wanglab/gogpt-training-data huggingface dataset:
Protein: Defense protein l(2)34Fc (Q9V3Y3)
Organism: Drosophila melanogaster (Fruit fly)
Function: May have antimicrobial activity. A late response immune regulated gene that is negatively regulated by spz during the immune response.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Reelin domain-containing protein
- Large ribosomal subunit protein uL23m
- Large ribosomal subunit protein mL46
- Large ribosomal subunit protein uL3m
- Large ribosomal subunit protein uL16m
- Large ribosomal subunit protein bL27m
- Small ribosomal subunit protein uS15m
- Large ribosomal subunit protein bL19m
- Large ribosomal subunit protein uL22m
- Large ribosomal subunit protein uL13m
Sequence:
MFRLLVLAACLAISVHAYSDGAPKAACRDLTPQHGAKLQVTKPPYSISGPSHVRSDQKLTLTLGGDEFLGFMIQARDGQNRVVGQFQVVDSVHSQTLDCSGKDDTITHLSAQKGKPLTGITFDWIPPAGYKGNVKFMATVVQTGFVYWVGRVTKDIDVE
Protein: UPF0719 inner membrane protein YjfL (P0AF80)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Putative acid--amine ligase YjfC
- Uncharacterized protein YjfM
- Uncharacterized protein YjfJ
- Uncharacterized protein YjfK
- Putative acid--amine ligase YgiC
Sequence:
MHILDSLLAFSAYFFIGVAMVIIFLFIYSKITPHNEWQLIKNNNTAASLAFSGTLLGYVIPLSSAAINAVSIPDYFAWGGIALVIQLLVFAGVRLYMPALSEKIINHNTAAGMFMGTAALAGGIFNAACMTW
Protein: Sugar kinase (Q97EQ3)
Organism: Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / IAM 19013 / LMG 5710 / NBRC 13948 / NRRL B-527 / VKM B-1787 / 2291 / W)
Interaction partners:
- Phosphoheptose isomerase
- D-glycero-alpha-D-manno-heptose-1,7-bisphosphate 7-phosphatase
- Nucleoside-diphosphate-sugar pyrophosphorylase
- Glycosyltransferase
- Glycosyltransferase
- Glycosyltransferase
- Glycosyltransferase
- AMSJ/WSAK related protein, possibly involved in exopolysaccharide biosynthesis
- mannose-1-phosphate guanylyltransferase
Sequence:
MIIRAKAPLRISFGGGGTDVEPYCNEYGGVVLNTTIDKYAYCSIVPNNTDSIVVNSLDFDMTVKYNCNENLVYDGKLDLVKAALKRMNINKGCEVYLQCDAPAGSGLGTSSTVVVALLGAMAKWKGVVLDQYALASIAYEVERKDLKIDGGYQDQYAAAFGGFNFMEVDGSDVVVNPLKINKGITNELQYNLLLCYTGNVHVSANIIKDQVNNYVEKKEEVVNAMHEIKALAYAMKKELLRNNLNNFGSLLHYGWEMKKKMSSRISNPQIDELYEAALKKGALGGKLLGAGGGGYLLVYCPYNKKHVVAESLEKMGGQLTDWNFDLGGMQSWVVDDSRWNYNEIAVATTEGKYKFGINTMEDIG
Protein: Carbamoyl phosphate synthase small chain (EC 6.3.5.5) (Carbamoyl phosphate synthetase glutamine chain) (Q726J4)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- Aspartate carbamoyltransferase catalytic subunit
- Carbamoyl phosphate synthase large chain
- Dihydroorotase
- Phosphoribosylformylglycinamidine synthase I
- Amidophosphoribosyltransferase
- Dihydroorotate dehydrogenase
- Glutamine synthetase, type I
- Argininosuccinate synthase
- Ornithine carbamoyltransferase
- Orotate phosphoribosyltransferase
Sequence:
MRALLALEDGFVLEGRSFTGPGETGGEAIFNTGMTGYQEVLTDPSYAGQMVCMTYPLVGNYGVTREDMESGKVHVEAFIVKECCKVPSNWRSEISLPDYLKRHGVMGIEGIDTRALTRHLRIHGAMRGVISTQETDPARLVERARALPSMEGQNLVTRVAPAAPYRWDGERPQAVTLEPGGCAWVGKGPRLVVYDFGIKWNILRLLAQQGFDMLVVPPSFKAADVAAVGAQAVFLSNGPGDPATLKDEIAEIAKLAQTYPTAGICLGHQLLGHALGGRTMKLKFGHHGCNHPVKDLTTGRIEISSQNHGFCVDIDSLTDVEITHVNLNDGTLEGFAHKTKPVIAVQHHPEASPGPNDSRYFFARFRNMVREAAGC
Protein: Zinc finger and BTB domain-containing protein 11 (O95625)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:29893856}.
Interaction partners:
Sequence:
MSSEESYRAILRYLTNEREPYAPGTEGNVKRKIRKAAACYVVRGGTLYYQRRQRHRKTFAELEVVLQPERRRDLIEAAHLGPGGTHHTRHQTWHYLSKTYWWRGILKQVKDYIKQCSKCQEKLDRSRPISDVSEMLEELGLDLESGEESNESEDDLSNFTSSPTTASKPAKKKPVSKHELVFVDTKGVVKRSSPKHCQAVLKQLNEQRLSNQFCDVTLLIEGEEYKAHKSVLSANSEYFRDLFIEKGAVSSHEAVVDLSGFCKASFLPLLEFAYTSVLSFDFCSMADVAILARHLFMSEVLEICESVHKLMEEKQLTVYKKGEVQTVASTQDLRVQNGGTAPPVASSEGTTTSLPTELGDCEIVLLVNGELPEAEQNGEVGRQPEPQVSSEAESALSSVGCIADSHPEMESVDLITKNNQTELETSNNRENNTVSNIHPKLSKENVISSSPEDSGMGNDISAEDICAEDIPKHRQKVDQPLKDQENLVASTAKTDFGPDDDTYRSRLRQRSVNEGAYIRLHKGMEKKLQKRKAVPKSAVQQVAQKLVQRGKKMKQPKRDAKENTEEASHKCGECGMVFQRRYALIMHKLKHERARDYKCPLCKKQFQYSASLRAHLIRHTRKDAPSSSSSNSTSNEASGTSSEKGRTKREFICSICGRTLPKLYSLRIHMLKHTGVKPHACQVCGKTFIYKHGLKLHQSLHQSQKQFQCELCVKSFVTKRSLQEHMSIHTGESKYLCSVCGKSFHRGSGLSKHFKKHQPKPEVRGYHCTQCEKSFFEARDLRQHMNKHLGVKPFQCQFCDKCYSWKKDWYSHVKSHSVTEPYRCNICGKEFYEKALFRRHVKKATHGKKGRAKQNLERVCEKCGRKFTQLREYRRHMNNHEGVKPFECLTCGVAWADARSLKRHVRTHTGERPYVCPVCSEAYIDARTLRKHMTKFHRDYVPCKIMLEKDTLQFHNQGTQVAHAVSILTAGMQEQESSGPQELETVVVTGETMEALEAVAATEEYPSVSTLSDQSIMQVVNYVLAQQQGQKLSEVAEAIQTVKVEVAHISGGE
Protein: TPM3 protein (cDNA FLJ32435 fis, clone SKMUS2001287, highly similar to Tropomyosin alpha-3 chain) (Q5VU62)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISEELDHALNDMTSI
Protein: Isochorismatase domain-containing protein 1 (Down-regulated in nephrectomized rat kidney protein 1) (DR-NR1) (Q6I7R3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAAAEPSVAALAGGGVGAGAPSGGVPVLFCFSVFARPASVPHGAGYDVLIQKFLSLYGDQVDMHRKFVVQLFAEEWGQYVDLPKGFAVSERCKLRLVPLQIQLTTLGNLTPPSTVFFCCDMQERFRPAIKYFGDIISVGQRLLQGARILGIPVIITEQYPKGLGSTVQEIDLTGVKLVLPKTKFSMVLPEVEAALAEIPGVRSVVLFGVETHVCIQQTALELVGRGIEVHIVADATSSRSMMDRMFALERLARTGIIVTTSEAVPLQLVADKDHPKFKEIQNLIKASAPESGLLSKV
Protein: CD166 antigen (Activated leukocyte cell adhesion molecule) (CD antigen CD166) (Q13740)
Organism: Homo sapiens (Human)
Function: Cell adhesion molecule that mediates both heterotypic cell-cell contacts via its interaction with CD6, as well as homotypic cell-cell contacts. Promotes T-cell activation and proliferation via its interactions with CD6. Contributes to the formation and maturation of the immunological synapse via its interactions with CD6. Mediates homotypic interactions with cells that express ALCAM. Acts as a ligand for the LILRB4 receptor, enhancing LILRB4-mediated inhibition of T cell proliferation. Required for normal hematopoietic stem cell engraftment in the bone marrow. Mediates attachment of dendritic cells onto endothelial cells via homotypic interaction. Inhibits endothelial cell migration and promotes endothelial tube formation via homotypic interactions. Required for normal organization of the lymph vessel network. Required for normal hematopoietic stem cell engraftment in the bone marrow. Plays a role in hematopoiesis; required for normal numbers of hematopoietic stem cells in bone marrow. Promotes in vitro osteoblast proliferation and differentiation (By similarity). Promotes neurite extension, axon growth and axon guidance; axons grow preferentially on surfaces that contain ALCAM. Mediates outgrowth and pathfinding for retinal ganglion cell axons (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:15048703, ECO:0000269|PubMed:15294938, ECO:0000269|PubMed:16352806, ECO:0000269|PubMed:23169771, ECO:0000269|PubMed:24740813, ECO:0000269|PubMed:24945728, ECO:0000269|PubMed:7760007}; Single-pass type I membrane protein {ECO:0000305}. Cell projection, axon {ECO:0000250|UniProtKB:Q61490}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q61490}. Note=Detected at the immunological synapse, i.e, at the contact zone between antigen-presenting dendritic cells and T-cells (PubMed:15294938, PubMed:16352806). Colocalizes with CD6 and the TCR/CD3 complex at the immunological synapse (PubMed:15294938). {ECO:0000269|PubMed:15294938, ECO:0000269|PubMed:16352806}.; SUBCELLULAR LOCATION: [Isoform 3]: Secreted {ECO:0000269|PubMed:15496415}.
Interaction partners:
- T-cell differentiation antigen CD6
- Neural cell adhesion molecule L1
- Galectin-8
- Thy-1 membrane glycoprotein
- Endoglin
- 5'-nucleotidase
- CD44 antigen
- Protein S100-B
- Integrin beta-1
- Leukocyte immunoglobulin-like receptor subfamily B member 4
Sequence:
MESKGASSCRLLFCLLISATVFRPGLGWYTVNSAYGDTIIIPCRLDVPQNLMFGKWKYEKPDGSPVFIAFRSSTKKSVQYDDVPEYKDRLNLSENYTLSISNARISDEKRFVCMLVTEDNVFEAPTIVKVFKQPSKPEIVSKALFLETEQLKKLGDCISEDSYPDGNITWYRNGKVLHPLEGAVVIIFKKEMDPVTQLYTMTSTLEYKTTKADIQMPFTCSVTYYGPSGQKTIHSEQAVFDIYYPTEQVTIQVLPPKNAIKEGDNITLKCLGNGNPPPEEFLFYLPGQPEGIRSSNTYTLTDVRRNATGDYKCSLIDKKSMIASTAITVHYLDLSLNPSGEVTRQIGDALPVSCTISASRNATVVWMKDNIRLRSSPSFSSLHYQDAGNYVCETALQEVEGLKKRESLTLIVEGKPQIKMTKKTDPSGLSKTIICHVEGFPKPAIQWTITGSGSVINQTEESPYINGRYYSKIIISPEENVTLTCTAENQLERTVNSLNVSAISIPEHDEADEISDENREKVNDQAKLIVGIVVGLLLAALVAGVVYWLYMKKSKTASKHVNKDLGNMEENKKLEENNHKTEA
Protein: Zinc-finger domain of monoamine-oxidase A repressor R1 protein (F4HTR3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- AT5g38690/MBB18_24
- Homeobox-DDT domain protein RLT1
- Homeobox-DDT domain protein RLT2
- DDT domain-containing protein
- DDT domain-containing protein DDR4
- Uncharacterized protein At5g25580
- PHD-finger and DNA binding domain-containing protein
- WD-40 repeat-containing protein MSI3
- PHD finger family protein
- DDT domain-containing protein PTM
Sequence:
MAIEGEKEKPSKRTTNPGVRVVGGRIYDSSNGKTCHQCRQKTMDFVASCKAMKKDKQCTINFCHKCLINRYGENAEEVAKLDDWICPQCRGICNCSFCRKKRGLNPTGILAHKAKASGLASVSMLLEVEGHDNFAYQKKPKLNDDSMEGSSGNSDSVSGTDVEVADVAKDKKKVVGKSKKANATHKLKEEIQFEAQLPQGISLISVSGVVIPTEEAGNVFQLFEFCSAFGKALELKEGQAETVVRELFSCGRNTRRQQYCSIIQLMIQLLDLISKDREMSLSLSVSDNWFTALGEILLQSEVLSDEFPPETFETGVAEYEKMDASRRLKLLNFVCDESLSTWAMRNCIKSQSTECKANNNEAKRKAAAAKEKEKQLKQKLQGDLAKAIMKKNGAPLSIEEHNEILSQIRAEAKEAHDGMMEAKGITSGMTRICDARRTEPIMVEDNGLVLWKLNCYDEEPKFLLQDLGTFDGLCSHEKWLAFKPEQKPDIENYISYKRRKVMQTLKNTNVVA
Protein: Cyclic nucleotide-gated channel beta-3 (CNG channel beta-3) (Cone photoreceptor cGMP-gated channel subunit beta) (Cyclic nucleotide-gated cation channel beta-3) (Cyclic nucleotide-gated cation channel modulatory subunit) (Cyclic nucleotide-gated channel subunit CNG6) (Q9JJZ9)
Organism: Mus musculus (Mouse)
Function: Visual signal transduction is mediated by a G-protein coupled cascade using cGMP as second messenger. This protein can be activated by cGMP which leads to an opening of the cation channel and thereby causing a depolarization of rod photoreceptors. Essential for the generation of light-evoked electrical responses in the red-, green- and blue sensitive cones (By similarity). Induced a flickering channel gating, weakened the outward rectification in the presence of extracellular calcium, increased sensitivity for L-cis diltiazem and enhanced the cAMP efficacy of the channel when coexpressed with CNGA3.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9NQW8}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cyclic nucleotide-gated channel alpha-3
- Cyclic nucleotide-gated channel alpha-1
- Guanine nucleotide-binding protein G
- Cyclic nucleotide-gated channel alpha-4
- Cone cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha'
- Cyclic nucleotide-gated channel alpha-2
- Retinal cone rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma
- Recoverin
Sequence:
MLKSLTVKFNKVNPMEGRMEKKLCPNLSSLSQPTIAQGDNQSEKEPLRSRTPITFEKSHSKEDNSTGENSLRDFTPNPDPECRAELTRTMAEMEKTRTGKERPVSFKTKVLETSIINEYTDAHLHNLVERMRERTALYKKTLTEEENFPEVEASSQTAMSTNISPKQENNSKLKEHQDTFSFKPQRVPVKEHLRRMILPRSIDSYTDRVYLLWLLLVTIAYNWNCWLLPVRLVFPCQTPDNKNYWIITDIVCDIIYLCDILLIQPRLQFVRGGEIIVDSNELKRNYRSSTKFRMDVASLLPFEVLYIFFGVNPIFRANRILKYTSFFEFNHHLESIMDKAYVYRVIRTTGYLLFLLHINACVYYWASDYEGIGSTKWVYNGEGNKYLRCFYWAVRTLITIGGLPEPQTSFEIVFQFLNFFSGVFVFSSLIGQMRDVIGAATANQNYFQACMDHIIAYMNKYSIPQSVQYRVRTWLEYTWNSQRILDESNLLENLPTAMQLSIALDINFSIIDKVELFKGCDTQMIYDLLLRLKSTIYLPGDFVCKKGEIGKEMYIIKHGEVQVLGGPDGAQVLVTLKAGSVFGEISLLAKGGGNRRTADVVAHGFANLLTLDKKTLQEILLHYPTSKKLLMKKAKILLSQKGKTTQAIPARPGPAFLFPPKEETPRMLKVLLGNTGKVDLGRLLKGKRKTTTQK
Protein: Stanniocalcin-1 (STC-1) (O55183)
Organism: Mus musculus (Mouse)
Function: Stimulates renal phosphate reabsorption, and could therefore prevent hypercalcemia.
Subcellular location: Secreted.
Interaction partners:
Sequence:
MLQNSAVILALVISAAAAHEAEQNDSVSPRKSRVAAQNSAEVVRCLNSALQVGCGAFACLENSTCDTDGMYDICKSFLYSAAKFDTQGKAFVKESLKCIANGITSKVFLAIRRCSTFQRMIAEVQEDCYSKLNVCSIAKRNPEAITEVIQLPNHFSNRYYNRLVRSLLECDEDTVSTIRDSLMEKIGPNMASLFHILQTDHCAQTHPRADFNRRRTNEPQKLKVLLRNLRGEGDSPSHIKRTSQESA
Protein: Tumor necrosis factor ligand superfamily member (A0A8I5ZY27)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004401}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}. Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MPSTGNLKGPSFSQHFTMTVICIVLLQVLLQALTVAVTYMYFNNEVKQLQDNYSKIGLACFSKEDGDFWDSTDEGILNRPCLQVKRQLYQLIEEDASSDTTVSFDKQKQLSTPPLPRGRRPQRVAAHITGITRRSNLALIPISKDGKTLGQKIETWESSRRGHSFLNHVHLRNGELVIQEEGLYYIYSQTYYRFKEAKEASKTVSKDGGRIKQMVQYIYKYTSYPDPILLMKSARNSCWSREAEYGLYSIYQGGLFELKENDRIFVSVTNEHLMDLDQEASFFGAFLIN
Protein: Refilin-A (Regulator of filamin protein A) (RefilinA) (Q7TS73)
Organism: Mus musculus (Mouse)
Function: Involved in the regulation of the perinuclear actin network and nuclear shape through interaction with filamins. Plays an essential role in the formation of cartilaginous skeletal elements.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:21709252, ECO:0000269|PubMed:24436304}. Note=Colocalizes with FLNA along actin bundle-like structures. {ECO:0000269|PubMed:24436304}.
Interaction partners:
Sequence:
MVGHLHLQAMGDTREQSRDGLLDSPDSGLPPSPSPSPPFYALSPGTLDTRTTTEAPAAPSLFQTPPALEMRSRLLPVFFGESIEVDPEPAHEIRCNSEITYASERYFRDKIFYAPVPTVTAYSETIVAAPNCTWRSYRSQLTLEPRPRALRFGSTAIIFPKLARSSFRTTLHCSLGQPRHWYSSSLQLRRCGDPTPGPSCPDVL
Protein: Nucleoid-associated protein YejK (P33920)
Organism: Escherichia coli (strain K12)
Subcellular location: Cytoplasm, nucleoid.
Interaction partners:
- Inner membrane protein YejM
- UPF0352 protein YejL
- Der GTPase-activating protein YihI
- UPF0208 membrane protein YfbV
- Negative modulator of initiation of replication
- Putative DNA repair helicase RadD
Sequence:
MSLDINQIALHQLIKRDEQNLELVLRDSLLEPTETVVEMVAELHRVYSAKNKAYGLFSEESELAQTLRLQRQGEEDFLAFSRAATGRLRDELAKYPFADGGFVLFCHYRYLAVEYLLVAVLSNLSSMRVNENLDINPTHYLDINHADIVARIDLTEWETNPESTRYLTFLKGRVGRKVADFFMDFLGASEGLNAKAQNRGLLQAVDDFTAEAQLDKAERQNVRQQVYSYCNEQLQAGEEIELKSLSKELAGVSEVSFTEFAAEKGYELEESFPADRSTLRQLTKFAGSGGGLTINFDAMLLGERIFWDPATDTLTIKGTPPNLRDQLQRRTSGGN
Protein: Lysosomal phospholipase A and acyltransferase (EC 2.3.1.-) (EC 3.1.1.32) (EC 3.1.1.4) (1-O-acylceramide synthase) (ACS) (LCAT-like lysophospholipase) (LLPL) (EC 3.1.1.5) (Lysophospholipase 3) (Lysosomal phospholipase A2) (LPLA2) (Phospholipase A2 group XV) (Q6XPZ3)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: Has dual calcium-independent phospholipase and O-acyltransferase activities with a potential role in glycerophospholipid homeostasis and remodeling of acyl groups of lipophilic alcohols present in acidic cellular compartments. Catalyzes hydrolysis of the ester bond of the fatty acyl group attached at sn-1 or sn-2 position of phospholipids (phospholipase A1 or A2 activity) and transfer it to the hydroxyl group at the first carbon of lipophilic alcohols (O-acyltransferase activity). Among preferred fatty acyl donors are phosphatidylcholines, phosphatidylethanolamines, phosphatidylglycerols and phosphatidylserines. Favors sn-2 over sn-1 deacylation of unsaturated fatty acyl groups of phosphatidylcholines and phosphatidylethanolamines (By similarity). Among preferred fatty acyl acceptors are natural lipophilic alcohols including short-chain ceramide N-acetyl-sphingosine (C2 ceramide), alkylacylglycerols, monoacylglycerols, and acylethanolamides such as anandamide and oleoylethanolamide (By similarity). Selectively hydrolyzes the sn-1 fatty acyl group of truncated oxidized phospholipids and may play a role in detoxification of reactive oxidized phospholipids during oxidative stress. Required for normal phospholipid degradation in alveolar macrophages with potential implications in pulmonary surfactant clearance (By similarity). At neutral pH, hydrolyzes the sn-1 fatty acyl group of the lysophosphatidylcholines (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q8NCC3}. Lysosome {ECO:0000269|PubMed:11790796}. Membrane {ECO:0000250|UniProtKB:Q8NCC3}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8NCC3}.
Interaction partners:
- Patatin like phospholipase domain containing 6.
- Patatin like phospholipase domain containing 7.
- Lysophosphatidylcholine acyltransferase 4.
- Lysophosphatidylcholine acyltransferase 1.
- Phospholipase B1.
- Phospholipase A2 group VI.
- Phospholipase A2 group III.
- Lysophosphatidylcholine acyltransferase 3
- Phospholipase A
- Glycerophosphocholine phosphodiesterase 1.
Sequence:
MGLRRGPCPAALLPGGFLFLLLLADPALLAGRRPPVVLVPGDLGNQLEAKLDKPTVVHYLCSKRTESYFTLWLNLELLLPVIIDCWIDNIRLVYNRTSRATQFPDGVDVRVPGFGKTFSLEFLDPSKSSVGSYFHTMVESLVDWGYIRGEDVRGAPYDWRRAPNENGPYFLALREMIEEMYQLYGGPVVLVAHSMGNMYTLYFLQRQPQAWKNKYIQAFVALGAPWGGVAKTLRVLASGDNNRIPVIRPLKIREQQRSAVSTSWLLPYNYTWSPEKIFVHTPTANYTLRDYHQFFQDIGFKDGWLMRQDTEGLVEAMVPPGVPLHCLYGTGVPTPDSFYYESFPDRDPKICFGDGDGTVNLQSALQCQAWRGHQEHQVSLQALPGSEHIEMLANATTLAYLKRVLLGP
Protein: Probable UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase SEC (EC 2.4.1.255) (Protein SECRET AGENT) (Q9M8Y0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: O-linked N-acetylglucosamine transferase (OGT) that mediates O-glycosylation of capsid protein (CP) of virus in case of infection by Plum pox virus. OGTs catalyze the addition of nucleotide-activated sugars directly onto the polypeptide through O-glycosidic linkage with the hydroxyl of serine or threonine. Probably acts by adding O-linked sugars to yet unknown proteins. Its OGT activity has been proved in vitro but not in vivo. Required with SPY for gamete and seed development. Mediates O-glycosylation of the DELLA protein RGA, a repressor of the gibberellin (GA) signaling pathway. O-glycosylation by SEC inhibits RGA binding to four of its interactors PIF3, PIF4, JAZ1, and BZR1 that are key regulators in light, jasmonate, and brassinosteroid signaling pathways, respectively. Activates ATX1 through O-GlcNAc modification to augment ATX1-mediated H3K4me3 histone epigenetic modification at FLC locus, thus preventing premature flowering.
Interaction partners:
- Probable UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase SPINDLY
- Alpha/beta-Hydrolases superfamily protein
- Ubiquitin carboxyl-terminal hydrolase
- Ubiquitin carboxyl-terminal hydrolase 2
- AT4g33900 family protein)
- Extracellular ligand-gated ion channel protein
- At1g13195
- AT5g37540/mpa22_p_70
- 1,4-dihydroxy-2-naphthoyl-CoA thioesterase 1
- Receptor like protein kinase S.2
Sequence:
MISSKNGAAMISRPVFLSDRVDEVFSRKLDLSVSSSSSSSLLQQFNKTHEGDDDARLALAHQLYKGGDFKQALEHSNMVYQRNPLRTDNLLLIGAIYYQLQEYDMCIARNEEALRIQPQFAECYGNMANAWKEKGDTDRAIRYYLIAIELRPNFADAWSNLASAYMRKGRLSEATQCCQQALSLNPLLVDAHSNLGNLMKAQGLIHEAYSCYLEAVRIQPTFAIAWSNLAGLFMESGDLNRALQYYKEAVKLKPAFPDAYLNLGNVYKALGRPTEAIMCYQHALQMRPNSAMAFGNIASIYYEQGQLDLAIRHYKQALSRDPRFLEAYNNLGNALKDIGRVDEAVRCYNQCLALQPNHPQAMANLGNIYMEWNMMGPASSLFKATLAVTTGLSAPFNNLAIIYKQQGNYSDAISCYNEVLRIDPLAADALVNRGNTYKEIGRVTEAIQDYMHAINFRPTMAEAHANLASAYKDSGHVEAAITSYKQALLLRPDFPEATCNLLHTLQCVCCWEDRSKMFAEVESIIRRQINMSVLPSVQPFHAIAYPIDPILALEISRKYAAHCSIIASRFGLPPFTHPAGLPVKREGGFKRLRIGYVSSDFGNHPLSHLMGSVFGMHNRENVEVFCYALSANDNTEWRQRIQSEAEHFLDVSAMSSDAIAKIINQDKIQILINLNGYTKGARNEIFAMQPAPIQVSYMGFPGTTGATYIDYLVTDEFVSPLQYAHIYSEKLVHLPHCYFVNDYKQKNQDVLDPNSKPKRSDYGLPEDKFIFACFNQLYKMDPEIVNTWCNILKRVPNSALWLLRFPAAGEMRFRTYAAAQGVQPDQIIFTDVAMKSEHIRRSVLADVILDTPLCNGHTTGTDVLWAGVPMITLPLEKMATRVAGSLCLATGLGHGMIVNSLEEYEEKAVSLALNKPKLQALTKELRASRLTCPLFDTMRWVKNLERSYFKMWNLHCSGQQPQHFKVLENDLEFPHDR
Protein: Oxysterol-binding protein 1 (P16258)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Lipid transporter involved in lipid countertransport between the Golgi complex and membranes of the endoplasmic reticulum: specifically exchanges sterol with phosphatidylinositol 4-phosphate (PI4P), delivering sterol to the Golgi in exchange for PI4P, which is degraded by the SAC1/SACM1L phosphatase in the endoplasmic reticulum (By similarity). Binds cholesterol and a range of oxysterols including 25-hydroxycholesterol. Cholesterol binding promotes the formation of a complex with PP2A and a tyrosine phosphatase which dephosphorylates ERK1/2, whereas 25-hydroxycholesterol causes its disassembly (By similarity). Regulates cholesterol efflux by decreasing ABCA1 stability (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P22059}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P22059}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P22059}; Peripheral membrane protein {ECO:0000250|UniProtKB:P22059}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P22059}; Peripheral membrane protein {ECO:0000250|UniProtKB:P22059}. Note=Predominantly cytosolic. {ECO:0000250|UniProtKB:P22059}.
Interaction partners:
- VAMP associated protein A
- Vesicle-associated membrane protein-associated protein A
- VAMP associated protein B and C
- Pleckstrin 2
- Pleckstrin
- NPC intracellular cholesterol transporter 1
- Phosphatidylinositol 4-kinase beta
- Extended synaptotagmin-1
- StAR-related lipid transfer protein 3
- Phosphatidylinositol 4-kinase alpha
Sequence:
MAATELRGVVGPGPAAIAAPGGGGAGPPVVGGGGGGRGDAGPGSGAASGTVAAAAAGGQGPGAGGVAAAAGPAPTPPAGGSGSSGTGGSGSAREGWLFKWTNYIKGYQRRWFVLSNGLLSYYRSKAEMRHTCRGTINLATANITVEDSCNFIISNGGAQTYHLKASSEVERQRWVTALELAKAKAVKMLAESDESGDEESVSQTDKTELQNTLRTLSSKVEDLSTCNDLIAKHGTALQRSLSELESLKLPAESNEKIKQVNERATLFRITSNAMINACRDFLVLAQTHSKKWQKSLQYERDQRIRLEETLEQLAKQHNHLERAFRGATVLPAHTSGSAGSGKDQCCSGKGDMSDEDDENEFFDAPEIITMPENLGHKRTGSNISGASSDISLDEQYKHQLEETKKEKRTRIPYKPNYSLNLWSIMKNCIGKELSKIPMPVNFNEPLSMLQRLTEDLEYHELLDRAAKCENSLEQLCYVAAFTVSSYSTTVFRTSKPFNPLLGETFELDRLEENGYRSLCEQVSHHPPAAAHHAESKNGWTLRQEIKITSKFRGKYLSIMPLGTIHCIFHATGHHYTWKKVTTTVHNIIVGKLWIDQSGEIDIVNHKTGDKCNLKFVPYSYFSRDVARKVTGEVTDPSGKVHFALLGTWDEKMDCFKVQPVSGENGGDARQRGHEAEESRVMLWKRNPLPKNAENMYYFSELALTLNAWEGGTAPTDSRLRPDQRLMENGRWDEANAEKQRLEEKQRLSRKKREAEAMKATEDGTPYDPYKALWFERKKDPVTKELTHIYRGEYWECKEKQDWNSCPDIF
Protein: RCG28722, isoform CRA_a (Similar to CG10806-PB, isoform B) (B2RYK8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MEDEDQTVECQYSKPPLGTTHAASRHHELQEERVTNLKSPDGNEPTEDSNLLTGGEKKPQDSLAEPRSLQSPRRFLACPPHGRLAGVITNGTMVVLLWAVVWSITGPECLPGGNLFGIIILFYCSITGGKLFGLIKFPTLPPLPPLLGMLLAGFLLRNVPVISDNVRIQHKWSSSLRSIALSVILVRAGLGLDSKALKKLKGVCVRLAMGPCIVEACASALLSHFLMGLPWQWGFILGFVVGAVSPAVVVPSMLLLQEGGYGVEKGIPTLLMAAGSFDDILAITGFNTCLGVAFSTGSTVFNIFRGILEVVIGVATGSLLGFFIQYFPSRDQDNLVWKRAFLVLGFAVLAVFSSVIFSFPGSGGLCTLVMAFLAGMRWTDKKSEVEKIIALTWDVFQPLLFGLIGAEVSIASLRAETVGLCVATLGIAVLIRILTTFLMVCFAGFNIKEKIFISFAWLPKATVQAAIGSVALDTARSHGEKQLEDYGMDVLTVAFLAILITAPIGSLLIGLLGPRVLQKSEHRNEEEVQGETSAHVQRKSGDSVTEA
Protein: Nuclear pore complex protein (A1YK65)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus, nuclear pore complex {ECO:0000256|RuleBase:RU365072}. Nucleus membrane {ECO:0000256|RuleBase:RU365072}.
Interaction partners:
Sequence:
MADSPFPRSSRSGLLRTTLNSSMAPQNLSHSLLILEQSNAEQNDRSLMEDTGDDLDRGKSRMDVLFPQFFDVLQAQGNGQEAFEVIQSLTQVCRGVVEQLELEIDHGMGGEQGARXRESMLTWLRQEINTWRLLHALFYDRILLQTDRQADDDMQDGPTLGGSEKEVIQQLYALNATLREYQVVVDWLEACYDRGEQQNPLHAHDRMMAWENTLFQLENLQGAAFGKGHKIVTRLDPDAPVREKRPLHALDEEDNLRLSRAIFELIRAGRVDDGLKLCKHFGQTWRAAILEGWRLHEDPNFEQNVSVLHEKLPIEGNPRRDIWKRCAWMLADSKNYDEYSRATAGVFSGHLGSLKTLLHSNWHDLLWAHLKVQIDIRVESEIRGCCLKNYQPMPDDYWNGRMTMEQIFEELNVAKDASVRDFAQSQLGIIQRHLILDTCGELIQHMVRWVEKDTSQQSPHQLRFMAHIVLFLRQIGRVEQERQAEKIVAAYVEALIARGEPQLIAYYTASLSNPLQVQLYSRFLEQVEQKRPRELAVDAALQAGLDVEQITRVTVQNIRLAHQPLGEFGEPQSGEISAIDQRKISALEWLIHLPEQRGELLWQANAMIRTYLASSKVECMRQTFRMVPADIVQQLVSLYGSVDNIPPREECCLKEYLCYKAYLSGVDSFVEWNRLQQNRPKKPQTSHAASSQDNFTERMASERKEQAHRSEVVRWEHKVKEQAKQTIELLYNVLMFPDKGWLVDPFIAKLPENAVQLNWDHRLLQMEKLRSICIPEIALFLNEVMFKSGDFAGCVRLADEISSENRQLYKVYTKHKLAELLAKIADASLELLNSKLDPWGYPITT