wanglab/gogpt-training-data huggingface dataset:
Protein: P2Y purinoceptor 2 (P2Y2) (ATP receptor) (P2U purinoceptor 1) (P2U1) (Purinergic receptor) (P41232)
Organism: Rattus norvegicus (Rat)
Function: Receptor for ATP and UTP coupled to G-proteins that activate a phosphatidylinositol-calcium second messenger system. The affinity range is UTP = ATP > ATP-gamma-S >> 2-methylthio-ATP = ADP.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Guanine nucleotide-binding protein G
- P2X purinoceptor 1
- P2X purinoceptor 2
- P2X purinoceptor 7
- P2X purinoceptor 6
- P2X purinoceptor 3
- P2X purinoceptor 4
- Ectonucleoside triphosphate diphosphohydrolase 1
- Pulmonary surfactant-associated protein B
- Surfactant protein C
Sequence:
MAAGLDSWNSTINGTWEGDELGYKCRFNEDFKYVLLPVSYGVVCVLGLCLNVVALYIFLCRLKTWNASTTYMFHLAVSDSLYAASLPLLVYYYAQGDHWPFSTVLCKLVRFLFYTNLYCSILFLTCISVHRCLGVLRPLHSLSWGHARYARRVAAVVWVLVLACQAPVLYFVTTSVRGTRITCHDTSARELFSHFVAYSSVMLGLLFAVPFSIILVCYVLMARRLLKPAYGTTGLPRAKRKSVRTIALVLAVFALCFLPFHVTRTLYYSFRSLDLSCHTLNAINMAYKITRPLASANSCLDPVLYFLAGQRLVRFARDAKPATEPTPSPQARRKLGLHRPNRTDTVRKDLSISSDDSRRTESTPAGSETKDIRL
Protein: Adhesion G protein-coupled receptor E5 (Leukocyte antigen CD97) (CD antigen CD97) [Cleaved into: Adhesion G protein-coupled receptor E5 subunit alpha; Adhesion G protein-coupled receptor E5 subunit beta] (P48960)
Organism: Homo sapiens (Human)
Function: Receptor potentially involved in both adhesion and signaling processes early after leukocyte activation. Plays an essential role in leukocyte migration.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9Z0M6}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Adhesion G protein-coupled receptor E5 subunit alpha]: Secreted, extracellular space {ECO:0000305}.
Interaction partners:
- Complement decay-accelerating factor
- Lysophosphatidic acid receptor 1
- Guanine nucleotide-binding protein subunit alpha-12
- CD59 glycoprotein
- Thy-1 membrane glycoprotein
- Secretin
Sequence:
MGGRVFLAFCVWLTLPGAETQDSRGCARWCPQNSSCVNATACRCNPGFSSFSEIITTPTETCDDINECATPSKVSCGKFSDCWNTEGSYDCVCSPGYEPVSGAKTFKNESENTCQDVDECQQNPRLCKSYGTCVNTLGSYTCQCLPGFKFIPEDPKVCTDVNECTSGQNPCHSSTHCLNNVGSYQCRCRPGWQPIPGSPNGPNNTVCEDVDECSSGQHQCDSSTVCFNTVGSYSCRCRPGWKPRHGIPNNQKDTVCEDMTFSTWTPPPGVHSQTLSRFFDKVQDLGRDSKTSSAEVTIQNVIKLVDELMEAPGDVEALAPPVRHLIATQLLSNLEDIMRILAKSLPKGPFTYISPSNTELTLMIQERGDKNVTMGQSSARMKLNWAVAAGAEDPGPAVAGILSIQNMTTLLANASLNLHSKKQAELEEIYESSIRGVQLRRLSAVNSIFLSHNNTKELNSPILFAFSHLESSDGEAGRDPPAKDVMPGPRQELLCAFWKSDSDRGGHWATEGCQVLGSKNGSTTCQCSHLSSFAILMAHYDVEDWKLTLITRVGLALSLFCLLLCILTFLLVRPIQGSRTTIHLHLCICLFVGSTIFLAGIENEGGQVGLRCRLVAGLLHYCFLAAFCWMSLEGLELYFLVVRVFQGQGLSTRWLCLIGYGVPLLIVGVSAAIYSKGYGRPRYCWLDFEQGFLWSFLGPVTFIILCNAVIFVTTVWKLTQKFSEINPDMKKLKKARALTITAIAQLFLLGCTWVFGLFIFDDRSLVLTYVFTILNCLQGAFLYLLHCLLNKKVREEYRKWACLVAGGSKYSEFTSTTSGTGHNQTRALRASESGI
Protein: (E,E)-geranyllinalool synthase (AtGES) (EC 4.2.3.144) (Terpenoid synthase 4) (AtTPS04) (Q93YV0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the biosynthesis of homoterpenes, attractants of herbivores parasitoids and predators (e.g. predatory mites and parasitoid wasps). Involved in diterpene (C20) biosynthesis. Catalyzes the conversion of geranylgeranyl diphosphate to (E,E)-geranyllinalool, the precursor of the insect-induced volatile C16-homoterpene TMTT.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18398052}.
Interaction partners:
- Dimethylnonatriene synthase
- Ent-copalyl diphosphate synthase, chloroplastic
- Geranylgeranyl diphosphate reductase, chloroplastic
- Solanesyl diphosphate synthase 1, chloroplastic
- Solanesyl diphosphate synthase 2, chloroplastic
- Geranylgeranyl pyrophosphate synthase 6, mitochondrial
- Geranylgeranyl pyrophosphate synthase 12, chloroplastic
- Geranylgeranyl pyrophosphate synthase 10, mitochondrial
- Heterodimeric geranylgeranyl pyrophosphate synthase large subunit 2
- Geranylgeranyl pyrophosphate synthase 7, chloroplastic
Sequence:
MKSSYGSSSNDLHAFVNEIKGEIQLSNINLDPYSFVSPSAYDTAWLSMIEEDINVDDNELKPMFQGCLDWIMCNQNAREGFWMNSTSYTTVADGRDEDGEKDMCILTSTLACVVALQKWNIGCFHLHKGTRYIERNTEMIIGKYINEEGSYPRWFAIKFTGILELAQKLGLHFVFSSRCIEMIKGMFYQRQEIIQREKLVHDCNYKPLLAYLEVLPSKLYVTNQEDIIVKSLDSMDGSLFQSPSATASAFMLTRNTKCLAYLQNLVQKCPNGVPQKYPLNEDLIKLSMVNLIESTGLGEFFGIEIEHVLEQVYSRYEEKDFERMPMSYLADQLHKDSLAFRMLRMHGRDVSPRSFCWFLNDQETRNHLERNIDSFLLVILSVYRATDLMFPGEHDLQEAREYTRNLLEKRRSIKEKMIMHELSTPWIARLKHLDHRMWIEDKNSNVLSMEKASFLRLHSSYSDKLTHLAARNFEFQQAKYCRELEELTMWVKKWGLSDIGFGREKTTYCYFATVTSLPYEYAIKFGKLAAKTAILITIADDFFDEKGSFNDLEGLTKAVLRWEGEELKSYGNIIFRALDDIVRETANTCRTHHKTDIIVHLRNIWGETFESWLREAEWSKKGHTSSMDEYIRNGMISIAAHTIALSISCLMEPCFPHNKLKPGNYDSITTLLMIIPRLLNDLQSYQKEQEQGKMNSVLLHMKNHPGLEIEDSIAHIEKIIDSKRKEFLEHVLVDGLSDLPKPCKEIHMSCCKVFEMFFNKKNRYDSNTEMLHDIKKALYDPINVYELSEMEPMPLMAHGDEYMILPLLLNSLPNILEFKRKDGYGAMKTSMCFGRSYRVNKRVMASQLDDQHKPLKIVASQRKPVPMMQSIFAPCFY
Protein: Down syndrome cell adhesion molecule 1, isoform AY (Q0E9L9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNMPNERLKWLMLFAAVALIACGSQTLAANPPDADQKGPVFLKEPTNRIDFSNSTGAEIECKASGNPMPEIIWIRSDGTAVGDVPGLRQISSDGKLVFPPFRAEDYRQEVHAQVYACLARNQFGSIISRDVHVRAVVHQFYQTRVIDEFVLRGNSATLKCLVPSFVADFIDVEGWIDEEGVEILRPLPDDSVDGKYLVLPSGELHIREVGPEDGYKSYQCRTKHRLTGETRLSATKGRLVITEPIGSVAPTISGDRLQEQTRKLGHSFSILCQGQAYPHPVFRWYKFIEGTTRKQAVVLNDRVKQVSGTLIIKDAVVEDSGKYLCVVNNSVGGESVETVLTVTAPLSAKIDPPTQTVDFGRPAVFTCQYTGNPIKTVSWMKDGKAIGHSEPVLRIESVKKEDKGMYQCFVRNDQESAEASAELKLGGRFDPPVIRQAFQEETMEPGPSVFLKCVAGGNPTPEISWELDGKKIANNDRYQVGQYVTVNGDVVSYLNITSVHANDGGLYKCIAKSKVGVAEHSAKLNVYGLPYIRQMEKKAIVAGETLIVTCPVAGYPIDSIVWERDNRALPINRKQKVFPNGTLIIENVERNSDQATYTCVAKNQEGYSARGSLEVQVMVPPKITPFDFGAEPTNVEDSVSVTCLISSGDLPIDIEWFFNDYGISSYSGINVVKGGKRNSMLSIDNVQARHAGKYSCRAKNYAAAVNYSTELIVNVPPRWILEPTDKAFAQGSDAKVECKADGFPKPQVTWKKAVGDTPGEYKDLKKSDNIRVEEGTLHVDNIQKTNEGYYLCEAINGIGSGLSAVIMISVQAPPEFTEKLRNQTARRGEPAVLQCEAKGEKPIGILWNMNNMRLDPKNDNRYTIREEILSTGVMSSLSIKRTERSDSALFTCVATNAFGSDDASINMIVQEVPEMPYALKVLDKSGRSVQLSWAQPYDGNSPLDRYIIEFKRSRASWSEIDRVIVPGHTTEAQVQKLSPATTYNIRIVAENAIGTSQSSEAVTIITAEEAPSGKPQNIKVEPVNQTTMRVTWKPPPRTEWNGEILGYYVGYKLSNTNSSYVFETINFITEEGKEHNLELQNLRVYTQYSVVIQAFNKIGAGPLSEEEKQFTAEGTPSQPPSDTACTTLTSQTIRVGWVSPPLESANGVIKTYKVVYAPSDEWYDETKRHYKKTASSDTVLHGLKKYTNYTMQVLATTAGGDGVRSVPIHCQTEPDVPEAPTDVKALVMGNAAILVSWRPPAQPNGIITQYTVYSKAEGAETETKTQKVPHYQMSFEATELEKNKPYEFWVTASTTIGEGQQSKSIVAMPSDQVPAKIASFDDTFTATFKEDAKMPCLAVGAPQPEITWKIKGVEFSANDRMRVLPDGSLLIKSVNRQDAGDYSCHAENSIAKDSITHKLIVLAPPQSPHVTLSATTTDALTVKLKPHEGDTAPLHGYTLHYKPEFGEWETSEVSVDSQKHNIEGLLCGSRYQVYATGFNNIGAGEASDILNTRTKGQKPKLPEKPRFIEVSSNSVSLHFKAWKDGGCPMSHFVVESKKRDQIEWNQISNNVKPDNNYVVLDLEPATWYNLRITAHNSAGFTVAEYDFATLTVTGGTIAPSRDLPELSAEDTIRIILSNLNLVVPVVAALLVIIIAIIVICILRSKGNHHKDDVVYNQTMGPGATLDKRRPDLRDELGYIAPPNRKLPPVPGSNYNTCDRIKRGRGGLRSNHSTWDPRRNPNLYEELKAPPVPMHGNHYGHAHGNAECHYRHPGMEDEICPYATFHLLGFREEMDPTKAMNFQTFPHQNGHAGPVPGHAGTMLPPGHPGHVHSRSGSQSMPRANRYQRKNSQGGQSSIYTPAPEYDDPANCAEEDQYRRYTRVNSQGGSLYSGPGPEYDDPANCAPEEDQYGSQYGGPYGQPYDHYGSRGSMGRRSIGSARNPGNGSPEPPPPPPRNHDMSNSSFNDSKESNEISEAECDRDHGPRGNYGAVKRSPQPKDQRTTEEMRKLIERNETGPKQLQLQQANGAGFTAYDTMAV
Protein: Anoctamin-8 (Transmembrane protein 16H) (Q9HCE9)
Organism: Homo sapiens (Human)
Function: Does not exhibit calcium-activated chloride channel (CaCC) activity.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20056604, ECO:0000269|PubMed:22946059}; Multi-pass membrane protein {ECO:0000269|PubMed:20056604, ECO:0000269|PubMed:22946059}. Note=Shows predominantly an intracellular localization with a weak expression in the cell membrane.
Interaction partners:
Sequence:
MAEAASGAGGTSLEGERGKRPPPEGEPAAPASGVLDKLFGKRLLQAGRYLVSHKAWMKTVPTENCDVLMTFPDTTDDHTLLWLLNHIRVGIPELIVQVRHHRHTRAYAFFVTATYESLLRGADELGLRKAVKAEFGGGTRGFSCEEDFIYENVESELRFFTSQERQSIIRFWLQNLRAKQGEALHNVRFLEDQPIIPELAARGIIQQVFPVHEQRILNRLMKSWVQAVCENQPLDDICDYFGVKIAMYFAWLGFYTSAMVYPAVFGSVLYTFTEADQTSRDVSCVVFALFNVIWSTLFLEEWKRRGAELAYKWGTLDSPGEAVEEPRPQFRGVRRISPITRAEEFYYPPWKRLLFQLLVSLPLCLACLVCVFLLMLGCFQLQELVLSVKGLPRLARFLPKVMLALLVSVSAEGYKKLAIWLNDMENYRLESAYEKHLIIKVVLFQFVNSYLSLFYIGFYLKDMERLKEMLATLLITRQFLQNVREVLQPHLYRRLGRGELGLRAVWELARALLGLLSLRRPAPRRLEPQADEGGGGGSGGGGRRCLSGGCGAPEEEEEAALVERRRAGEGGEEGDGPPGGKEEDEDDEEEEDEEEEEDEEEGEEGGLLDCGLRLKKVSFAERGAGRRRPGPSPEALLEEGSPTMVEKGLEPGVFTLAEEDDEAEGAPGSPEREPPAILFRRAGGEGRDQGPDGGPDPEPGSNSDSTRRQRRQNRSSWIDPPEEEHSPQLTQAELESCMKKYEDTFQDYQEMFVQFGYVVLFSSAFPLAALCALVNNLIEIRSDAFKLCTGLQRPFGQRVESIGQWQKVMEAMGVLAIVVNCYLIGQCGQLQRLFPWLSPEAAIVSVVVLEHFALLLKYLIHVAIPDIPGWVAEEMAKLEYQRREAFKRHERQAQHRYQQQQRRRREEEERQRHAEHHARREHDSGGREEARAEGSGLDPATSSEKASAKAKGSTAGGHGPERPKRPGSLLAPNNVMKLKQIIPLQGKFLSSGATSSLAAAGAGATTRPPPAQSPTGSDTRLPAFLSFKFLKSPETRRDSERSHSPPKAFHAGKLFPFGGTRAEPGSNGAGGQARPDGTPSSGSSRVQRSGPVDEALAEELEAPRPEEEGSGTALAPVGAPALRTRRSRSPAPPPPMPLPRPPTPPAGCWQWDGPWGCGGEGAAPRQALAAAECPPCAMAGPPPAPQPLPGDASFYSLPPPPLPPTSDPLETPAPSPSPSPSPQAVCWPSGWH
Protein: Nodal homolog (Nodal-related protein 1) (Xnr-1) (Xnr1) (nr-1) (Q91619)
Organism: Xenopus laevis (African clawed frog)
Function: Cooperation and regulatory loops of multiple nodals are essential for mesendoderm patterning in early embryos. Essential for mesoderm formation and axial patterning during embryonic development. Activates the activin-like signaling pathway to induce dorsal and ventral mesoderm in animal cap ectoderm. In addition, also dorsalizes ventral marginal zone (VMZ) tissues during gastrulation. Acts in a downstream signaling cascade via cripto and cer1 to mediate cardiogenesis in embryonic mesoderm. Directs the orientation of the left-right axis by driving the left-specific gene cascade in the left lateral plate mesoderm.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
Sequence:
MAFLTAVLYLGFACISQGLPTWPDRVESRNPLFGSRVALNLPSLLDGNRHHRDMRYPLYMMQLYQNLVTGNDTGLANRPNTATKEYDTVLSLFAKKCTESENRWTLSFDMSAVSRSNELKLAELRILLPHTEPSHNITMDMYHSRDGEDNLYLGSFNANPPSTKGSPWKVFNVTKILQPYFKERRDIDSEHLKAKERAERGSGMSNAEFIDAPGPSQQYNPHQTSVPTYLNTKGVMLVLFTKVKSSANHIGFPSLIKTAESSKYVDIEKASRVPGIRRHRRNRNENHHLSIGSIPSRHVENGKPLCRRVDMIVDFEDIGWSSWIVYPKKYNAYRCEGACPIPLNETFKPTNHAYMKSVVKLYQPERVECPLCVPVKMSPLSMLYYEGDEVVLRHHQEMIVEECGCS
Protein: Flavonol synthase/flavanone 3-hydroxylase (EC 1.14.11.9) (EC 1.14.20.6) (FLS 1) (Q96330)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the formation of flavonols from dihydroflavonols. It can act on dihydrokaempferol to produce kaempferol, on dihydroquercetin to produce quercitin and on dihydromyricetin to produce myricetin. In vitro catalyzes the oxidation of both enantiomers of naringenin to give both cis- and trans-dihydrokaempferol.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21502189}. Nucleus {ECO:0000269|PubMed:21502189}.
Interaction partners:
- Dihydroflavonol 4-reductase
- Flavonoid 3'-monooxygenase
- Chalcone synthase
- Naringenin,2-oxoglutarate 3-dioxygenase
- Flavonol 3-O-glucosyltransferase
- Transcription factor MYB12
- Trans-cinnamate 4-monooxygenase
- Anthocyanidin reductase
- Flavonol-3-O-rhamnosyltransferase
- Phenylalanine ammonia-lyase 1
Sequence:
MEVERVQDISSSSLLTEAIPLEFIRSEKEQPAITTFRGPTPAIPVVDLSDPDEESVRRAVVKASEEWGLFQVVNHGIPTELIRRLQDVGRKFFELPSSEKESVAKPEDSKDIEGYGTKLQKDPEGKKAWVDHLFHRIWPPSCVNYRFWPKNPPEYREVNEEYAVHVKKLSETLLGILSDGLGLKRDALKEGLGGEMAEYMMKINYYPPCPRPDLALGVPAHTDLSGITLLVPNEVPGLQVFKDDHWFDAEYIPSAVIVHIGDQILRLSNGRYKNVLHRTTVDKEKTRMSWPVFLEPPREKIVGPLPELTGDDNPPKFKPFAFKDYSYRKLNKLPLD
Protein: Chaperonin homolog Hsp-60, mitochondrial (Heat shock protein 60) (HSP-60) (P50140)
Organism: Caenorhabditis elegans
Function: Implicated in mitochondrial protein import and macromolecular assembly. May facilitate the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix (By similarity).
Subcellular location: Mitochondrion matrix.
Interaction partners:
- Heat shock protein hsp-6
- 10 kDa heat shock protein, mitochondrial
- Endoplasmic reticulum chaperone BiP homolog
- Heat shock protein 90
- GrpE protein homolog
- T-complex protein 1 subunit alpha
- ATP-dependent Clp protease proteolytic subunit 1, mitochondrial
- T-complex protein 1 subunit theta
- AFG3-like protein spg-7
- Stress activated transcription factor atfs-1
Sequence:
MLRLARKGLQTAVVRSYAKDVKFGAEGRQAMLVGVNLLADAVSVTMGPKGRNVIIEQSWGSPKITKDGVTVAKSIDLKDKYQNLGAKLIQDVANKANEEAGDGTTCATVLARAIAKEGFESIRQGGNAVEIRRGVMNAVEVVVAELKKISKKVTTPEEIAQVATISANGDTVVGNLISDAMKKVGTTGVITVKDGKTLNDELELIEGMKFDRGYISPYFITSAKGAKVEYEKALVLLSEKKISQVQDIVPALELANKLRRPLVIIAEDVDGEALTTLVLNRLKVGLQVVAIKAPGFGDNRKNTLKDMGIATGATIFGDDSNLIKIEDITANDLGEVDEVTITKDDTLLLRGRGDQTEIEKRIEHITDEIEQSTSDYEKEKLNERLAKLSKGVAVLKIGGGSEVEVGEKKDRVTDALCATRAAVEEGIVPGGGVALLRSLTALKNYKAANEDQQIGVNIVKKALTQPIATIVKNAGLEPSSIIDEVTGNSNTSYGYDALNGKFVDMFEAGIIDPTKVVRTALQDASGVASLLATTECVVTEIPKEEAVGGPAGGMGGMGGMGGMGGMGF
Protein: Possible oxidoreductase (O69694)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Isoniazid-induced protein IniB
- ESX-1 secretion-associated protein EspE
- Probable conserved two-domain membrane protein
- PPE family protein PPE8
- PPE family protein PPE55
- PPE family protein PPE5
- Probable membrane protein
- Uncharacterized protein Rv2209
- PPE family protein PPE56
- PE-PGRS family protein PE_PGRS28
Sequence:
MKPSPADTHVVIAGAGIAGLAAAMILAEAGVRVTLCEAASEAGGKAKSLRLADGHPTEHSLRVYTDTYQTLLTLFSRIPTEHDRTVLDNLVGVSMVSATAQGVIGRIAAPVALQRRRPTFARIIGKVVEPPRQLVRILLRGPMVIVGLAQRGVPATDVLHYLYAHLRLLWMCRERLLAELGDISYADYLQLGCKSAQAQEFFSAVPRIYVAARTSAEAAAIAPIVLKGLFRLKSNCPSALNDAKLPAIMMMDGPTSERMVDPWIRHLTRLGVDIHFNTRVGDLEFDDGRVTALISSDGRRFACDYALLAVPYLTLRELAKSAHVKRYLPQLTQQHALALEASNGIQCFLRDLPATWPPFIRPGVVTTHLQSQWSLVCVLQGEGFWKNVRLPEGTRYVLSITWSDVETPGPVFDRPLSECTPDEILTECLTQCGLDKSNVLGWRIDHELKHLDEAEYEKVASELPPHLVSAPARGQRMVNFSPLTVLMPGARHRSPGICTSVPNLLLAGEVIYSPDLTLFVPTMEKAACSGYLAARQIMNMVASHAAPLRIDFRDPAPFAVLRRVDRWFWSRRRRPPDRSTFATPPTAMPAPSHLTDVDRSAS
Protein: HLH54F (RT01030p) (Q0IGU7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Protein daughterless
Sequence:
MPRKKRSSSPTEFFDDDFDEDASSQSSQPPVQRNAANARERMRMRVLSSAYGRLKTKLPNIPPDTKLSKLDTLRLATLYIKQLITAVETGSHSQNHPHNHNQHHSLNHSHSSTTSSEGLDTSHMADSSGGGNYNFHNNGHGMSWPFEFHQSSRSLAFAPSSSTTSSARMDWQTLHTQSYPKTTRGETHVSADLSYHQLPESHSHWYPAEVHQMEPAASCSYDSGMGQHQRGIAIATSHAHGI
Protein: Perilipin-2 (Adipophilin) (Adipose differentiation-related protein) (ADRP) (Q4PLW0)
Organism: Sus scrofa (Pig)
Function: Structural component of lipid droplets, which is required for the formation and maintenance of lipid storage droplets.
Subcellular location: Membrane {ECO:0000250|UniProtKB:P43883}; Peripheral membrane protein {ECO:0000250|UniProtKB:P43883}. Lipid droplet {ECO:0000250|UniProtKB:P43883}.
Interaction partners:
- Hormone-sensitive lipase
- 1-acylglycerol-3-phosphate O-acyltransferase ABHD5
- Peroxisome proliferator-activated receptor gamma
- carnitine O-palmitoyltransferase
- Fatty acid-binding protein, adipocyte
- O-acyltransferase
Sequence:
MASVAVESQPSVVTRVANLPLVSSTYDLVSSAYISTKDQYPYLKSLCEMAEKGVKTITSVAMSGALPIIQKLEPQIAIANTYACKGLDRIEEKLPILNQPTNQVVANAKGAVTGAKDAMTTTVTGAKDCVASTITEVVDKTKEAVTGSVEKTKSVVNGSINTVLGGRMMQLVSSGVEKAFTKSELLVDQYLPLTEEELEKEAKKVEGFDMVQKPSYYIRLGSLSTKLRSRAYQQALTRVKEVKQKSQETISQLHSTVNLIEFARKNVHNANQKIQGTQDKLYLSWVEWKRSIGYDDTDESHCAEHIESRTLAIARNLTQQLQTTCHTLVSNIQGLPQNIHDQANHLGVMAGDIYSVFHNASSFKEMSDGLLSSSKGQLQKMKESLDDVMDYLVNNTPLNWLVGPFYPQLTESQDAQSRGAENTTSPETQQPETKRIKPAPASSAWGSQSGDTSCTVATC
Protein: T cell receptor beta, variable 13-3 (A0A0B4J1H2)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MGSRLFFVVLILLCAKHMEAAVTQSPRSKVAVTGGKVTLSCHQTNNHDYMYWYRQDTGHGLRLIHYSYVADSTEKGDIPDGYKASRPSQENFSLILELASLSQTAVYFCASSD
Protein: Probable E3 SUMO-protein ligase RNF212 (EC 2.3.2.-) (Probable E3 SUMO-protein transferase RNF212) (RING finger protein 212) (F6TQD1)
Organism: Mus musculus (Mouse)
Function: SUMO E3 ligase that acts as a regulator of crossing-over during meiosis: required to couple chromosome synapsis to the formation of crossover-specific recombination complexes. Localizes to recombination sites and stabilizes meiosis-specific recombination factors, such as MutS-gamma complex proteins (MSH4 and MSH5) and TEX11. May mediate sumoylation of target proteins MSH4 and/or MSH5, leading to enhance their binding to recombination sites. Acts as a limiting factor for crossover designation and/or reinforcement and plays an antagonist role with CCNB1IP1/HEI10 in the regulation of meiotic recombination.
Subcellular location: Nucleus. Chromosome. Note=Associates to the synaptonemal complex. Localizes to a minority of double-strand breaks (DSBs) sites. Marks crossover sites during midpachynema.
Interaction partners:
- MutS protein homolog 4
- E3 ubiquitin-protein ligase CCNB1IP1
- Synaptonemal complex protein 1
- Meiotic recombination protein SPO11
- Testis-expressed protein 11
- Histone-lysine N-methyltransferase PRDM9
- Meiotic recombination protein REC8 homolog
- Probable ATP-dependent DNA helicase HFM1
- Cyclin N-terminal domain-containing protein 1
Sequence:
MASWVFCNRCFQSPHRKSSFSLTSCGHVYCHSCLLKGTKNECVICQAPCQTVLLSKHTNSNIQTFFLGIDGLCKKYSQETSQISEFQEKHRRRLVAFYQEKISQLEESLRKSVLQIKQLQSMRSSQQPAFNKIKNSVSTKPNGYLFLPPNSSLPDRIESMDIDLTPPARKPEMSAGPSRISVISPPQDGRMGSVTCRGPQHLSLTPSHASMTKASRVPPLQMPYKELSPPPASQLSSRATQGPSPSVSSSWTGPPRQPISISGLLQRQCAGSASPRGMDTEKMSPFLPSTPTNLRSVASPWHACVHR
Protein: Uncharacterized protein C16A11.15c (Q9USM2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
Sequence:
MSLRHSTQLIVQTVKLGLPTARKACSLPIQNPVVAANRFFASSVHSRNPQEEDVIPPKENASREDATDSEAYVRSDWDNTPIPELEKETAEKAASERQHSEKVTINDKTSPPSVDEM
Protein: Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (UDP-GlcNAc-2-epimerase/ManAc kinase) [Includes: UDP-N-acetylglucosamine 2-epimerase (hydrolyzing) (EC 3.2.1.183) (UDP-GlcNAc-2-epimerase) (Uridine diphosphate-N-acetylglucosamine-2-epimerase) (rEpi); N-acetylmannosamine kinase (EC 2.7.1.60) (ManAc kinase)] (O35826)
Organism: Rattus norvegicus (Rat)
Function: Regulates and initiates biosynthesis of N-acetylneuraminic acid (NeuAc), a precursor of sialic acids. Required for normal sialylation in hematopoietic cells. Sialylation is implicated in cell adhesion, signal transduction, tumorigenicity and metastatic behavior of malignant cells. Plays an essential role in early development (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:9305887, ECO:0000269|PubMed:9305888}.
Interaction partners:
- N-acetylneuraminate-9-phosphate synthase
- N-acetylneuraminate lyase
- N-acylglucosamine 2-epimerase
- UDP-N-acetylhexosamine pyrophosphorylase
- N-acetylglucosamine-6-phosphate deacetylase
- UDP-N-acetylhexosamine pyrophosphorylase-like protein 1
- Transaldolase
- Glucose-6-phosphate isomerase
- GDH/6PGL endoplasmic bifunctional protein
- Protein-glucosylgalactosylhydroxylysine glucosidase
Sequence:
MEKNGNNRKLRVCVATCNRADYSKLAPIMFGIKTEPAFFELDVVVLGSHLIDDYGNTYRMIEQDDFDINTRLHTIVRGEDEAAMVESVGLALVKLPDVLNRLKPDIMIVHGDRFDALALATSAALMNIRILHIEGGEVSGTIDDSIRHAITKLAHYHVCCTRSAEQHLISMCEDHDRILLAGCPSYDKLLSAKNKDYMSIIRMWLGDDVKCKDYIVALQHPVTTDIKHSIKMFELTLDALISFNKRTLVLFPNIDAGSKEMVRVMRKKGIEHHPNFRAVKHVPFDQFIQLVAHAGCMIGNSSCGVREVGAFGTPVINLGTRQIGRETGENVLHVRDADTQDKILQALHLQFGKQYPCSKIYGDGNAVPRILKFLKSIDLQEPLQKKFCFPPVKENISQDIDHILETLSALAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKTYEERISLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPQEGVVLHSTKLIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDLLLVEGMSVPKDEAVGALHLIQAAKLGNVKAQSILRTAGTALGLGVVNILHTMNPSLVILSGVLASHYIHIVRDVIRQQALSSVQDVDVVVSDLVDPALLGAASMVLDYTTRRIH
Protein: Uncharacterized protein C9.08c (Q9UT20)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Delta
- Delta
- Delta
Sequence:
MFYSDYLKLLKIFVVGVFPCTLFVNAPHGKLAKQSKLFSKGYISGRVGWVLMELVAPLTFLYAIRNNRHFESTLPSLGDGSNRDYLDSCRKVLAGMFLVHYANRALVSPLLMAPQVSPMHWTVFVSAVLFNFLNGMSIGLYLVQASVQHHPVSIIRRYIGMFLWLMGWLGNMYHDNILYDLRRSSNKKKDPDNLDTVQSENSYYRIPYGGLFQYVSCPNYFCEWIEWFGCYLAAGPSAEPFWWFFLSEILLMLPRALKAHQWYCKKFPKYPANRRAIIPFLM
Protein: Polyadenylate-binding protein 8 (PABP-8) (Poly(A)-binding protein 8) (Q9FXA2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds the poly(A) tail of mRNA. Appears to be an important mediator of the multiple roles of the poly(A) tail in mRNA biogenesis, stability and translation (By similarity). During infection with potyvirus TuMV, acts as a potential integral component of the viral replicase complex that could play an important role in the regulation of potyviral RNA-dependent RNA polymerase (RdRp) (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Eukaryotic translation initiation factor 4E-1
- mRNA-decapping enzyme-like protein
- Eukaryotic translation initiation factor 4G
- Nuclear cap-binding protein subunit 2
- Large ribosomal subunit protein eL15y
- Eukaryotic translation initiation factor 2 subunit alpha homolog
- At5g23850
- Eukaryotic translation initiation factor isoform 4G-2
- Gb|AAD20086.1 family protein with RNA binding
- Eukaryotic translation initiation factor isoform 4G-1
Sequence:
MAQIQHQGQNANGGVAVPGAAAAEAAAAAAGAAAAAAGAAQQGTTSLYVGDLDATVTDSQLFEAFTQAGQVVSVRVCRDMTTRRSLGYGYVNYATPQDASRALNELNFMALNGRAIRVMYSVRDPSLRKSGVGNIFIKNLDKSIDHKALHETFSAFGPILSCKVAVDPSGQSKGYGFVQYDTDEAAQGAIDKLNGMLLNDKQVYVGPFVHKLQRDPSGEKVKFTNVYVKNLSESLSDEELNKVFGEFGVTTSCVIMRDGEGKSKGFGFVNFENSDDAARAVDALNGKTFDDKEWFVGKAQKKSERETELKQKFEQSLKEAADKSQGSNLYVKNLDESVTDDKLREHFAPFGTITSCKVMRDPSGVSRGSGFVAFSTPEEATRAITEMNGKMIVTKPLYVALAQRKEDRKARLQAQFSQMRPVNMPPAVGPRMQMYPPGGPPMGQQLFYGQGPPAMIPQPGFGYQQQLVPGMRPGGSPMPNFFMPMMQQGQQQQQQQQQQQRPGGGRRGALPQPQQPSPMMQQQMHPRGRMYRYPQRDVNTMPGPTQNMLSVPYDVSSGGGVHHRDSPTSQPVPIVALATRLANAAPEQQRTMLGENLYPLVEQLEPESAAKVTGMLLEMDQTEVLHLLESPEALKAKVTEAMDVLRSVAQQQAGGAADQLASLSLGDNIVP
Protein: Transcriptional regulator MntR (Manganese transport regulator) (P0A9F1)
Organism: Escherichia coli (strain K12)
Function: In the presence of manganese, represses expression of mntH and mntS. Up-regulates expression of mntP.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Divalent metal cation transporter MntH
- Inner membrane protein YbiR
- Probable manganese efflux pump MntP
- Small protein MntS
- Formate hydrogenlyase subunit 7
- Methionine import ATP-binding protein MetN
- HTH-type transcriptional regulator PerR
- Zinc transporter ZupT
- Epimerase family protein YfcH
- Transcriptional repressor RcnR
Sequence:
MSRRAGTPTAKKVTQLVNVEEHVEGFRQVREAHRRELIDDYVELISDLIREVGEARQVDMAARLGVSQPTVAKMLKRLATMGLIEMIPWRGVFLTAEGEKLAQESRERHQIVENFLLVLGVSPEIARRDAEGMEHHVSEETLDAFRLFTQKHGAK