wanglab/gogpt-training-data huggingface dataset:
Protein: Ena/VASP-like protein (Ena/vasodilator-stimulated phosphoprotein-like) (Q9UI08)
Organism: Homo sapiens (Human)
Function: Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance and lamellipodial and filopodial dynamics in migrating cells. EVL enhances actin nucleation and polymerization.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P70429}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:P70429}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:P70429}. Note=Targeted to the leading edge of lamellipodia and the distal tip of stress fibers through interaction with a number of proteins. In activated T-cells, localizes to the F-actin collar and the distal tip of microspikes. {ECO:0000250|UniProtKB:P70429}.
Interaction partners:
- Vasodilator-stimulated phosphoprotein
- Protein enabled homolog
- Amyloid beta A4 precursor protein-binding family B member 1-interacting protein
- Zyxin
- Actin, cytoplasmic 2
- Actin, cytoplasmic 1
- Semaphorin-6A
- Profilin-1
- Profilin-2
- Semaphorin-6B
Sequence:
MSEQSICQARASVMVYDDTSKKWVPIKPGQQGFSRINIYHNTASNTFRVVGVKLQDQQVVINYSIVKGLKYNQATPTFHQWRDARQVYGLNFASKEEATTFSNAMLFALNIMNSQEGGPSSQRQVQNGPSPDEMDIQRRQVMEQHQQQRQESLERRTSATGPILPPGHPSSAASAPVSCSGPPPPPPPPVPPPPTGATPPPPPPLPAGGAQGSSHDESSMSGLAAAIAGAKLRRVQRPEDASGGSSPSGTSKSDANRASSGGGGGGLMEEMNKLLAKRRKAASQSDKPAEKKEDESQMEDPSTSPSPGTRAASQPPNSSEAGRKPWERSNSVEKPVSSILSRTPSVAKSPEAKSPLQSQPHSRMKPAGSVNDMALDAFDLDRMKQEILEEVVRELHKVKEEIIDAIRQELSGISTT
Protein: Protein LMBR1L (Limb region 1 protein homolog-like) (Lipocalin-1-interacting membrane receptor) (LIMR) (Q6UX01)
Organism: Homo sapiens (Human)
Function: Plays an essential role in lymphocyte development by negatively regulating the canonical Wnt signaling pathway (By similarity). In association with UBAC2 and E3 ubiquitin-protein ligase AMFR, promotes the ubiquitin-mediated degradation of CTNNB1 and Wnt receptors FZD6 and LRP6 (By similarity). LMBR1L stabilizes the beta-catenin destruction complex that is required for regulating CTNNB1 levels (By similarity). Acts as a LCN1 receptor and can mediate its endocytosis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11287427, ECO:0000269|PubMed:17991420, ECO:0000269|PubMed:31073040}; Multi-pass membrane protein {ECO:0000269|PubMed:11287427}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:31073040}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Lipocalin-1
- Aryl hydrocarbon receptor repressor
Sequence:
MEAPDYEVLSVREQLFHERIRECIISTLLFATLYILCHIFLTRFKKPAEFTTVDDEDATVNKIALELCTFTLAIALGAVLLLPFSIISNEVLLSLPRNYYIQWLNGSLIHGLWNLVFLFSNLSLIFLMPFAYFFTESEGFAGSRKGVLGRVYETVVMLMLLTLLVLGMVWVASAIVDKNKANRESLYDFWEYYLPYLYSCISFLGVLLLLVCTPLGLARMFSVTGKLLVKPRLLEDLEEQLYCSAFEEAALTRRICNPTSCWLPLDMELLHRQVLALQTQRVLLEKRRKASAWQRNLGYPLAMLCLLVLTGLSVLIVAIHILELLIDEAAMPRGMQGTSLGQVSFSKLGSFGAVIQVVLIFYLMVSSVVGFYSSPLFRSLRPRWHDTAMTQIIGNCVCLLVLSSALPVFSRTLGLTRFDLLGDFGRFNWLGNFYIVFLYNAAFAGLTTLCLVKTFTAAVRAELIRAFGLDRLPLPVSGFPQASRKTQHQ
Protein: Exocrine gland secreted peptide 15 (Exocrine gland-secreting peptide 15) (A8R0U8)
Organism: Mus musculus (Mouse)
Interaction partners:
- Exocrine gland secreted peptide 16
Sequence:
MASFPLMYFLIILVFPTILLEGMALKRTEKEPNISADLNDDFEISFIQTIRDRLDLMRMLSGSVIGKIYLNYDVVMYCRECSLTM
Protein: IMP U3 small nucleolar ribonucleoprotein 4 (H0Y714)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
Sequence:
XSKCLPAVFLAHWVLLLVLRVFLPCDENRLIPTELRREALALQGSLEFDDAGGEGVTSHVDDEYRWAGVEDPKVMITTSRDPSSRLKMFAKELKLVFPGAQRMNRGRHEVGALVRACKANGVTDLLVVHEHRGTPVGLIVSHLPFGPTAYFTLCNVVMRHDIPDLGTMSEAKPHLITHGFSSRLGKRVSDILRYLFPVPKDDSHRVITFANQDDYISFRHHVYKKTDHRNVELTEVGPRFELKLYMIRLGTLEQEATADVEWRWHPYTNTARKRVFLSTE
Protein: C-type lectin domain family 4 member K (Langerin) (CD antigen CD207) (Q9UJ71)
Organism: Homo sapiens (Human)
Function: Calcium-dependent lectin displaying mannose-binding specificity. Induces the formation of Birbeck granules (BGs); is a potent regulator of membrane superimposition and zippering. Binds to sulfated as well as mannosylated glycans, keratan sulfate (KS) and beta-glucans. Facilitates uptake of antigens and is involved in the routing and/or processing of antigen for presentation to T cells. Major receptor on primary Langerhans cells for Candida species, Saccharomyces species, and Malassezia furfur. Protects against human immunodeficiency virus-1 (HIV-1) infection. Binds to high-mannose structures present on the envelope glycoprotein which is followed by subsequent targeting of the virus to the Birbeck granules leading to its rapid degradation.
Subcellular location: Membrane {ECO:0000269|PubMed:10661407}; Single-pass type II membrane protein {ECO:0000269|PubMed:10661407}. Note=Found in Birbeck granules (BGs), which are organelles consisting of superimposed and zippered membranes.
Interaction partners:
- T-cell surface glycoprotein CD1a
- T-cell surface glycoprotein CD1e, membrane-associated
- T-cell surface glycoprotein CD1b
- T-cell surface glycoprotein CD1c
- Inter-alpha-trypsin inhibitor heavy chain H4
- Antigen-presenting glycoprotein CD1d
- Integrin alpha-X
- Lymphocyte antigen 75
- T-cell surface glycoprotein CD4
- Lysosome-associated membrane glycoprotein 3
Sequence:
MTVEKEAPDAHFTVDKQNISLWPREPPPKSGPSLVPGKTPTVRAALICLTLVLVASVLLQAVLYPRFMGTISDVKTNVQLLKGRVDNISTLDSEIKKNSDGMEAAGVQIQMVNESLGYVRSQFLKLKTSVEKANAQIQILTRSWEEVSTLNAQIPELKSDLEKASALNTKIRALQGSLENMSKLLKRQNDILQVVSQGWKYFKGNFYYFSLIPKTWYSAEQFCVSRNSHLTSVTSESEQEFLYKTAGGLIYWIGLTKAGMEGDWSWVDDTPFNKVQSVRFWIPGEPNNAGNNEHCGNIKAPSLQAWNDAPCDKTFLFICKRPYVPSEP
Protein: Isocitrate dehydrogenase [NAD] subunit 2, mitochondrial (EC 1.1.1.41) (Isocitric dehydrogenase) (NAD(+)-specific ICDH) (Q9USP8)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Performs an essential role in the oxidative function of the citric acid cycle and is involved in glutamate biosynthesis. Also binds RNA; specifically to the 5'-untranslated leaders of mitochondrial mRNAs.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Isocitrate dehydrogenase subunit 1, mitochondrial
- Aconitate hydratase, mitochondrial
- 2-oxoglutarate dehydrogenase, mitochondrial
- Probable isocitrate dehydrogenase, mitochondrial
- Probable citrate synthase, mitochondrial
- Glutamate synthase
- Probable NAD-specific glutamate dehydrogenase
- Aconitase-ribosomal protein bL21m fusion protein
- NADP-specific glutamate dehydrogenase
- Succinate--CoA ligase subunit beta, mitochondrial
Sequence:
MSMLSTLRTAGSLRTFSRSACYSFQRFSSTKAAAGTYEGVKNANGNYTVTMIAGDGIGPEIAQSVERIFKAAKVPIEWERVKVYPILKNGTTTIPDDAKESVRKNKVALKGPLATPIGKGHVSMNLTLRRTFGLFANVRPCVSITGYKTPYDNVNTVLIRENTEGEYSGIEHEVIPGVVQSIKLITRAASERVIRYAFQYARQTGKNNITVVHKATIMRMADGLFLECAKELAPEYPDIELREEILDNACLKIVTDPVPYNNTVMVMPNLYGDIVSDMCAGLIGGLGLTPSGNIGNQASIFEAVHGTAPDIAGKGLANPTALLLSSVMMLKHMNLNDYAKRIESAIFDTLANNPDARTKDLGGKSNNVQYTDAIISKLK
Protein: Ell-associated factor Eaf (Q9TXQ9)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- OCEL domain-containing protein
- Putative transcription elongation factor S-II
- DNA-directed RNA polymerase II subunit rpb-9
- IWS1-like protein
- DNA-directed RNA polymerase II subunit RPB2
- RNA polymerase II subunit A C-terminal domain phosphatase
- Suppressor of Ty 6 homolog
- DNA-directed RNA polymerase RpoA/D/Rpb3-type domain-containing protein
- Transcription elongation factor SPT5
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
Sequence:
MAESSDIPNGTYTLTLGKSFEVKGRKSDPKAEQFHTLRYDFKPSSVSNNADTFIAFGNSGDVHVSVPSEGDNMTVYKGSKKEAKPKECLLFFDKKTNTVRLEKITSNINVKKTRDLDQGTELALKRGIERLRTSSNNQRSGPSSPEEKAKIQKQMQRDTSDSSSDSDGSSDSDKSNGDSSDDEDESEKILLEEMKKPKPYTEREPAPPSSSNTYNHKESHVAPYISSSGNKNKDSEEKYGLALSESSDEDD
Protein: Calcyclin-binding protein (CacyBP) (Siah-interacting protein) (Q9CXW3)
Organism: Mus musculus (Mouse)
Function: May be involved in calcium-dependent ubiquitination and subsequent proteasomal degradation of target proteins. Probably serves as a molecular bridge in ubiquitin E3 complexes. Participates in the ubiquitin-mediated degradation of beta-catenin (CTNNB1) (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:11927578}. Cytoplasm {ECO:0000269|PubMed:11927578}. Note=Cytoplasmic in unstimulated cultured neurons. Upon increase of calcium, it localizes to a ring around the nucleus. In neuroblastoma cells, after a Retinoic acid (RA) induction and calcium increase, it localizes in both the nucleus and cytoplasm. The nuclear and perinuclear fractions may be phosphorylated.
Interaction partners:
- Protein S100-A6
- S-phase kinase-associated protein 1
- E3 ubiquitin-protein ligase SIAH1A
- E3 ubiquitin-protein ligase SIAH1B
- Catenin beta-1
- Heat shock protein HSP 90-alpha
- E3 ubiquitin-protein ligase SIAH2
- Glycogen synthase kinase-3 beta
- Beta-catenin-interacting protein 1
- Glutaredoxin-3
Sequence:
MASVLEELQKDLEEVKVLLEKSTRKRLRDTLTSEKSKIETELKNKMQQKSQKKPELDNEKPAAVVAPLTTGYTVKISNYGWDQSDKFVKIYITLTGVHQVPTENVQVHFTERSFDLLVKNLNGKNYSMIVNNLLKPISVESSSKKVKTDTVIILCRKKAENTRWDYLTQVEKECKEKEKPSYDTEADPSEGLMNVLKKIYEDGDDDMKRTINKAWVESREKQAREDTEF
Protein: Transcription factor MafB (Maf-B) (Kreisler) (Segmentation protein Kr) (Transcription factor Maf-1) (V-maf musculoaponeurotic fibrosarcoma oncogene homolog B) (P54841)
Organism: Mus musculus (Mouse)
Function: Acts as a transcriptional activator or repressor. Plays a pivotal role in regulating lineage-specific hematopoiesis by repressing ETS1-mediated transcription of erythroid-specific genes in myeloid cells. Required for monocytic, macrophage, osteoclast, podocyte and islet beta cell differentiation. Involved in renal tubule survival and F4/80 maturation. Activates the insulin and glucagon promoters. Together with PAX6, transactivates weakly the glucagon gene promoter through the G1 element. SUMO modification controls its transcriptional activity and ability to specify macrophage fate. Binds element G1 on the glucagon promoter. Involved either as an oncogene or as a tumor suppressor, depending on the cell context. Required for the transcriptional activation of HOXB3 in the rhombomere r5 in the hindbrain.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:15135046}.
Interaction partners:
- Transcription factor Jun
- Protein c-Fos
- Protein C-ets-1
- Homeobox protein Nkx-6.1
- Interferon regulatory factor 8
- Transcription factor PU.1
- Paired box protein Pax-6
Sequence:
MAAELSMGQELPTSPLAMEYVNDFDLLKFDVKKEPLGRAERPGRPCTRLQPAGSVSSTPLSTPCSSVPSSPSFSPTEPKTHLEDLYWMASNYQQMNPEALNLTPEDAVEALIGSHPVPQPLQSFDGFRSAHHHHHHHHPHPHHGYPGAGVTHDDLGQHAHPHHHHHHQASPPPSSAASPAQQLPTSHPGPGPHATAAATAAGGNGSVEDRFSDDQLVSMSVRELNRHLRGFTKDEVIRLKQKRRTLKNRGYAQSCRYKRVQQKHHLENEKTQLIQQVEQLKQEVSRLARERDAYKVKCEKLANSGFREAGSTSDSPSSPEFFL
Protein: Guanine nucleotide-binding protein alpha-1 subunit (GP-alpha-1) (Protein Daikoku dwarf) (Protein Dwarf1) (Q0DJ33)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems (Probable). May function in a signal transduction pathway required for normal growth and development of internodes, leaves, panicles and seeds. Involved in gibberellin signal transduction. Involved in R gene-mediated disease resistance. Functions upstream of the small GTPase RAC1 in the early steps of signaling. Involved in brassinosteroid (BR) response. May not be a signaling molecule in BRI1-mediated perception or transduction. Acts together with the E3 ubiquitin ligase TUD1 to mediate a BR signaling pathway that affects plant growth and development.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15078334}.
Interaction partners:
- Guanine nucleotide-binding protein subunit beta
- Os02g0329300 protein.
- Ubiquitin carboxyl-terminal hydrolase
- ubiquitinyl hydrolase 1
- Ubiquitin carboxyl-terminal hydrolase
- protein-serine/threonine phosphatase
- Guanine nucleotide-binding protein subunit gamma 2
- Expressed protein
- Os07g0187400 protein
- Os06g0155600 protein
Sequence:
MGSSCSRSHSLSEAETTKNAKSADIDRRILQETKAEQHIHKLLLLGAGESGKSTIFKQIKLLFQTGFDEAELRSYTSVIHANVYQTIKILYEGAKELSQVESDSSKYVISPDNQEIGEKLSDIDGRLDYPLLNKELVLDVKRLWQDPAIQETYLRGSILQLPDCAQYFMENLDRLAEAGYVPTKEDVLYARVRTNGVVQIQFSPVGENKRGGEVYRLYDVGGQRNERRKWIHLFEGVNAVIFCAAISEYDQMLFEDETKNRMMETKELFDWVLKQRCFEKTSFILFLNKFDIFEKKIQKVPLSVCEWFKDYQPIAPGKQEVEHAYEFVKKKFEELYFQSSKPDRVDRVFKIYRTTALDQKLVKKTFKLIDESMRRSREGT
Protein: Protease inhibitor/seed storage/lipid transfer protein (LTP) family protein (F4JLV4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Probable carboxylesterase 6
- Short-chain dehydrogenase reductase 5
- NAD
- Protein PELPK1
- Acyltransferase-like protein
- Acyltransferase-like protein
- 2S seed storage protein 5
- Ankyrin repeat/KH domain protein
Sequence:
MASTTIILFLSFSIIPLLTIVRADNHSVYCPPPPPCICICNPGPPPPQPDPQPPTPPTFQPAPPANDQPPPPPQSTSPPPVATTPPALPPKPLPPPLSPPQTTPPPPPAITPPPPPAITPPLSPPPPAITPPPPLATTPPALPPKPLPPPLSPPQTTPPPPPAITPPLSPPLVGICSKNDTELKICAGILAISDGLLTTGRAEPCCSIIRNVSDLDAVTCFCKSVGAPRFSLSPNFGIFFKVCGRRIPQGFSCPGPSPTISPPPLPPQTLKPPPPQTTPPPPPAITPPLSPPLVGICSKNDTELKICAGILAISDGLLTTGRAEPCCSIVRNVSDLDAVTCFCKSVGARRFSLSPNFGIFFKVCGRRIPQGFSCP
Protein: Membrane-bound lytic murein transglycosylase D (EC 4.2.2.n1) (Murein hydrolase D) (Regulatory protein DniR) (P0AEZ7)
Organism: Escherichia coli (strain K12)
Function: Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division (By similarity).
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
Interaction partners:
- Membrane-bound lytic murein transglycosylase F
- Endolytic murein transglycosylase
- Soluble lytic murein transglycosylase
- Membrane-bound lytic murein transglycosylase B
- Membrane-bound lytic murein transglycosylase A
- Membrane-bound lytic murein transglycosylase C
- Endo-type membrane-bound lytic murein transglycosylase A
- Endolytic peptidoglycan transglycosylase RlpA
- Anhydromuropeptide permease
- Peptidoglycan D,D-transpeptidase MrdA
Sequence:
MKAKAILLASVLLVGCQSTGNVQQHAQSLSAAGQGEAAKFTSQARWMDDGTSIAPDGDLWAFIGDELKMGIPENDRIREQKQKYLRNKSYLHDVTLRAEPYMYWIAGQVKKRNMPMELVLLPIVESAFDPHATSGANAAGIWQIIPSTGRNYGLKQTRNYDARRDVVASTTAALNMMQRLNKMFDGDWLLTVAAYNSGEGRVMKAIKTNKARGKSTDFWSLPLPQETKQYVPKMLALSDILKNSKRYGVRLPTTDESRALARVHLSSPVEMAKVADMAGISVSKLKTFNAGVKGSTLGASGPQYVMVPKKHADQLRESLASGEIAAVQSTLVADNTPLNSRVYTVRSGDTLSSIASRLGVSTKDLQQWNKLRGSKLKPGQSLTIGAGSSAQRLANNSDSITYRVRKGDSLSSIAKRHGVNIKDVMRWNSDTANLQPGDKLTLFVKNNNMPDS
Protein: Diamine acetyltransferase 1 (EC 2.3.1.57) (Polyamine N-acetyltransferase 1) (Putrescine acetyltransferase) (Spermidine/spermine N(1)-acetyltransferase 1) (Q4V8U3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- ornithine decarboxylase
- Agmatine ureohydrolase
- Amine oxidase [flavin-containing]
- Spermidine synthase
- Amine oxidase.
- Amine oxidase
- Acyl-CoA thioesterase 9, tandem duplicate 1
Sequence:
MASYILRKAEPKDVSDILRLIKELAKFEEMEDQVILTEKDLLEDGFGDHPFYHCMVAEVAKQHQSADGHVIVGFAMYYFTYDPWIGKLLYLEDFYVMKEYRGFGIGSEILKKLSQTAVRTRCSSMHFIVAEWNTTSIEFYKRRGASDLSHEEGWRLFKIDKQSLLKMTSEE
Protein: Aminomethyltransferase folate-binding domain-containing protein (D6XM32)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
MGFKCLLSSRALLQVTGSVAHEFLQGLFTNDLRQLQPGGSLWGCFLHHTGRVMCDAYLYQSTRTPEGQVTIMIDVHCGVADTLLEHLKEYRMRKKLEIRSAAEELVVVAAATIGNSISSCGDNAGSSPSSSSATYGGDQELSGPQGVDSFDTLAETFTDPRSFALPATLRKMIVPRKGAPPTLDSEKLYKKFLYAAGVGEGPEVFRPSKTLPFEANTDLLRGVSFHKGCYMGQELTHRTHVMLVTRKRTVPLFLQGELFDGKGGEKTPHVEGTLVIGNQKVGEVLTACGNVGLGLLRLNHVDITTRSFPGLSLSDGTTVDARIPEWWDEKELRKVLTKS
Protein: EKC/KEOPS complex subunit GON7 (Low-dye-binding protein 6) (Polarized growth chromatin-associated controller 2) (P46984)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. GON7 likely plays a supporting role to the catalytic subunit KAE1 in the complex. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators.
Subcellular location: Nucleus {ECO:0000269|PubMed:16874308}. Chromosome, telomere {ECO:0000305|PubMed:16874308}.
Interaction partners:
- EKC/KEOPS complex subunit BUD32
- EKC/KEOPS complex subunit CGI121
- EKC/KEOPS complex subunit PCC1
- tRNA N6-adenosine threonylcarbamoyltransferase
- Threonylcarbamoyl-AMP synthase
- tRNA N6-adenosine threonylcarbamoyltransferase, mitochondrial
Sequence:
MKLPVAQYSAPDGVEKSFAPIRDDPRYMTTEGRTTGPSDHVLNAGQIDRDKPSEPERTKDGSQLTYLGQLRTQLTGLQDDINEFLTGRMELAKNKKKAGADEKRIQEEINQLLDGGDGDEDAV
Protein: Selenoprotein K (SelK) (Q9Y6D0)
Organism: Homo sapiens (Human)
Function: Required for Ca(2+) flux in immune cells and plays a role in T-cell proliferation and in T-cell and neutrophil migration (By similarity). Involved in endoplasmic reticulum-associated degradation (ERAD) of soluble glycosylated proteins. Required for palmitoylation and cell surface expression of CD36 and involved in macrophage uptake of low-density lipoprotein and in foam cell formation (By similarity). Together with ZDHHC6, required for palmitoylation of ITPR1 in immune cells, leading to regulate ITPR1 stability and function. Plays a role in protection of cells from ER stress-induced apoptosis. Protects cells from oxidative stress when overexpressed in cardiomyocytes.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16962588, ECO:0000269|PubMed:21220695, ECO:0000269|PubMed:22016385, ECO:0000269|PubMed:25368151}; Single-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:12775843}; Single-pass membrane protein {ECO:0000255}. Note=Probably mainly localized in the ER. {ECO:0000269|PubMed:21220695}.
Interaction partners:
- Selenoprotein S
- Thioredoxin reductase-like selenoprotein T
- Protein adenylyltransferase SelO, mitochondrial
- Selenoprotein N
- Transitional endoplasmic reticulum ATPase
- Selenocysteine insertion sequence-binding protein 2
- Selenoprotein F
- Palmitoyltransferase ZDHHC6
- Selenoprotein H
- Selenoprotein M
Sequence:
MVYISNGQVLDSRSQSPWRLSLITDFFWGIAEFVVLFFKTLLQQDVKKRRSYGNSSDSRYDDGRGPPGNPPRRMGRINHLRGPSPPPMAGGUGR
Protein: Mannosyl-oligosaccharide glucosidase (EC 3.2.1.106) (Processing A-glucosidase I) (Glucosidase I) (P53008)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Cleaves the distal alpha 1,2-linked glucose residue from the Glc(3)Man(9)GlcNAc(2) oligosaccharide precursor highly specifically. Seems to play a role in beta-1,6-glucan synthesis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:8576053}; Single-pass type II membrane protein {ECO:0000269|PubMed:8576053}.
Interaction partners:
- Glucosidase 2 subunit alpha
- Calnexin homolog
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 3
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST6
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit WBP1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3
- Killer toxin-resistance protein 5
- Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST2
Sequence:
MLISKSKMFKTFWILTSIVLLASATVDISKLQEFEEYQKFTNESLLWAPYRSNCYFGMRPRYVHESPLIMGIMWFNSLSQDGLHSLRHFATPQDKLQKYGWEVYDPRIGGKEVFIDEKNNLNLTVYFVKSKNGENWSVRVQGEPLDPKRPSTASVVLYFSQNGGEIDGKSSLAMIGHDGPNDMKFFGYSKELGEYHLTVKDNFGHYFKNPEYETMEVAPGSDCSKTSHLSLQIPDKEVWKARDVFQSLVSDSIRDILEKEETKQRPADLIPSVLTIRNLYNFNPGNFHYIQKTFDLTKKDGFQFDITYNKLGTTQSISTREQVTELITWSLNEINARFDKQFSFGEGPDSIESVEVKRRFALETLSNLLGGIGYFYGNQLIDRETEFDESQFTEIKLLNAKEEGPFELFTSVPSRGFFPRGFYWDEGFHLLQIMEYDFDLAFEILASWFEMIEDDSGWIAREIILGNEARSKVPQEFQVQNPNIANPPTLLLAFSEMLSRAIENIGDFNSDSYHQVMFNSRTAKFMTNNLEANPGLLTEYAKKIYPKLLKHYNWFRKSQTGLIDEYEEILEDEGIWDKIHKNEVYRWVGRTFTHCLPSGMDDYPRAQPPDVAELNVDALAWVGVMTRSMKQIAHVLKLTQDEQRYAQIEQEVVENLDLLHWSENDNCYCDISIDPEDDEIREFVCHEGYVSVLPFALKLIPKNSPKLEKVVALMSDPEKIFSDYGLLSLSRQDDYFGKDENYWRGPIWMNINYLCLDAMRYYYPEVILDVAGEASNAKKLYQSLKINLSNNIYKVWEEQGYCYENYSPIDGHGTGAEHFTGWTALVVNILGRF
Protein: Small ribosomal subunit protein mS41 (Protein fyv4, mitochondrial) (O74972)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in telomere length regulation.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Small ribosomal subunit protein uS9m
- Small ribosomal subunit protein uS19m
- Small ribosomal subunit protein mS33
- Small ribosomal subunit protein bS18m
- Small ribosomal subunit protein uS14m
- Small ribosomal subunit protein uS4m
- Small ribosomal subunit protein uS2m
- Small ribosomal subunit protein uS7m
- Small ribosomal subunit protein mS47
- Small ribosomal subunit protein mS45
Sequence:
MLILKRIFIIRNFIFPFSNCRYASTVPSPRSGISNTNDFFKRIGRDTAEKVNGKFESWDGLFRKSTKTMKKEGIDVRTRKYIASQRNRFKEGFIVKPYPVMVKKNGGERRKRK
Protein: Protein EVI2A (Ecotropic viral integration site 2A protein homolog) (EVI-2A) (P22794)
Organism: Homo sapiens (Human)
Function: May complex with itself or/and other proteins within the membrane, to function as part of a cell-surface receptor.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Protein EVI2B
- Oligodendrocyte-myelin glycoprotein
- Neurofibromin
- E3 ubiquitin-protein ligase RNF135
- Arf-GAP with dual PH domain-containing protein 2
Sequence:
MPTDMEHTGHYLHLAFLMTTVFSLSPGTKANYTRLWANSTSSWDSVIQNKTGRNQNENINTNPITPEVDYKGNSTNMPETSHIVALTSKSEQELYIPSVVSNSPSTVQSIENTSKSHGEIFKKDVCAENNNNMAMLICLIIIAVLFLICTFLFLSTVVLANKVSSLRRSKQVGKRQPRSNGDFLASGLWPAESDTWKRTKQLTGPNLVMQSTGVLTATRERKDEEGTEKLTNKQIG