wanglab/gogpt-training-data huggingface dataset:
Protein: Methyl-CpG-binding domain protein 2 (Demethylase) (DMTase) (Methyl-CpG-binding protein MBD2) (Q9UBB5)
Organism: Homo sapiens (Human)
Function: Binds CpG islands in promoters where the DNA is methylated at position 5 of cytosine within CpG dinucleotides. Binds hemimethylated DNA as well. Recruits histone deacetylases and DNA methyltransferases to chromatin. Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin. Acts as transcriptional repressor and plays a role in gene silencing. Functions as a scaffold protein, targeting GATAD2A and GATAD2B to chromatin to promote repression. May enhance the activation of some unmethylated cAMP-responsive promoters.
Subcellular location: Nucleus {ECO:0000269|PubMed:12183469, ECO:0000269|PubMed:15701600, ECO:0000269|PubMed:20523938, ECO:0000269|PubMed:27732854, ECO:0000269|PubMed:28977666, ECO:0000269|PubMed:33283408, ECO:0000269|PubMed:9774669}. Chromosome {ECO:0000269|PubMed:20523938, ECO:0000269|PubMed:27732854}. Note=Nuclear, in discrete foci (PubMed:12183469). Detected at replication foci in late S phase. Localizes to methylated chromatin (PubMed:16428440). Localizes to sites of DNA damage in a manner partially dependent on ZMYND8 (PubMed:27732854). {ECO:0000269|PubMed:12183469, ECO:0000269|PubMed:16428440, ECO:0000269|PubMed:27732854}.
Interaction partners:
- Transcriptional repressor p66-alpha
- Histone deacetylase 1
- Metastasis-associated protein MTA1
- Histone-binding protein RBBP4
- Transcriptional repressor p66-beta
- DNA
- Histone deacetylase 2
- Metastasis-associated protein MTA2
- Metastasis-associated protein MTA3
- Histone-binding protein RBBP7
Sequence:
MRAHPGGGRCCPEQEEGESAAGGSGAGGDSAIEQGGQGSALAPSPVSGVRREGARGGGRGRGRWKQAGRGGGVCGRGRGRGRGRGRGRGRGRGRGRPPSGGSGLGGDGGGCGGGGSGGGGAPRREPVPFPSGSAGPGPRGPRATESGKRMDCPALPPGWKKEEVIRKSGLSAGKSDVYYFSPSGKKFRSKPQLARYLGNTVDLSSFDFRTGKMMPSKLQKNKQRLRNDPLNQNKGKPDLNTTLPIRQTASIFKQPVTKVTNHPSNKVKSDPQRMNEQPRQLFWEKRLQGLSASDVTEQIIKTMELPKGLQGVGPGSNDETLLSAVASALHTSSAPITGQVSAAVEKNPAVWLNTSQPLCKAFIVTDEDIRKQEERVQQVRKKLEEALMADILSRAADTEEMDIEMDSGDEA
Protein: Enoyl-[acyl-carrier-protein] reductase [NADPH] FabI (ENR) (EC 1.3.1.39) (NADPH-dependent enoyl-ACP reductase) (Q6GI75)
Organism: Staphylococcus aureus (strain MRSA252)
Function: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity).
Interaction partners:
Sequence:
MLNLENKTYVIMGIANKRSIAFGVAKVLDQLGAKLVFTYRKERSRKELEKLLEQLNQPEAHLYQIDVQSDEEVINGFEQIGKDVGNIDGVYHSIAFANMEDLRGRFSETSREGFLLAQDISSYSLTIVAHEAKKLMPEGGSIVATTYLGGEFAVQNYNVMGVAKASLEANVKYLALDLGPDNIRVNAISAGPIRTLSAKGVGGFNTILKEIEERAPLKRNVDQVEVGKTAAYLLSDLSSGVTGENIHVDSGFHAIK
Protein: Sterol regulatory element-binding protein ECM22 (Extracellular mutant protein 22) (Q05958)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Transcription factor involved in sterol uptake and regulation of sterol biosynthesis. Binds to sterol regulatory elements (SRE) with the consensus sequence 5'-TCGTATA-3' present in ERG2 and ERG3 promoters and regulates transcription of ERG2 and ERG3 in response to sterol levels. Seems to be involved in activation of DAN2 and DAN3 cell wall mannoproteins.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227, ECO:0000269|PubMed:14562095}.
Interaction partners:
- Sterol uptake control protein 2
- Transcriptional activator/repressor MOT3
- C-8 sterol isomerase ERG2
- Delta
- Repressor ROX1
Sequence:
MTSDDGNAGQEREKDAELIEVGGKKVSKTSTGKRKFHNKSKTGCDNCKRRRVKCDEGKPFCKKCTNMKLDCVYSPIQPRRRKDSSSSKFASAVHDRVGKKNLSDNAIMLQQQQQQLHHQQEQQFRQQQQVQLQQQLLPHVGTDEQSNSPNSVPPSVSNNMENLLLPHLLASLVNNTSNSTNSSANGAEAHNNITQTAPSSMINNNHPNMALPGNSPLSIPITPSFQSTAMNLSSSLNGLLSPGRLNSVTNGLQQPQLQQQNQQIPQQQGTQSPFSNIPFDQLAQLNKMGLNFNMKSFNTLFPYGAANGMASEFQELFGLGKFATSNNRAIKVSTAEEALANMQQEQEDKNKQFTKNPLDNTKTDAVNSGNNPLNGNENKVTASDILSHNKNLIIDNTGLTISPPHTLSKPSIDQNIASPSTGVSNVTSTKSLLSIPDNRTALGNSPTLKTSPMGDLLSNSEALSPRSSNSHTQQQSSPHSNASSASRLVPELVGLSRKSNLNLIDLKLFHHYCTDVWHTITEAGISGPEVWSTYIPDLAFHFPFLMHTILAFSATHLSRTEAGLDNYVSSHRLEALRLLREAVLEISDDNTDALVASALILILDSLANASSSSPTAWIFHVKGAVTILTAVWPLSETSKFYNLISVDLSDLGEAVINQSNHNNDNDNSNNGDGNNNNTISELVCFDESIADLYPVEIDSPYLITLAYLDKLHREKNQLDFMLRVFSFPALLDRTFLALLMTGDLGAMRIMRSYYTLLRGYTTEIKDKVWFLDSVSQVLPQDVDEYSGGGGMHMMLDFLGGGLPSMTTTNFSAFM
Protein: Apoptosis-resistant E3 ubiquitin protein ligase 1 (EC 2.3.2.26) (Apoptosis-resistant HECT-type E3 ubiquitin transferase 1) (O15033)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase that catalyzes 'Lys-11'- or 'Lys-33'-linked polyubiquitin chains, with some preference for 'Lys-33' linkages. E3 ubiquitin-protein ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Ubiquitinates SEPTIN4, DIABLO/SMAC and HTRA2 in vitro. Modulates pulmonary inflammation by targeting SOCS2 for ubiquitination and subsequent degradation by the proteasome.
Interaction partners:
- Ubiquitin-conjugating enzyme E2 D1
- Polyubiquitin-C
Sequence:
MFYVIGGITVSVVAFFFTIKFLFELAARVVSFLQNEDRERRGDRTIYDYVRGNYLDPRSCKVSWDWKDPYEVGHSMAFRVHLFYKNGQPFPAHRPVGLRVHISHVELAVEIPVTQEVLQEPNSNVVKVAFTVRKAGRYEITVKLGGLNVAYSPYYKIFQPGMVVPSKTKIVCHFSTLVLTCGQPHTLQIVPRDEYDNPTNNSMSLRDEHNYTLSIHELGPQEEESTGVSFEKSVTSNRQTFQVFLRLTLHSRGCFHACISYQNQPINNGEFDIIVLSEDEKNIVERNVSTSGVSIYFEAYLYNATNCSSTPWHLPPMHMTSSQRRPSTAVDEEDEDSPSECHTPEKVKKPKKVYCYVSPKQFSVKEFYLKIIPWRLYTFRVCPGTKFSYLGPDPVHKLLTLVVDDGIQPPVELSCKERNILAATFIRSLHKNIGGSETFQDKVNFFQRELRQVHMKRPHSKVTLKVSRHALLESSLKATRNFSISDWSKNFEVVFQDEEALDWGGPRREWFELICKALFDTTNQLFTRFSDNNQALVHPNPNRPAHLRLKMYEFAGRLVGKCLYESSLGGAYKQLVRARFTRSFLAQIIGLRMHYKYFETDDPEFYKSKVCFILNNDMSEMELVFAEEKYNKSGQLDKVVELMTGGAQTPVTNANKIFYLNLLAQYRLASQVKEEVEHFLKGLNELVPENLLAIFDENELELLMCGTGDISVSDFKAHAVVVGGSWHFREKVMRWFWTVVSSLTQEELARLLQFTTGSSQLPPGGFAALCPSFQIIAAPTHSTLPTAHTCFNQLCLPTYDSYEEVHRMLQLAISEGCEGFGML
Protein: Probable conserved transmembrane protein (I6Y748)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Putative transport protein Rv0205
- Alpha-
- Probable conserved transmembrane protein
Sequence:
MSHDAPARNLRQRVGALPRTRVGAPPAEGVPPRGKYWWLRWAVLAIVAIVLAIEVALGWDQLAKAWVSLYRAKWWWLLAAVAAAGASMHSFAQIQRTLLKSAGVHVKQWRSEAAFYAANSLSTTLPGGPVLSATFLLRQQRIWGASTVVASWQLVMSGVLQAVGLALLGLGGAFFLGAKNNPFSLLFTLGGFVTLLLLAQAVASRPELIEGIGRRVLSWANSVRGRPADAGLPKWRETLMQLESVSLGRRDLGVAFGWSLFNWIADVACLGFAAYAAGDHASVGGLAVAYAAARAVGTIPLMPGGLLVVEAVLVPGLVSSGMPLPSAISAMLIYRLISWLLIAAIGWVVFFFMFRTESTADSDNDRDPPTDPNLRLVIQPQGTPCDDPVETTPQGPAPTPDLRPEGGETPPR
Protein: Protein OPG164 (P68619)
Organism: Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR))
Function: Involved in the intracellular transport and egress of virions to the host cell surface with help of protein OPG056. Participates also in the formation of actin tails at the plasma membrane to allow efficient actin-based motility and thus cell to cell transmission of viral particles. Recruits host intersectin-1/ITSN1 and activates host CDC42 to drive ARP2/3-mediated actin polymerization.
Subcellular location: Host cell membrane {ECO:0000269|PubMed:27670116, ECO:0000269|PubMed:28631604}; Single-pass membrane protein {ECO:0000305}. Note=Found exclusively on the wrapped enveloped virion. Absent in the mature virion (MV) and extracellular enveloped virion (EV).
Interaction partners:
Sequence:
MMLVPLITVTVVAGTILVCYILYICRKKIRTVYNDNKIIMTKLKKIKSSNSSKSSKSTDSESDWEDHCSAMEQNNDVDNISRNEILDDDSFAGSLIWDNESNVMAPSTEHIYDSVAGSTLLINNDRNEQTIYQNTTVVINETETVEVLNEDTKQNPNYSSNPFVNYNKTSICSKSNPFITELNNKFSENNPFRRAHSDDYLNKQEQDHEHDDIESSVVSLV
Protein: Gluconokinase (EC 2.7.1.12) (Q6FM38)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- 6-phosphogluconate dehydrogenase, decarboxylating
- 6-phosphogluconolactonase-like protein
- 6-phosphogluconolactonase-like protein
- 6-phosphogluconolactonase-like protein
- Candida glabrata strain CBS138 chromosome H complete sequence
- Ribose-5-phosphate isomerase
- Ribulose-phosphate 3-epimerase
- Glucose-6-phosphate 1-dehydrogenase
Sequence:
MTNHKLKVIVLAGTAGTGKSTVAARLLKEYSTKYPGIKFVEGDELHPKANIDKMASGNPLNDDDRWGWLKEVALKSAQSAEEGGCGVSVVACSSLKKSYRDLIRSTRPDVEYHFVFLYGSKVEILNRLNSRKGHFMKSNMMESQFKDLQLPEESEANCVVVLLDHKGFDEIEDDVLKYTNTVL
Protein: Aquaporin-9 (AQP-9) (Aquaglyceroporin-9) (Small solute channel 1) (O43315)
Organism: Homo sapiens (Human)
Function: Forms a water channel with a broad specificity. Also permeable glycerol and urea. Mediates passage of a wide variety of small, non-charged solutes including carbamides, polyols, purines, and pyrimidines.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10564231, ECO:0000269|PubMed:9514918}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q96PS8}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q9JJJ3}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q96PS8}. Note=Functions at the hepatocyte basolateral membrane. {ECO:0000250|UniProtKB:Q9JJJ3}.
Interaction partners:
- Glycerol kinase
- Aquaporin-11
- Glycerol kinase 2
- Putative aquaporin-12A
- Myeloid cell nuclear differentiation antigen
- Triggering receptor expressed on myeloid cells 1
- Aquaporin-1
- Lens fiber major intrinsic protein
- Aquaporin-8
- Aquaporin-10
Sequence:
MQPEGAEKGKSFKQRLVLKSSLAKETLSEFLGTFILIVLGCGCVAQAILSRGRFGGVITINVGFSMAVAMAIYVAGGVSGGHINPAVSLAMCLFGRMKWFKLPFYVGAQFLGAFVGAATVFGIYYDGLMSFAGGKLLIVGENATAHIFATYPAPYLSLANAFADQVVATMILLIIVFAIFDSRNLGAPRGLEPIAIGLLIIVIASSLGLNSGCAMNPARDLSPRLFTALAGWGFEVFRAGNNFWWIPVVGPLVGAVIGGLIYVLVIEIHHPEPDSVFKTEQSEDKPEKYELSVIM
Protein: Protein kinase, putative (Q38CK3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MISVLSPSDFEKAKEFRAFLRNLGLSKSLDLFSEQWDELVKQQKEITTNEERMSEQDKEKSQRVSSAGSTPSVTAARVLRVKHRVVSAVGIEDDLWQPVGHEFLSPAFTTGAGISLEAYEMARQNDAVTLVCTNPYFKEPPPSNLPLEHFDLRVWYESGKTGFEEEKELPISVDSIVAGRYQMLQYLDSAAFSRTVRCMDLHEDREVCLKIIRNSKDFFDQSIDEIKLLKLINSSGDTEENCVVKMYDFFYYKEHMCIVTELLRDNLYRFSKYNRDEETELYFTLPRLQATARQVLTGLRFLHSLGLIHSDLKPENILIQSYSRCAVKIIDFGSSCFLTDNLSSYVQSRCYRAPEVILGCKYDSGIDIWSLGAILAELATGNVLFENNSIPQMLASICSVCNELPSKLLHEGRNTHHYVTKFGAFYEYCENMDLIFHYPVQGTPLPELFGYDDPLYVDFVRSCLTLDHRQRPTAEELLKHPFIHNDYGSAYSKPPPLKKQVADTNGIKDTSI
Protein: Trafficking protein particle complex II-specific subunit 130 homolog (AtTRS130) (TRAPP II-specific subunit 130 homolog) (F4K0C4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Specific subunit of the TRAPP II complex, a highly conserved vesicle tethering complex that is required for the proper transport of proteins in post-Golgi trafficking pathways to the growing cell plate in mitotic active cells. Required for the polarized and selective transport of PIN2, but not PIN1, to the plasma membrane. Not required for ER-to-Golgi as well as biosynthetic and endocytic vacuolar transport.
Subcellular location: Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:21689172}. Early endosome {ECO:0000303|PubMed:21689172}.
Interaction partners:
- Trafficking protein particle complex subunit
- Trafficking protein particle complex II-specific subunit 120 homolog
- Trafficking protein particle complex subunit
- Trafficking protein particle complex subunit
- Transport protein particle
- Trafficking protein particle complex subunit 2-like protein
- Trafficking protein particle complex subunit
- SNARE-like superfamily protein
- Tetratricopeptide repeat
- Trafficking protein particle complex subunit-like protein
Sequence:
MANYLAQFQTIKNSCDRLVAAVEDVCDLWPTVKGLFEEHQPLKRAFLTNKTRNPVFVENLPVEFILTTDARLRSRFPQEQYLFWFREPYATIVLVTCEDLDEFKNILKPRLKLIVQNDEREWFIVFVSKAHPSNDQATKNVKKVYAKLEVDFSSKKRERCCKLDVHGPEGNFWEDLELKITECIRNTLDRRAQFYEDEIRKLSEQRFMPIWNFCNFFILKESLAFIFEMAHLHEDALREYDELELCYLETVNMPGKQRDFGGFDGEDDQAVLLKPGSKPLTQIVQDDSFREFEFRQYLFACQSRLLFKLNRPFEVASRGYSFVISFAKALTLHESVLPFCMREVWVITACLALIEATASHHHDGVVAPDIEKEFFRLQGDLYSLSRVKFMRLGYLIGYGTDIEKSPLNSACLSMLPWPKPAVWPSLPQDASSEVLEKEKTILQATSRTKHFGIQRKALPLEPSVLLRVANRRRASLSTGNIPEMFDGRPSFTEGSGLEASPRTPSSLKVQAPPMSRTNSSPGNFESPLDRPMRLAEIFVAAEHALRLTISDHDLLKTLSSIQDFENKYLNLTKGAAENYHRSWWKRHGVVLDGEIAAVCFKHGKYDLAANSYEKVCALYAGEGWQDLLAEVLPNLAQCQKILDDQAGYMSSCVRLLSLDKGLFSSKERQAFQSEVVTLAHSEMKNPVPLDVSSLITFSGNTGPPLQLCDGDPGNLSVTVWSGFPDDITLDSLSLTLVATNNTDEGGQALKSSAATVLNPGRNTITFALPPQKPGSYVLGVVTGQIGRLRFRSHSFSKGGPADSDDFMSYEKPTRPILKVSKPRALVDLAAAVSSALLINEAQWIGIIVRPIAYSLKGAILHIDTGPGLKIEDSYGIEMERYMDADCDTGASKAEVFVEDSPVSSKRDSEVLNLCDGKIVFSDWASNVSSILWVPVRALSEKLARGSSSVTPLKQDILEGMRTVALKLEFGVHHNQIFERTIAAHFTDPFDVTTRVANKCNDGTLVLQVMLHSLVKANLIVLDVWLDLQDGFIHGQNDGRPTSTFFPLVVSPGSRAAVVFSICLDKSMSSEGKDLQLPESILNIKYGIHGDRAAGAHRPVDADHSETDTEGRDLVFKSAIVLQRPVLDPCLTVGFLPLPSDGLRVGKLITMQWRVERLKELKESEAVEQQHDEVLYEVNANSENWMIAGRKRGHVSLSEEQGSRVVISILCVPLVAGYVRPPQLGLPNVEEANVSSNPSGPHLVCVLPPLLSSSYCLPVK
Protein: Interferon-related developmental regulator 1 (LP04564p) (Q9VQI5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Small ribosomal subunit protein uS9
- Small ribosomal subunit protein eS6
- Large ribosomal subunit protein eL20
- Large ribosomal subunit protein uL2
- Large ribosomal subunit protein eL36
- Small ribosomal subunit protein uS2
- Large ribosomal subunit protein uL3
- 60S ribosomal protein L27
- Small ribosomal subunit protein RACK1
- Small ribosomal subunit protein eS12
Sequence:
MPRRNKKSAAGRGRTNDSNSEDESFDNVSVYSHMSEVASSEATDELANERFEEKFEKALEQATEKSAQTRVQALQAICELLMHRYMPDFVEDRKMTLMDFVEKSIRRGKGQEQVWGARLAPLLVLQMGGDEGISKAMNQFLLNTVQDKSVGFDARAKCCTAVGLLSFLGCEDVGELVHLMQSFEAIFAGSYLRGDDKTPVSVTAEAGTFHAEALNAWGLLLTLIPSGDFVSLMTTGQNMFPSIKKFLGLLQSTHLDVRMAAGETIALILESGRAHEEDFLEDDIAELSEAVKQLATDSHKYRAKRDRKAQRATFRDVLRYLEEDISPEISIRFGTESLTLDSWSIHHQYSAMCTVMGPGMTSQLQENEFIRDIFQLGPRPTNTGINGNAKVKPTKLERHLVNAAAFKARSITRGKNRDKRSAVVT
Protein: HL01743p (Lazaro (EC 3.1.3.4)) (Q9VNU2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- O-acyltransferase
- Phosphatidate cytidylyltransferase, photoreceptor-specific
- Sphingosine-1-phosphate lyase
- sphingosine kinase
- sphingosine kinase
- LD18904p
- 3-dehydrosphinganine reductase
- Phospholipase
- Alkaline ceramidase
- Neutral ceramidase
Sequence:
MHTFKRGFFCSDLSIRYPYKDCTITVPMLLLMMLLLPMLFVAVVEIMRICKRFRTRLYFRNLWRAEATFSFGFIATYLTTELAKHAVGRLRPHFFHGCQPRLDDGSSCSDLQNAELYVEQFHCTNNNLSTRQIRELHVSFPSAHSSLSFYSMVLLALYVHGVWRGRGGVRVLRHVLQFLLLMAALCVSLSRVADYWHHWSDVLAGALLGVTYAAITAAYVGNLLRRQTSSTGRIPPSLNYSHHLHHQLMADNNNSTASAKVHFLAAAASASMTTTTPLDDIQDSDVEDSRDCRDSEDSHDSQDSHAENEDDNEEVYKSQMSRPVTPPTDLTHVV
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (F4IVM7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MLIPNKKLREMNRRQQVKRRVGKYEVGRTIGEGTFAKVKFARNSETGEPVALKILDKEKVLKHKMAEQIRREIATMKLIKHPNVVQLYEVMASKTKIFIILEYVTGGELFDKIVNDGRMKEDEARRYFQQLIHAVDYCHSRGVYHRDLKPENLLLDSYGNLKISDFGLSALSQQVRDDGLLHTSCGTPNYVAPEVLNDRGYDGATADMWSCGVVLYVLLAGYLPFDDSNLMNLYKKISSGEFNCPPWLSLGAMKLITRILDPNPMTRVTPQEVFEDEWFKKDYKPPVFEERDDSNMDDIDAVFKDSEEHLVTEKREEQPAAINAFEIISMSRGLNLENLFDPEQEFKRETRITLRGGANEIIEKIEEAAKPLGFDVQKKNYKMRLENVKAGRKGNLNVATEIFQVAPSLHMVQVSKSKGDTLEFHKFYKKLSNSLEQVVWTNNEVKKETAK
Protein: GPI-anchor transamidase (GPI transamidase) (EC 3.-.-.-) (GPI8 homolog) (hGPI8) (Phosphatidylinositol-glycan biosynthesis class K protein) (PIG-K) (Q92643)
Organism: Homo sapiens (Human)
Function: Mediates GPI anchoring in the endoplasmic reticulum, by replacing a protein's C-terminal GPI attachment signal peptide with a pre-assembled GPI. During this transamidation reaction, the GPI transamidase forms a carbonyl intermediate with the substrate protein.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11483512}; Single-pass type I membrane protein {ECO:0000269|PubMed:11483512}.
Interaction partners:
- GPI-anchor transamidase component PIGU
- GPI-anchor transamidase component PIGT
- GPI-anchor transamidase component PIGS
- GPI-anchor transamidase component GPAA1
- GPI ethanolamine phosphate transferase 3, catalytic subunit
- GPI inositol-deacylase
- GPI ethanolamine phosphate transferase, stabilizing subunit
- GPI ethanolamine phosphate transferase 2, catalytic subunit
- N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
- GPI alpha-1,2-mannosyltransferase 3
Sequence:
MAVTDSLSRAATVLATVLLLSFGSVAASHIEDQAEQFFRSGHTNNWAVLVCTSRFWFNYRHVANTLSVYRSVKRLGIPDSHIVLMLADDMACNPRNPKPATVFSHKNMELNVYGDDVEVDYRSYEVTVENFLRVLTGRIPPSTPRSKRLLSDDRSNILIYMTGHGGNGFLKFQDSEEITNIELADAFEQMWQKRRYNELLFIIDTCQGASMYERFYSPNIMALASSQVGEDSLSHQPDPAIGVHLMDRYTFYVLEFLEEINPASQTNMNDLFQVCPKSLCVSTPGHRTDLFQRDPKNVLITDFFGSVRKVEITTETIKLQQDSEIMESSYKEDQMDEKLMEPLKYAEQLPVAQIIHQKPKLKDWHPPGGFILGLWALIIMVFFKTYGIKHMKFIF
Protein: Sulfotransferase 1C4 (ST1C4) (EC 2.8.2.1) (A0A2K5X3B6)
Organism: Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of phenolic compounds and estrogen (E2). Can also sulfonate estrogenic compounds, however, the dietary flavonoids (phytoestrogen) and environmental estrogens, like bisphenol A are better substrates than 17beta-estradiol (E2) (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:31100221}.
Interaction partners:
Sequence:
TALHKMEDFTFDGTKRLSVNYVKGILQPTVTCDIWDEIWNFQAKPDDLLISTYPKAGTTWTQEIVELIQNEGDVEKSKRAPTHQRFPFLEWKIPSLGSGLEQAQAMPSPRILKTHLPFHLLPPSFLEKNCKIIYVARNPKDNMVSYYHFQRMNKALPDPGTWEEYFETFLAGKVCWGSWHEHVKGWWEAKDKHRILYLFYEDMKKNPKHEVQKLTEFIEKKLDDKVLDKIVHYTSFDVMKQNSMANYSSIPAEIMDHSISPFMRKGAVGDWKKHFTVAQNERFDEDYKKKMADTRLTFHFQF
Protein: Gag protein (Q71B31)
Organism: Human immunodeficiency virus type 1 (HIV-1)
Subcellular location: Virion {ECO:0000256|ARBA:ARBA00004328}.
Interaction partners:
Sequence:
PIVQNIQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRVHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTNNPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEPFRDYVDRFYKTLRAEQASQEVKNWMTETLLVQNANPDCKTILKALGPAATLEEMMTACQGVGGPGHKARVL
Protein: Rho GTPase activating protein 19 (R4GNI4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MATEAQSEGEVPARESGRSDAICSFVICNDSSLREKGVIFGSPLTEEGIAQIYQLIEYLHKNLRVEGLFRVPGNSVRQQILRDALNNGTDIDLESGEFHSNDVATLLKMFLGELPEPLLTHKHFNAHLKIADLMQFDDKGNKTNIPDKDRQIEALQLLFLILPPPNRNLLKLLLDLLYQTAKKQDKNKMSAYNLALM
Protein: Collectrin (Transmembrane protein 27) (Q9HBJ8)
Organism: Homo sapiens (Human)
Function: Plays an important role in amino acid transport by acting as binding partner of amino acid transporters SLC6A18 and SLC6A19, regulating their trafficking on the cell surface and their amino acid transporter activity (By similarity). May also play a role in trafficking of amino acid transporters SLC3A1 and SLC7A9 to the renal cortical cell membrane (By similarity). Regulator of SNARE complex function. Stimulator of beta cell replication.
Subcellular location: Cell membrane {ECO:0000269|PubMed:22628310}; Single-pass type I membrane protein {ECO:0000255}. Note=Localizes to the brush border membranes of cells in the proximal tubules of kidney (By similarity). Colocalizes with SLC6A19 in the early proximal S1 tubule (By similarity). {ECO:0000250|UniProtKB:Q9ESG4}.
Interaction partners:
- Sodium-dependent neutral amino acid transporter B
- Insulin
- Angiotensin-converting enzyme
- Amino acid transporter heavy chain SLC3A1
Sequence:
MLWLLFFLVTAIHAELCQPGAENAFKVRLSIRTALGDKAYAWDTNEEYLFKAMVAFSMRKVPNREATEISHVLLCNVTQRVSFWFVVTDPSKNHTLPAVEVQSAIRMNKNRINNAFFLNDQTLEFLKIPSTLAPPMDPSVPIWIIIFGVIFCIIIVAIALLILSGIWQRRRKNKEPSEVDDAEDKCENMITIENGIPSDPLDMKGGHINDAFMTEDERLTPL
Protein: Octanoyl-[GcvH]:protein N-octanoyltransferase (EC 2.3.1.204) (Octanoyl-[GcvH]:E2 amidotransferase) (P39648)
Organism: Bacillus subtilis (strain 168)
Function: Catalyzes the amidotransfer (transamidation) of the octanoyl moiety from octanoyl-GcvH to the lipoyl domain of the E2 subunit of lipoate-dependent enzymes.
Interaction partners:
- Lipoate-protein ligase LplJ
- Octanoyltransferase LipM
- Lipoyl synthase
- Glycine cleavage system H protein
- HTH-type transcriptional regulator CysL
- Lipoprotein LipO
- Protein LplB
- Uncharacterized transporter YwfM
- Pyruvate dehydrogenase inhibitor
- Carboxylesterase
Sequence:
MANQPIDLLMQPKWRVIDQSSLGPLFDAKQSFAMDDTLCMSVGKGVSPATARSWVHHDTIVLGIQDTRLPFLQDGISLLESEGYRVIVRNSGGLAVVLDDGVLNISLIFEDEKKGIDIDKGYEAMVELMRRMLRPYNAKIEAYEIEGSYCPGSYDLSINGKKFAGISQRRVRGGVAVQIYLCADKSGSERADLIRRFYQAALKDKQNDKKGVYPEIRPETMASLSELLQKDISVQDLMFALLTELKALSTHLYSAGLSIDEEMEFEKNLVRMAERNAKVFG
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q387G5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- N
Sequence:
MNTHAAAVTVGSVLFQCAESRVYECDFYSHPAVCKYRLPKPYRHPTLDKRLREQRSVREARALVRCQKQGIAVPAVYAIDRESCAIVMERIIGMSVRDVLNEAQRPLEGAVSPVAARLLEGMGEVVGLLHNAHIIHGDLTTSNFMYRTATVAEGKADSAACGAAPRDRLVVLDFGLVMDKNSAEERAVDLYVLERAIKSSHPSLEGVASAFILNGYRRTADPHQVEATITRLGAVRARGRKRSMVG
Protein: Nuclear pore complex-interacting protein family member B4 (C9JG80)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MVKLSIVLTPQFLSHDQGQLTKELQQHVKSVTCPCEYLRKVINTLADHHHRGTDFGGSPWLHVIIAFPTSYKVVITLWIVYLWVSLLKTIFWSRNGHDGSTDVQQRAWRSNRRRQEGLRSICMHTKKRVSSFRGNKIVLKDVITLRRHVETKVRAKIRKRKVTTKINHHDKINGKRKTARKQKMFQRAQELRRRAEDYHKCKIPPSARKALCNWVRMAAAEHRHSSGLPYWPYLTAETLKNRMGHQPPPPTQQHSITDNSLSLKTPPECLLTPLPPSADDNLKTPPECVLTPLPPSADDNLKTPPECVLTPLPPSADDNLKTPPECLLTPLPPSADDKLKTPPECLLTPLPPSALPSAPPSADDNLKTRAECLLHPLPPSADDNLKTPSERQLTPLPPSAPPSADDNIKTPAERLRGPLPPSADDNLKTPSERQLTPLPPSAPPSADDNIKTPAERLRGPLPPSADDNLKTPSERQLTPLPPSAPPSADDNIKTPAERLRGPLPPSADDNLKTPSERQLTPLPPSAPPSADDNIKTPAERLRGPLPPSADDNLKTPSERQLTPLPPSAPPSADDNIKTPAERLRGPLPPSADDNLKTPSERQLTPLPPSAPPSADDNIKTPAFHPQRMIISRHLPSVSSLPFHPQLHPQQMIISRYLLSVCGFRFHHQPMIISRHLPSVSSLPFHPQLHPQQMIISRHLPSVCGGRFHPQRMIISRHLPSVSSLPFHPQLHPQQMIISRHLPSVCGGRFHPQRMIISRHLPSVSSLPFHPQLHPQQMIISRHLPSVCGGRFHPQRMIISRHLPSVSSLPFHPQLHPQQMIISRHLPSVCGGRFHPQRMIISRHLPSVSSLPFHPQLHPQQMIISRHLPSVCGERLRGPLPPSADDNLKTPSERQLTPLPPSAPPSADDNIKTPAERLRGPLPPSADDNLKTPSERQLTPLPPSAPPSADDNIKTPAERLRGPLPPSADDNLKTPSERQLTPLPPSAPPSADDNIKTPAERLRGPLPPSADDNLKTPPLATQEAEAEKPRKPKRQRAAEMEPPPEPKRRRVGDVEPSRKPKRRRAADVEPSSPEPKRRRVGDVEPSRKPKRRRAADVEPSSPEPKRRRVGDVEPSRKPKRRRAADVEPSLPEPKRRRLS
Protein: Kinesin-like protein (Q385C9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Kinesin-like protein, putative
- Kinesin-like protein
- Kinesin-like protein
- Kinesin-like protein
- Kinesin-like protein
- Kinesin, putative
- Kinesin-like protein
- Kinesin, putative
- Kinesin-like protein
- Kinesin-like protein
Sequence:
MGGEDNVARRGSCSGAVVEAKQPSDDGTIRVVVRVRPLSTVEHANPSVRNIVQCLKDGIVVNGAPSKMSSRYFGAPHAKPRPRQFNVDQVFHHYSSQFEVYEACRHVIAGAFEGVNGSVLAYGSTGSGKTHTMFGGQMSAAGVIYQAVQDILETKSELEENEKTVTTRCSFMEVYNEKVYDLLAQTSGQGKRKELNVQELTHSNDTSCYGSFINGRCGVNPESLAVRGLTYCTPETADDFARCVERGHINRFVASTDANAHSSRSHAIFTVEIEVKDTVNASLGTVGRIRFCDLAGSERAAGSSNRGDRLREGGNINRSLLALSAVVQELVQRREHPERTHYIPYRGSKLTRLLQDSIGGNCRTLMLFCISPSSMNYEETINTMLFAMQAKKIRVTAKRHEFAVDSKVVAANQEALIEELRAELALARDELLQLRGANANNANGAARTSPRAVSPPQAKDLEVPTLSLSAQRTERDWMQLPLEATGRASMRSSTRTPKVVEAMELSADLQKKTKSLSATKELLYREMREAEEAHSELNMRLRQQKWKLVRFLSAKQKGSGKGVDGELSTSVGVAGQQRAIKEMEVELTAHGGEIKRLREKMDATDKELDKVRQELLREKQHPFLELLLDNVKLRQNCTEAECLAAHYHQEYRAVMSHEEEFSQALSKCVQAIKSMLPLTTPNSSVWEEAQLALMYANLPSIPTADIIHVVQKSMRSGRASPMASAESRFRRSSTQGIEARLQYQVSNGPDSRSLVVHSSPKKATGAYSNRSVAGTNTPLSGNSRSTIAAAKCQRTPKAMTVPPRPVTRPSTRQPAGATFKKPPCPKGAIKVGHRDPANLSTVNGKKNTIIGSPCKEMTLASSRPHAARTDAGKAASPTFSRCATRTHVKFSEDVVPFTRSLTFNGISRTKARQSNGTPSLRERHNNFTPPRRVRRTNKDYGTGEEDIHPRRVLNDGLEERFKKLLDEVKLWHSDKASTDSGLNVST