wanglab/gogpt-training-data huggingface dataset:
Protein: CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1 (Alpha 2,3-ST 1) (Beta-galactoside alpha-2,3-sialyltransferase 1) (EC 2.4.3.4) (Gal-NAc6S) (Gal-beta-1,3-GalNAc-alpha-2,3-sialyltransferase) (Monosialoganglioside sialyltransferase) (EC 2.4.3.2) (ST3Gal I) (ST3GalI) (ST3GalA.1) (ST3O) (Sialyltransferase 4A) (SIAT4-A) (Q02745)
Organism: Sus scrofa (Pig)
Function: A beta-galactoside alpha2-3 sialyltransferase involved in terminal sialylation of glycoproteins and glycolipids. Catalyzes the transfer of sialic acid (N-acetyl-neuraminic acid; Neu5Ac) from the nucleotide sugar donor CMP-Neu5Ac onto acceptor Galbeta-(1->3)-GalNAc-terminated glycoconjugates through an alpha2-3 linkage. Adds sialic acid to the core 1 O-glycan, Galbeta-(1->3)-GalNAc-O-Ser/Thr, which is a major structure of mucin-type O-glycans. As part of a homeostatic mechanism that regulates CD8-positive T cell numbers, sialylates core 1 O-glycans of T cell glycoproteins, SPN/CD43 and PTPRC/CD45. Prevents premature apoptosis of thymic CD8-positive T cells prior to peripheral emigration, whereas in the secondary lymphoid organs controls the survival of CD8-positive memory T cells generated following a successful immune response (By similarity). Transfers sialic acid to asialofetuin, presumably onto Galbeta-(1->3)-GalNAc-O-Ser. Sialylates GM1a, GA1 and GD1b gangliosides to form GD1a, GM1b and GT1b, respectively (By similarity).
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:Q11201}; Single-pass type II membrane protein {ECO:0000255}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q11201}; Single-pass type II membrane protein {ECO:0000255}. Secreted. Note=Membrane-bound form in medial and trans cisternae of Golgi (By similarity). Secreted into the body fluid. {ECO:0000250|UniProtKB:Q11201}.
Interaction partners:
- Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase
- Glucosaminyl
- Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1
- alpha-N-acetylneuraminyl-2,3-beta-galactosyl-1,3-N-acetylgalactosaminide6-alpha-sialyltransferase
- Galactoside alpha-
- Hexosyltransferase
- Hexosyltransferase
- Galactoside alpha-
- Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 3
- alpha-N-acetylneuraminyl-2,3-beta-galactosyl-1,3-N-acetylgalactosaminide6-alpha-sialyltransferase
Sequence:
MAPMRKKSTLKLLTLLVLFIFLTSFFLNYSHTVVTTAWFPKQMVIELSENFKKLMKYPYRPCTCTRCIEEQRVSAWFDERFNRSMQPLLTAKNAHLEEDTYKWWLRLQREKQPNNLNDTIRELFQVVPGNVDPLLEKRLVSCRRCAVVGNSGNLKESYYGPQIDSHDFVLRMNKAPTEGFEADVGSKTTHHFVYPESFRELAQEVSMILVPFKTTDLEWVISATTTGRISHTYVPVPAKIKVKKEKILIYHPAFIKYVFDRWLQGHGRYPSTGILSVIFSLHICDEVDLYGFGADSKGNWHHYWENNPSAGAFRKTGVHDGDFESNVTTILASINKIRIFKGR
Protein: Ephrin type-A receptor 4a (EC 2.7.10.1) (EPH-like kinase 2) (Tyrosine-protein kinase receptor ZEK2) (O13148)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Receptor tyrosine kinase which binds membrane-bound ephrin family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Highly promiscuous, it has the unique property among Eph receptors to bind and to be physiologically activated by both GPI-anchored ephrin-A and transmembrane ephrin-B ligands including efna1 and efnb3. Upon activation by ephrin ligands, modulates cell morphology and integrin-dependent cell adhesion through regulation of the Rac, Rap and Rho GTPases activity. Plays an important role in the development of the nervous system controlling different steps of axonal guidance including the establishment of the corticospinal projections (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q03137}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q03137}. Early endosome {ECO:0000250|UniProtKB:Q03137}. Note=Clustered upon activation and targeted to early endosome. {ECO:0000250|UniProtKB:Q03137}.
Interaction partners:
- Ephrin-A2
- Ephrin-A3
- Ephrin-A5b
- Ephrin-A3a
- Ephrin-A1
- Si:dkey-246i14.3
- Ephrin-A2b
- Ephrin-A1
- Ephrin-B1
- Ephrin-B2a
Sequence:
IGIGEFGEVCSGRLKMPGKREICVAIKTLKAGYTDKQRRDFLSEASIMGQFDHPNIIRLEGVVTKCKPVMIITEYMENGSLDAFLRKNDGRFTVIQLVGILRGIASGMKYLSDMSYVHRDLAARNILVNSNLVCKVSDFGMSRVLEEDPDAAYTTREITGTYQSQGGKIPIRWTAPEAITYRKFTSASDVWSYGIVMWEVMSYGERPYWDMSNQDVIKAIEEGYRLPPPMDCPVSLHQLMLDCWQKERAERPKFSQIVNMLDKLIRNPNSLKRTGGEIARPNTTLLEPSSPE
Protein: H/ACA ribonucleoprotein complex non-core subunit NAF1 (Nuclear assembly factor 1) (P53919)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: RNA-binding protein required for the maturation of box H/ACA snoRNPs complex and ribosome biogenesis. During assembly of the H/ACA snoRNPs complex, it associates with the complex and disappears during maturation of the complex and is replaced by GAR1 to yield mature H/ACA snoRNPs complex. Acts as a competitive binder for CBF5 probably required to prevent non-cognate RNAs from being loaded during transport of the particle by inducing a non-productive conformation of CBF5.
Subcellular location: Nucleus {ECO:0000269|PubMed:12228251, ECO:0000269|PubMed:12242285, ECO:0000269|PubMed:12515383, ECO:0000269|PubMed:14562095}. Note=Mostly present in the nucleoplasm. Absent from the nucleolus. {ECO:0000269|PubMed:12228251}.
Interaction partners:
- H/ACA ribonucleoprotein complex subunit CBF5
- H/ACA ribonucleoprotein complex subunit NHP2
- H/ACA ribonucleoprotein complex subunit NOP10
- Protein NAM8
- U1 small nuclear ribonucleoprotein A
- H/ACA ribonucleoprotein complex subunit GAR1
- Protein SHQ1
- Proteasome-interacting protein CIC1
- Nucleolar protein 58
- rRNA 2'-O-methyltransferase fibrillarin
Sequence:
MSDDLFSKALENPDQDLNVELPKDDVDLGLLGDGGNERKTDEPVADAERSTGLGSGSSESESDSGSDSDSDSGSSGSEDDSADQDVEGEDEGGDAIENEDEDEDPSPSGPILSKNEILEETVPELPEDYEISEKTIITPIGVLKSAFENNIIIHATMSGEKRVLKEGSIFCLEDRTLIGMLTEVFGPLQNPFYRIKLPDSKKNLFDELKVRLGEKAFIVTPDAHWIDTFELKRNKGTDASNGYDEELPEEEQEFSDDEKEALFKKMKKQQRQRKKRDNRKLANDSDNVKVKRARQPKANSLPKLVPPLGMSSNAPMQHGYKSRNARENIKRESSATSNRNGSSPVPITQHHQQQFSANNYPFPQQPNGMPYPPYSPFPQPTNFQYPPPPFGQATPAQFSNTVPYGSLPPAYNNMSPPTQQSFMPMTQSQPPLPYGVPPMNQMQNPMYIQPPPQAPPQGNGNFQQVMELHQILLQQQQQQHQYQHQHQQDPRT
Protein: Protein farnesyltransferase subunit beta (FTase-beta) (EC 2.5.1.58) (CAAX farnesyltransferase subunit beta) (Ras proteins prenyltransferase subunit beta) (P49356)
Organism: Homo sapiens (Human)
Function: Essential subunit of the farnesyltransferase complex. Catalyzes the transfer of a farnesyl moiety from farnesyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X.
Interaction partners:
- Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
- CAAX prenyl protease 2
- CAAX prenyl protease 1 homolog
- Geranylgeranyl pyrophosphate synthase
- Farnesyl pyrophosphate synthase
- Dehydrodolichyl diphosphate synthase complex subunit DHDDS
- All trans-polyprenyl-diphosphate synthase PDSS1
- All trans-polyprenyl-diphosphate synthase PDSS2
- Dehydrodolichyl diphosphate synthase complex subunit NUS1
- Protein Churchill
Sequence:
MASPSSFTYYCPPSSSPVWSEPLYSLRPEHARERLQDDSVETVTSIEQAKVEEKIQEVFSSYKFNHLVPRLVLQREKHFHYLKRGLRQLTDAYECLDASRPWLCYWILHSLELLDEPIPQIVATDVCQFLELCQSPEGGFGGGPGQYPHLAPTYAAVNALCIIGTEEAYDIINREKLLQYLYSLKQPDGSFLMHVGGEVDVRSAYCAASVASLTNIITPDLFEGTAEWIARCQNWEGGIGGVPGMEAHGGYTFCGLAALVILKRERSLNLKSLLQWVTSRQMRFEGGFQGRCNKLVDGCYSFWQAGLLPLLHRALHAQGDPALSMSHWMFHQQALQEYILMCCQCPAGGLLDKPGKSRDFYHTCYCLSGLSIAQHFGSGAMLHDVVLGVPENALQPTHPVYNIGPDKVIQATTYFLQKPVPGFEELKDETSAEPATD
Protein: Tight junction protein ZO-3 (Tight junction protein 3) (Zona occludens protein 3) (Zonula occludens protein 3) (O95049)
Organism: Homo sapiens (Human)
Function: TJP1, TJP2, and TJP3 are closely related scaffolding proteins that link tight junction (TJ) transmembrane proteins such as claudins, junctional adhesion molecules, and occludin to the actin cytoskeleton. The tight junction acts to limit movement of substances through the paracellular space and as a boundary between the compositionally distinct apical and basolateral plasma membrane domains of epithelial and endothelial cells. Binds and recruits PATJ to tight junctions where it connects and stabilizes apical and lateral components of tight junctions. Promotes cell-cycle progression through the sequestration of cyclin D1 (CCND1) at tight junctions during mitosis which prevents CCND1 degradation during M-phase and enables S-phase transition. With TJP1 and TJP2, participates in the junctional retention and stability of the transcription factor DBPA, but is not involved in its shuttling to the nucleus (By similarity). Contrary to TJP2, TJP3 is dispensable for individual viability, embryonic development, epithelial differentiation, and the establishment of TJs, at least in the laboratory environment (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:21411630}; Peripheral membrane protein {ECO:0000269|PubMed:21411630}; Cytoplasmic side {ECO:0000269|PubMed:21411630}. Cell junction, tight junction {ECO:0000269|PubMed:21411630, ECO:0000269|PubMed:23608536}. Nucleus {ECO:0000269|PubMed:23608536}. Note=Exhibits predominant nuclear expression in proliferating cells but is exclusively junctionally expressed after confluence is reached (PubMed:23608536). Shows an epithelial-specific tight junction localization in a TJP1/TJP2-dependent fashion (By similarity). {ECO:0000250|UniProtKB:Q9QXY1, ECO:0000269|PubMed:23608536}.
Interaction partners:
- Occludin
- Cingulin
- Claudin-1
- InaD-like protein
- MARVEL domain-containing protein 2
- Claudin-7
- Tight junction protein 1
- Claudin-3
- Tight junction protein 2
- Claudin-8
Sequence:
MEELTIWEQHTATLSKDPRRGFGIAISGGRDRPGGSMVVSDVVPGGPAEGRLQTGDHIVMVNGVSMENATSAFAIQILKTCTKMANITVKRPRRIHLPATKASPSSPGRQDSDEDDGPQRVEEVDQGRGYDGDSSSGSGRSWDERSRRPRPGRRGRAGSHGRRSPGGGSEANGLALVSGFKRLPRQDVQMKPVKSVLVKRRDSEEFGVKLGSQIFIKHITDSGLAARHRGLQEGDLILQINGVSSQNLSLNDTRRLIEKSEGKLSLLVLRDRGQFLVNIPPAVSDSDSSPLEDISDLASELSQAPPSHIPPPPRHAQRSPEASQTDSPVESPRLRRESSVDSRTISEPDEQRSELPRESSYDIYRVPSSQSMEDRGYSPDTRVVRFLKGKSIGLRLAGGNDVGIFVSGVQAGSPADGQGIQEGDQILQVNDVPFQNLTREEAVQFLLGLPPGEEMELVTQRKQDIFWKMVQSRVGDSFYIRTHFELEPSPPSGLGFTRGDVFHVLDTLHPGPGQSHARGGHWLAVRMGRDLREQERGIIPNQSRAEQLASLEAAQRAVGVGPGSSAGSNARAEFWRLRGLRRGAKKTTQRSREDLSALTRQGRYPPYERVVLREASFKRPVVILGPVADIAMQKLTAEMPDQFEIAETVSRTDSPSKIIKLDTVRVIAEKDKHALLDVTPSAIERLNYVQYYPIVVFFIPESRPALKALRQWLAPASRRSTRRLYAQAQKLRKHSSHLFTATIPLNGTSDTWYQELKAIIREQQTRPIWTAEDQLDGSLEDNLDLPHHGLADSSADLSCDSRVNSDYETDGEGGAYTDGEGYTDGEGGPYTDVDDEPPAPALARSSEPVQADESQSPRDRGRISAHQGAQVDSRHPQGQWRQDSMRTYEREALKKKFMRVHDAESSDEDGYDWGPATDL
Protein: At2g27890 (Coiled-coil protein) (Q8RXC2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Vacuolar protein sorting-associated protein 51 homolog
- Vacuolar protein sorting-associated protein 53 A
- Vacuolar protein sorting-associated protein 52 A
- Vacuolar protein sorting-associated protein 53 B
- Vacuolar protein sorting-associated protein 54, chloroplastic
- Probable magnesium transporter NIPA4
- Vacuolar protein sorting-associated protein 52 B
- WD repeat-containing protein DWA2
- Transducin/WD40 repeat-like superfamily protein
- Protein PARALOG OF AIPP2
Sequence:
MQPNLFFPFGSVLGNPFLFNGGGDLNELGSGAAFESSRVFFLLPFLLSQGTGVMDLSKVGEKFLSSVKSATSLGLLPSPSISDRPEIPARAAAAAAVARALAGLPSDQRLSISSTATELNSIYGNRPLPQQVEELEEGFYEEDFDPVRHILENVPDDESELAYFEKQATLRLVQLDKVAETLSHHVMEHHEVMVKGMNLVRELEKDLKIANVICKNGRRNLTSSMNEASRDLIVHTHSKKKQALLDMLPILTDLRHARVMQSNLEDLVEDGNYCKAFQVLSEYLQLLDSLSEFSAAQEMTRGVEVWLGRTLHKLDSLLLGVCQEFKEDSYVMVLDAYALIGDVSGLAEKIQSFFMQEVISETHSVLKSIVGEDNSAATQYSRLTYSDLCLQTPESKFRQCLLRTLAVLFQLIYSYHEIMSFTPEKEAEILVSPSLATTQMVDSVTGSSCDPQDGGLLPGSIPPCTISAEESDGSGTSSSVQLASNIAIDESRNSEDRVSSSESPWYYLRKESAAFVSETLQRGRRNLWQLTTSRVSVLLSSPGASSTSIHQFLKNYEDLSIFILAGEAFCGFEVVDFREKLKGVCENYFTAFHRQSMHALKMVLEKETWTKLSPDTVQAINFAGLVGDGAPLIISSRSASGSSRFPHSDKPSNSIDPSGNRSGFSYWLKSGNPFSAKLTHYREDQDYSSINGEDHEGNDSIHDDVVNPKIRDIKRINGGSPVSEDENEDLLADFIDEDSQLPRRSFTRSQSRTSSSHFSTNDDLTAQTGSSLCLLRSMDKYARLMQKLEIVNAEFFKGICQLFGVFFYFVFQVFGQENTNSGGKGVSDSFNHRLKSCLSRISQECEQWIKPHVSSSPSSSLAFPNTVHSLADVTPASPLNTSGHLSGVSFSLKERCAAVDTVSLVARVLHKSKAHLQSMLMSRNGSLVEDFFGQLVGSVPDLTEHLHRTTARILLHVNGYVDRIANSKWEIKELGMEHNGYVDLMLGEFKHYKTRLAHGGIPQEVQNLLLEYGVEIFAEMLVEGLSRIKRCTDEGRVLMSLDLQVLINGLQHFVPTKVKPKLQIVETFIKAYYLPETEYVHWARAHPEYTKAQVVGLVNLVATMKGWKRKTRLEVIEKIESASM
Protein: Oxysterol-binding protein-related protein 1 (ORP-1) (OSBP-related protein 1) (Q9BXW6)
Organism: Homo sapiens (Human)
Function: Binds phospholipids; exhibits strong binding to phosphatidic acid and weak binding to phosphatidylinositol 3-phosphate (By similarity). Stabilizes GTP-bound RAB7A on late endosomes/lysosomes and alters functional properties of late endocytic compartments via its interaction with RAB7A. Binds 25-hydroxycholesterol and cholesterol.
Subcellular location: Late endosome {ECO:0000269|PubMed:16176980, ECO:0000269|PubMed:29858488}. Note=Colocalizes with RAB7A, RAB9A and LAMP1 in late endosomes.
Interaction partners:
- Ras-related protein Rab-7a
- Motile sperm domain-containing protein 2
- Rab-interacting lysosomal protein
- Vesicle-associated membrane protein-associated protein A
- Vesicle-associated membrane protein-associated protein B/C
Sequence:
MNTEAEQQLLHHARNGNAEEVRQLLETMARNEVIADINCKGRSKSNLGWTPLHLACYFGHRQVVQDLLKAGAEVNVLNDMGDTPLHRAAFTGRKELVMLLLEYNADTTIVNGSGQTAKEVTHAEEIRSMLEAVERTQQRKLEELLLAAAREGKTTELTALLNRPNPPDVNCSDQLGNTPLHCAAYRAHKQCALKLLRSGADPNLKNKNDQKPLDLAQGAEMKHILVGNKVIYKALKRYEGPLWKSSRFFGWRLFWVVLEHGVLSWYRKQPDAVHNIYRQGCKHLTQAVCTVKSTDSCLFFIKCFDDTIHGFRVPKNSLQQSREDWLEAIEEHSAYSTHYCSQDQLTDEEEEDTVSAADLKKSLEKAQSCQQRLDREISNFLKMIKECDMAKEMLPSFLQKVEVVSEASRETCVALTDCLNLFTKQEGVRNFKLEQEQEKNKILSEALETLATEHHELEQSLVKGSPPASILSEDEFYDALSDSESERSLSRLEAVTARSFEEEGEHLGSRKHRMSEEKDCGGGDALSNGIKKHRTSLPSPMFSRNDFSIWSILRKCIGMELSKITMPVIFNEPLSFLQRLTEYMEHTYLIHKASSLSDPVERMQCVAAFAVSAVASQWERTGKPFNPLLGETYELVRDDLGFRLISEQVSHHPPISAFHAEGLNNDFIFHGSIYPKLKFWGKSVEAEPKGTITLELLEHNEAYTWTNPTCCVHNIIVGKLWIEQYGNVEIINHKTGDKCVLNFKPCGLFGKELHKVEGYIQDKSKKKLCALYGKWTECLYSVDPATFDAYKKNDKKNTEEKKNSKQMSTSEELDEMPVPDSESVFIIPGSVLLWRIAPRPPNSAQMYNFTSFAMVLNEVDKDMESVIPKTDCRLRPDIRAMENGEIDQASEEKKRLEEKQRAARKNRSKSEEDWKTRWFHQGPNPYNGAQDWIYSGSYWDRNYFNLPDIY
Protein: Flagellin (Q7DBI0)
Organism: Escherichia coli O157:H7
Subcellular location: Secreted {ECO:0000256|RuleBase:RU362073}. Bacterial flagellum {ECO:0000256|RuleBase:RU362073}.
Interaction partners:
Sequence:
MAQVINTNSLSLITQNNINKNQSALSSSIERLSSGLRINSAKDDAAGQAIANRFTSNIKGLTQAARNANDGISVAQTTEGALSEINNNLQRIRELTVQATTGTNSDSDLDSIQDEIKSRLDEIDRVSGQTQFNGVNVLAKDGSMKIQVGANDGETITIDLKKIDSDTLGLNGFNVNGKGTITNKAATVSDLTSAGAKLNTTTGLYDLKTENTLLTTDAAFDKLGNGDKVTVGGVDYTYNAKSGDFTTTKSTAGTGVDAAAQAADSASKRDALAATLHADVGKSVNGSYTTKDGTVSFETDSAGNITIGGSQAYVDDAGNLTTNNAGSAAKADMKALXKAASEGSDGASLTFNGTEYTIAKATPATTTPVAPLIPGGITYQATVSKDVVLSETKAAAATSSITFNSGVLSKTIGFTAGESSDAAKSYVDDKGGITNVADYTVSYSVNKDNGSVTVAGYASATDTNKDYAPAIGTAVNVNSAGKITTETTSAGSATTNPLAALDDAISSIDKFRSSLGAIQNRLDSAVTNLNNTTTNLSEAQSRIQDADYATEVSNMSKAQIIQQAGNSVLAKANQVPQQVLSLLQG
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (M0R0P9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKTERPRPNTFVIRCLQWTTVIERTFHVDSPDEREEWMRAIQMVANSLKQRAPGEDPMDYKCGSPSDSSTTEEMEVAVSKARAKVTMNDFDYLKLLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVAHTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGGELFFHLSRERVFTEERARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGISDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIRFPRTLSPEAKSLLAGLLKKDPKQRLGGGPSDAKEVMEHRFFLSINWQDVVQKKLLPPFKPQVTSEVDTRYFDDEFTAQSITITPPDRCECLGPPRWCACPRGGGMGSALNSLLKEGPRRPPLHVWEISPSLLSGPFAVGPLWTW
Protein: Coiled-coil alpha-helical rod protein 1 (Alpha-helical coiled-coil rod protein) (Q8K2I2)
Organism: Mus musculus (Mouse)
Function: May be a regulator of keratinocyte proliferation or differentiation.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Corneodesmosin
- Transcription factor 19-like protein
Sequence:
MLPPSGFAGLVPPSHFQARPLPTLPRMAPTWASDVPLVQSPASQDVLERRLDAQRSTVTTWGQDFCGDGQGLGRRGRSLELGFSSALSQQAELISRQLQELRRLEEEVRSLRETSLQQKMRLETQAVELDALAVAEKAGQAEAEGLRTALAGAEMVRKNLEEAKHKELEEIQSLHQEQLSSLTQAHQKALDSLASKAEGLEKSLNSLETKRAGEAKQLAMAQKEADMLRNQLSKTQEELEAQVTLVESLRKYVGEQVLPEFPSQEWELERKELLDTLKHLKEDRADLQATVELLQVRVQSLTHMLALQEEELTRKIQPLDPLEPEFPKKCRSLLRNWREKVFALMVQLKAQDLQHRDSTSQLRIQVAELQEQVTSQSQEQAILQRALQDKTAQVEVERMSTKSLQMELDQAQEARRRQEQQIASAEEQLKFVVGAMNSTQAKLQSTMTRMDQAVARIPSLSNRLSYAVRKVHTIKGLMARKVALAQLRVESSPPSEAAPPLDTDLSVELEQLREERNRLDAELQLSAHLIQQEVGRAREQGEVERRRLIEVAQQLEQELQRAQESLASVGQQLEAARRGQQESTEEAASLRQELTQQQEIYGQALQEKVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHKATQEKERNQELRRLQDEARKEEGQRLTRRVQELERDKNLMLQRLLAVLPSGVNKKCSPRSVESSSSESPAAASCKESVKGSLTVLLDNLQGLSEAISRDEDICVEDNQNTKKTKNPPSDPLLS
Protein: Alcohol acyl transferase 1 allele RGa (AAT1-RGa) (MpAAT1) (EC 2.3.1.-) (Q64FJ6)
Organism: Malus domestica (Apple) (Pyrus malus)
Function: Involved in the biosynthesis of volatile esters which confer ripe apple fruit flavor. Alcohol acyl transferase that can use a wide range of alcohols as substrate, including 2-methylbutanol, hexanol and ethanol, to produce esters such as butyl butanoate, butyl hexanoate, hexyl butanoate, 2-methylbutyl acetate (2MBA), butyl acetate, hexyl acetate and 2-methylbutyl butanoate (2MBB), and, to some extent, ethyl butanoate and ethyl hexanoate.
Interaction partners:
Sequence:
MMSFSVLQVKRLQPELITPAKSTPQETKFLSDIDDQESLRVQIPIIMCYKDNPSLNKNRNPVKAIREALSRALVYYYPLAGRLREGPNRKLVVDCNGEGILFVEASADVTLEQLGDKILPPCPLLEEFLYNFPGSDGIIDCPLLLIQVTCLTCGGFILALRLNHTMCDAAGLLLFLTAIAEMARGAHAPSILPVWERELLFARDPPRITCAHHEYEDVIGHSDGSYASSNQSNMVQRSFYFGAKEMRVLRKQIPPHLISTCSTFDLITACLWKCRTLALNINPKEAVRVSCIVNARGKHNNVRLPLGYYGNAFAFPAAISKAEPLCKNPLGYALELVKKAKATMNEEYLRSVADLLVLRGRPQYSSTGSYLIVSDNTRVGFGDVNFGWGQPVFAGPVKALDLISFYVQHKNNTEDGILVPMCLPSSAMERFQQELERITQEPKEDICNNLRSTSQ
Protein: Galactoside alpha-(1,2)-fucosyltransferase 1 (Alpha(1,2)FT 1) (Fucosyltransferase 1) (MFUT-1) (GDP-L-fucose:beta-D-galactoside 2-alpha-L-fucosyltransferase 1) (Type 1 galactoside alpha-(1,2)-fucosyltransferase FUT1) (EC 2.4.1.69) (Type 2 galactoside alpha-(1,2)-fucosyltransferase FUT1) (EC 2.4.1.344) (O09160)
Organism: Mus musculus (Mouse)
Function: Catalyzes the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to the terminal galactose residue of glycoconjugates through an alpha(1,2) linkage leading to H antigen synthesis that is an intermediate substrate in the synthesis of ABO blood group antigens. H antigen is essential for maturation of the glomerular layer of the main olfactory bulb, in cell migration and early cell-cell contacts during tumor associated angiogenesis. Preferentially fucosylates soluble lactose and to a lesser extent, fucosylates glycolipids gangliosides GA1 and GM1a.
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305|PubMed:11368156}. Note=Membrane-bound form in trans cisternae of Golgi. {ECO:0000305}.
Interaction partners:
- 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase 9
- Alpha-
- Beta-1,3-galactosyltransferase 5
- N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 3
- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1
- Beta-1,3-galactosyltransferase 1
- CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3-sialyltransferase
- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 4
- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 2
- Type 2 lactosamine alpha-2,3-sialyltransferase
Sequence:
MWTPSRRQLCLAFLLVCVLSAGSFFFHLNGGNFFRNGLTLSVLCSDYHLLKSPVAMVCLPHPLQTSNGSPSCPEQSSSLSGTWTITPGGRFGNQMGQYATLLALAQLNGRQAFIQPEMHAALAPVFRISLPVLDPEVDSLTPWQHLVLHDWMSEEYSHLEDPFLKLSGFPCSWTFFHHLREQIRREFTLHNHLREGAQYLLSGLRIGPAGIRPHTFVGVHVRRGDYLEVMPNRWKGVVGDRAYLQQAMDWFRARHKDPIFVVTSNGMKWCLENIDTSHGDVVFAGNGQEGTPGKDFALLTQCNHTIMTIGTFGFWAAYLAGGDTVYLANFTLPDSEFLKIFRPEAAFLPEWVGINADLSPLQAQFDPWKPDSLFRLV
Protein: Neurotensin/neuromedin N (Q6FH20)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasmic vesicle, secretory vesicle {ECO:0000256|ARBA:ARBA00004398}. Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MMAGMKIQLVCMLLLAFSSWSLCSDSEEEMKALEADFLTNMHTSKISKAHVPSWKMTLLNVCSLVNNLNSPAEETGEVHEEELVARRKLPTALDGFSLEAMLTIYQLHKICHSRAFQHWELIQEDILDTGNDKNGKEEVIKRKIPYILKRQLYENKPRRPYILKRDSYYY
Protein: Protein transport protein SEC9 (Q6FY22)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Candida glabrata strain CBS138 chromosome F complete sequence
- Candida glabrata strain CBS138 chromosome K complete sequence
- Candida glabrata strain CBS138 chromosome E complete sequence
- Candida glabrata strain CBS138 chromosome E complete sequence
- Protein transport protein SEC22
- Candida glabrata strain CBS138 chromosome G complete sequence
- Candida glabrata strain CBS138 chromosome E complete sequence
- Candida glabrata strain CBS138 chromosome C complete sequence
- Candida glabrata strain CBS138 chromosome L complete sequence
- Exocyst complex protein EXO70
Sequence:
MGIKKFFKIKPPKEDTVEQNRENLMDIGIATKSTTKKPQSKFAAYGQFAKDRATSKIYAPPGYEDFARPPEELEKKEGEEDDLNKSELDEKETKKDKKKKKKKHQQEDEPAAVQDPYARTEKSYRYNPDPYGAGAAGEKAFSSSGVYNEFNNYENGPSYGNEYGRRDRSEDLNAYNGTPGQPMKPVNRATPVLDRRDSAREDPAYGYNNQNRSNPYAGAGVGALAGGAAGGAVGAMGSVVSGSNPYGGASYGSGYGSSATTSAPVSKPISRTNTSASNPYGNASYGSTPGVNDRPAGSNPYAAISGDSYLNGTRSGNISRSGTNPYLRRNASNSVPPQAGYITPDSNNVALAEEENQQNQDELDLNDAPEDANEFVFEDKYMGRESKYAENSAALDELDLNATINDRGEDLNATGYGNMYEQQQQPQWQREEEEYGYGTQDDMNRGYKTFDEIQREEEERQKEEEDQAVDEIKEQIRFTKQSSVASTRNTLKMAQEAEMAGMNTLGMLGHQSEKLNNVERNLDLIKIQNTAADEKVAELKKLNRNILAVHVSNPFNSKRRRREREDMIKGRKMEDKMRAEHMSQELHQSTQRIEGALGGGNETSAVREKYQREKVLAAAKKYQFENDEEDDEMEVEIDRNLDKIQQISGRLKKLALATGEELDSQQRRIRDIEENTDEMDIKIHMNTTRLADIR
Protein: Heat shock protein HspQ (P0AB20)
Organism: Escherichia coli (strain K12)
Function: Involved in the degradation of certain denaturated proteins, including DnaA, during heat shock stress.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Ribosomal RNA large subunit methyltransferase I
- TDP-N-acetylfucosamine:lipid II N-acetylfucosaminyltransferase
- dTDP-fucosamine acetyltransferase
- Lipopolysaccharide export system protein LptC
Sequence:
MIASKFGIGQQVRHSLLGYLGVVVDIDPVYSLSEPSPDELAVNDELRAAPWYHVVMEDDNGLPVHTYLAEAQLSSELQDEHPEQPSMDELAQTIRKQLQAPRLRN
Protein: Peroxisomal (S)-2-hydroxyacid oxidase GLO3 (EC 1.1.3.15) (Glycolate oxidase 3) (AtGLO3) (GOX 3) (Short chain alpha-hydroxy acid oxidase GLO3) (lHAOX2) (Q24JJ8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Oxidase that catalyzes the oxidation of a broad range of 2-hydroxyacids to the corresponding 2-oxoacids, with a reduction of O2 to H2O2. Displays the highest activity with leucic acid (2-hydroxy-4-methylpentanoate) and has intermediate activity with 2-hydroxyhexanoate and 2-hydroxyoctanote. Shows lower activity with 2-hydroxydodecanoate, valic acid, and isoleucic acid and extremely low activity with glycolate and L-lactate. Cannot use 2-hydroxyhexadecanoate or D-lactate as substrates. May be involved in the conversion or degradation of 2-hydroxyacids produced during the metabolism of fatty acids or amino acids.
Subcellular location: Peroxisome {ECO:0000305|PubMed:19329564}.
Interaction partners:
- Serine--glyoxylate aminotransferase
- Glutamate--glyoxylate aminotransferase 2
- Glyoxylate/hydroxypyruvate reductase A HPR2
- Malate synthase
- Glycerate dehydrogenase HPR, peroxisomal
- Isocitrate lyase
- Glutamate--glyoxylate aminotransferase 1
- Phosphoglycolate phosphatase 2
- Phosphoglycolate phosphatase 1A, chloroplastic
- Catalase-2
Sequence:
MDQIVNVDEFQELAKQALPKMYYDFYNGGAEDQHTLNENVQAFRRIMFRPRVLVDVSKIDMSTKILGYPISAPIMIAPTGNHKLAHPEGETATAKAAAACNTIMIVSYMSSCTFEEIASSCNAVRFLQIYVYKRRDITAQVVKRAEKAGFKAIVLTVDVPRLGRREADIKNKMISPQLKNFEGLFSTEVRPSKGSGVQAFASRAFDASFSWKDIEWLRSITELPILVKGILTREDALKAVEAGVDGIIVSNHGGRQLDYSPATITVLEEVVQVVRGRIPVLLDGGVRRGTDVFKALALGAQAVLIGRPIIYGLAAKGEDGVKKVIDMLKNEFEITMALSGCPTIDDITRNHVRTENERLHSML