAQGGINAALGNMEEDNWRWHFYDTVKGSDWLGDQDAIHYMTEQAPASVVELENYGMPFSRTEDGRIYQRAFGGQSLKFGKGGQAHRCCCVADRTGHSLLHTLYGRSLRYDTSYFVEYFALDLLMENGECRGVIALCIEDGSIHRIRAKNTIIATGGYGRTYFSCTSAHTSTGDGTAMVTRAGLPCQDLEFVQFHPTGIYGAGCLITEGCRGEGGILINSQGERFMERYAPVAKDLASRDVVSRSMTLEIREGRGCGPEKDHVYLQLHHLPPEQLATRLPGISETAMIFAGVDVTKEPIPVLPTVHYNMGGIPTNYKGQVLKHVNGQDQIVPGLYACGEAACASVHGANRLGANSLLDLVVFGRACALSIAESCRPGDKVPPIKANAGEESVMNLDKLRFADGSVRTSELRLSMQKSMQSHAAVFRVGSVLQEGCEKVSQLYGDLQHLKTFDRGMVWNTDLVETLELQNLMLCALQTIYGAEARKESRGAHAREDYKVRIDEYDYSKPIEGQQKKPFAEHWRKHTLSYVDTKTGKVTLDYRPVIDKTLNEADCATVPPAIRSY
Protein: Niemann-Pick type C-2e (Q9VH33)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- GEO08227p1
- NPC intracellular cholesterol transporter 2 homolog a
- GEO07678p1
- Niemann-Pick type C-2g, isoform A
- NPC intracellular cholesterol transporter 1 homolog 1b
- Niemann-Pick type C-1a, isoform A
- Niemann-Pick type C-2c
Sequence:
MLRIVVTLALILATVNATNVQQCKNKPFPLDVNIKDCEEPPCVVYKGTIAVMEVHFLGNNNNIKSITATTTAKVLGMNLPYALPDEVSDVCRNLLYGAICPIDKDEDVTYQFNFYVEPSFPEITADVTVTLNDAQNEPITCFVVSCKIRKGATAAQMDGYLLDWTNPL
Protein: Solute carrier family 30 (Zinc transporter), member 6, isoform CRA_b (Solute carrier family 30 member 6) (B5MCR8)
Organism: Homo sapiens (Human)
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000256|ARBA:ARBA00004166}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004166}.
Interaction partners:
Sequence:
MTCLISYWVTLRKPSPVYSFGFERLEVLAVFASTVLAQLGALFILKESAERFLEQPEIHTGRLLVGTFVALCFNLFTMLSIRNKPFAYVSEAASTSWLQEHVADLSRSLCGIIPGLSSIFLPRMNPFVLIDLAGAFALCITYMLIEINNYFAVDTASAIAIALMTFGTMYPMSVYSGKVLLQTTPPHVIGQLDKLIREVSTLDGVLEVRNEHFWTLGFGSLAGSVHVRIRRDANEQMVLAHVTNRLYTLVSTLTVQIFKDDWIRPALLSGPVAANVLNFSDHHVIPMPLLKGTDDLNPVTSTPAKPSSPPPEFSFNTPGKNVNPVILLNTQTRPYGFGLNHGHTPYSSMLNQGLGVPGIGATQGLRTGFTNIPSRYGTNNRIGQPRP
Protein: Enhancer of split m8 protein (E(spl)m8) (P13098)
Organism: Drosophila melanogaster (Fruit fly)
Function: Participates in the control of cell fate choice by uncommitted neuroectodermal cells in the embryo. Transcriptional repressor. Binds DNA on N-box motifs: 5'-CACNAG-3'. Part of the Notch signaling pathway.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Enhancer of split m7 protein
- Protein groucho
- Enhancer of split m4 protein
- Dpr-interacting protein gamma
- Achaete-scute complex protein T5
- Neurogenic locus Notch protein
- Achaete-scute complex protein T4
- Sphingosine-1-phosphate lyase
- Defective proboscis extension response 11, isoform B
- Enhancer of split m5 protein
Sequence:
MEYTTKTQIYQKVKKPMLERQRRARMNKCLDNLKTLVAELRGDDGILRMDKAEMLESAVIFMRQQKTPKKVAQEEQSLPLDSFKNGYMNAVNEVSRVMASTPGMSVDLGKSVMTHLGRVYKNLQQFHEAQSAADFIQNSMDCSSMDKAPLSPASSGYHSDCDSPAPSPQPMQQPLWRPW
Protein: Repulsive guidance molecule BMP co-receptor a (D4A188)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
- Neogenin
- Serine/threonine-protein kinase receptor
- Bone morphogenetic protein receptor type-1A
- Activin receptor type-1
- Repulsive guidance molecule BMP co-receptor b
- Bone morphogenetic protein 4
- Bone morphogenetic protein 2
- Netrin-1
- Growth/differentiation factor 5
- Netrin receptor DCC
Sequence:
MQPPRERLVVTGRAGWMGMGRGAGRSALGLWPTLAFLLCSFPAAISPCKILKCNSEFWSATSSGSHAPASDDVPEFCAALRTYALCTRRTARTCRGDLAYHSAVHGIEDLMSQHNCSKDGPTSQPRVRTLPPAGDSQERSDSPEICHYEKSFHKHSAAPNYTHCGLFGDPHLRTFTDHFQTCKVQGAWPLIDNNYLNVQVTNTPVLPGSAATATSKLTIIFKNFQECVDQKVYQAEMDELPSAFADGSKNGGDKHGANSLKITEKVSGQHVEIQAKYIGTTIVVRQVGRYLTFAVRMPEEVVNAVEDRDSQGLYLCLRGCPLNQQIDFQAFRANAESPRRPAAASPSPVVPETFPYETAVAKCKEKLPVEDLYYQACVFDLLTTGDVNFTLAAYYALEDGKMLHSNKDKLHLFERTRELPGAVAAAAFPLAPEMLPGTVTLLVLLPLFW
Protein: D-glucoside 3-dehydrogenase (EC 1.1.1.-) (P77503)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the NADH-dependent reduction of the oxo group at C3 of 3-dehydro-D-glucosides leading to D-glucosides. Probably functions in a metabolic pathway that transforms D-gulosides to D-glucosides. Can use 3-dehydro-D-glucose, methyl alpha-3-dehydro-D-glucoside and methyl beta-3-dehydro-D-glucoside as substrates in vitro. However, the actual specific physiological substrates for this metabolic pathway are unknown. To a lesser extent, is also able to catalyze the reverse reactions, i.e. the NAD(+)-dependent oxidation of the hydroxyl group at C3 of D-glucosides leading to 3-dehydro-D-glucosides. Cannot act on UDP-glucose, UDP-N-acetyl-D-glucosamine, D-glucosamine, N-acetyl-D-glucosamine, or UDP-D-galactose.
Interaction partners:
- 3-dehydro-D-guloside 4-epimerase
- D-guloside 3-dehydrogenase
- Putative ABC transporter periplasmic-binding protein YcjN
- Inner membrane ABC transporter permease protein YcjO
- Inner membrane ABC transporter permease protein YcjP
- Kojibiose phosphorylase
- Beta-phosphoglucomutase
- Glucosylglycerate phosphorylase
- Uncharacterized HTH-type transcriptional regulator YcjW
- Putative oxidoreductase YceM
Sequence:
MKSAMTSSPLRVAIIGAGQVADKVHASYYCTRNDLELVAVCDSRLSQAQALAEKYGNASVWDDPQAMLLAVKPDVVSVCSPNRFHYEHTLMALEAGCHVMCEKPPAMTPEQAREMCDTARKLGKVLAYDFHHRFALDTQQLREQVTNGVLGEIYVTTARALRRCGVPGWGVFTNKELQGGGPLIDIGIHMLDAAMYVLGFPAVKSVNAHSFQKIGTQKSCGQFGEWDPATYSVEDSLFGTIEFHNGGILWLETSFALNIREQSIMNVSFCGDKAGATLFPAHIYTDNNGELMTLMQREIADDNRHLRSMEAFINHVQGKPVMIADAEQGYIIQQLVAALYQSAETGTRVEL
Protein: Bidirectional sugar transporter SWEET14 (OsSWEET14) (Q2R3P9)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Mediates both low-affinity uptake and efflux of sugar across the plasma membrane.
Subcellular location: Cell membrane {ECO:0000269|PubMed:21107422}; Multi-pass membrane protein {ECO:0000269|PubMed:21107422}.
Interaction partners:
Sequence:
MAGMSLQHPWAFAFGLLGNIISFMTYLAPLPTFYRIYKSKSTQGFQSVPYVVALFSAMLWIYYALLKSDECLLITINSAGCVIETIYIAVYLVYAPKKAKMFTAKLLLLVNVGVFGLILLLTLLLSAGDRRIVVLGWVCVGFSVSVFVAPLSIIRLVVRTKSVEFMPFSLSFSLTISAVVWFLYGLLIKDKYVALPNVLGFSFGVIQMGLYAMYRNSTPKAVLTKEVEAATATGDDDHSAAGVKEHVVNIAKLSAAVDVVKTREVHPVDVESPPAEAPPEEDDKAAAATAAAVAGAGEKKVAA
Protein: Class I peptide chain release factor (Putative peptide chain release factor) (Q9C875)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- At5g64156
- AT3g13440/MRP15_7
- Translation elongation factor EF1B/ribosomal protein S6 family protein
- 50S ribosomal protein L33
- Large ribosomal subunit protein bL31c
- 50S ribosomal protein L20
- Large ribosomal subunit protein bL20c
- Ribosomal protein L25/Gln-tRNA synthetase, anti-codon-binding domain-containing protein
- Large ribosomal subunit protein bL27c
- AT5g15220/F8M21_110
Sequence:
MAIMAVAALFHARFPLLLRRSIPLLSAPTSVIYNHRTLLSDGLSTRLCSILRYSSSDGVNGGSSGGDFGNDNDSVSVVSDVQSPNYLKFTDEELMKQCRLETFRVSGPGGQHRNKRDSAVRLKHLPTGIVAQAVEDRSQHKNRASALNRLRTLLAIKVRNKVDIEAYAPPPELLQILPPKSTIRTSSGSQIGPNNPKFVPGMQALLDVISASDGSIADSAKLLGLSTGGLSRLILSHDGLRMAVNSMRAAKGIKPLK
Protein: RNA helicase (EC 3.6.4.13) (Q38CI6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- RNA-binding protein, putative
- RRM domain-containing protein
- MI domain-containing protein
- Peptidyl-prolyl cis-trans isomerase
- ATP-dependent DEAD/H RNA helicase, putative
- Pre-mRNA-splicing factor SLU7
- Peptidyl-prolyl cis-trans isomerase
- peptidylprolyl isomerase
- Pre-mRNA splicing factor, putative
- Probable eukaryotic initiation factor 4A
Sequence:
MSSGLADFDGDDVRAPVVAAQPHIGVGLGTHSAVALGGFQDFCLKSELANAIRENGFEHPSEVQHQALPQAMLGADILAQAKSGMGKTAVFVFALLEQVEKPTDGQRPFCQAIVIAHARELAYQIEQEFKRFNKYLPHCTTGVFFGGVPEDENIKQLKKEVPAIVVATPGRICSLIERKALDVSRVKWFVVDEFDRCLEDVKMRRDVQTAFLKTPKEKQVMMFSATMTEELRNVAKKFMSNPTEIYVDQRSKLTLHGLAQYYINVTEAQKLRKLCDILDAVEFNQVIIFTSTVERCEALSRQLQALKFPSKAIHSRMEQAERLVVYESCKTNQARIIVATDIFGRGVDIDRINLVVQFDMASDADSYLHRVGRAGRFGTKGLTVAFLTEEEKEIKRENRKYTDQGIMKEVQERFEMQVQELTDIATQLNQSQYMNQ
Protein: Integral membrane protein SED5 (Q01590)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for vesicular transport between the endoplasmic reticulum and the Golgi complex. Acts as a target organelle soluble NSF attachment protein receptor (t-SNARE).
Subcellular location: Membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}. Golgi apparatus membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}.
Interaction partners:
- Protein transport protein SEC22
- Protein transport protein SFT1
- Golgi SNAP receptor complex member 1
- Synaptobrevin homolog YKT6
- Protein SLY1
- Synaptobrevin homolog 2
- Protein transport protein BET1
- t-SNARE VTI1
- Protein transport protein BOS1
- Vacuolar v-SNARE NYV1
Sequence:
MNIKDRTSEFQQSVLSYKKRNKNFREQQRERLQEKESENFANNTTGNGKSVSEFQKKASGIAHEISSTAQLLSKLAVLAKRKPMFNDNPVEIAELSFLIKRKIYAIEQSLVQLSQLKKTDVNGNTSNQSSKQPSAVQHSKNVVNLLNTQMKNISGSFKDVLEERQRLEMANKDRWQKLTTDTGHAPADDQTQSNHAADLTTYNNSNPFMTSLLDESSEKNNNSSNQGELSFPQNDSQLMLMEEGQLSNNVYLQERNRAVETIESTIQEVGNLFQQLASMVQEQGEVIQRIDANVDDIDLNISGAQRELLKYFDRIKSNRWLAAKVFFIIFVFFVIWVLVN
Protein: Chondroitin sulfate synthase 2 (EC 2.4.1.175) (EC 2.4.1.226) (Chondroitin glucuronyltransferase 2) (Chondroitin-polymerizing factor) (ChPF) (Glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase II) (N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase II) (N-acetylgalactosaminyltransferase 2) (Q8IZ52)
Organism: Homo sapiens (Human)
Function: Has both beta-1,3-glucuronic acid and beta-1,4-N-acetylgalactosamine transferase activity. Transfers glucuronic acid (GlcUA) from UDP-GlcUA and N-acetylgalactosamine (GalNAc) from UDP-GalNAc to the non-reducing end of the elongating chondroitin polymer. Seems to act as a specific activating factor for CHSY1 in chondroitin polymerization.
Subcellular location: [Isoform 1]: Golgi apparatus, Golgi stack membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Cytoplasm, cytosol {ECO:0000269|PubMed:22082830}.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm, cytosol {ECO:0000269|PubMed:22082830}. Mitochondrion {ECO:0000269|PubMed:22082830}.; SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion matrix {ECO:0000269|PubMed:22082830}.
Interaction partners:
- Chondroitin sulfate synthase 1
- Chondroitin sulfate N-acetylgalactosaminyltransferase 1
- Chondroitin sulfate N-acetylgalactosaminyltransferase 2
- Chondroitin sulfate synthase 3
- Chondroitin sulfate glucuronyltransferase
- Beta-1,4 N-acetylgalactosaminyltransferase 1
Sequence:
MRASLLLSVLRPAGPVAVGISLGFTLSLLSVTWVEEPCGPGPPQPGDSELPPRGNTNAARRPNSVQPGAEREKPGAGEGAGENWEPRVLPYHPAQPGQAAKKAVRTRYISTELGIRQRLLVAVLTSQTTLPTLGVAVNRTLGHRLERVVFLTGARGRRAPPGMAVVTLGEERPIGHLHLALRHLLEQHGDDFDWFFLVPDTTYTEAHGLARLTGHLSLASAAHLYLGRPQDFIGGEPTPGRYCHGGFGVLLSRMLLQQLRPHLEGCRNDIVSARPDEWLGRCILDATGVGCTGDHEGVHYSHLELSPGEPVQEGDPHFRSALTAHPVRDPVHMYQLHKAFARAELERTYQEIQELQWEIQNTSHLAVDGDQAAAWPVGIPAPSRPASRFEVLRWDYFTEQHAFSCADGSPRCPLRGADRADVADVLGTALEELNRRYHPALRLQKQQLVNGYRRFDPARGMEYTLDLQLEALTPQGGRRPLTRRVQLLRPLSRVEILPVPYVTEASRLTVLLPLAAAERDLAPGFLEAFATAALEPGDAAAALTLLLLYEPRQAQRVAHADVFAPVKAHVAELERRFPGARVPWLSVQTAAPSPLRLMDLLSKKHPLDTLFLLAGPDTVLTPDFLNRCRMHAISGWQAFFPMHFQAFHPAVAPPQGPGPPELGRDTGRFDRQAASEACFYNSDYVAARGRLAAASEQEEELLESLDVYELFLHFSSLHVLRAVEPALLQRYRAQTCSARLSEDLYHRCLQSVLEGLGSRTQLAMLLFEQEQGNST