wanglab/gogpt-training-data huggingface dataset:
Protein: Heat shock transcription factor (HSTF) (Heat shock factor protein) (HSF) (P10961)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: DNA-binding transcription factor that specifically binds heat shock promoter elements (HSE) and activates transcription.
Subcellular location: Nucleus {ECO:0000305|PubMed:3044613}.
Interaction partners:
- Heat shock protein SSA1
- ATP-dependent molecular chaperone HSC82
- ATP-dependent molecular chaperone HSP82
- Heat shock protein SSA2
- Zinc finger protein MSN2
- Zinc finger protein MSN4
- Heat shock protein SSA3
- Heat shock protein SSA4
- AP-1-like transcription factor YAP1
- Heat shock protein 104
Sequence:
MNNAANTGTTNESNVSDAPRIEPLPSLNDDDIEKILQPNDIFTTDRTDASTTSSTAIEDIINPSLDPQSAASPVPSSSFFHDSRKPSTSTHLVRRGTPLGIYQTNLYGHNSRENTNPNSTLLSSKLLAHPPVPYGQNPDLLQHAVYRAQPSSGTTNAQPRQTTRRYQSHKSRPAFVNKLWSMLNDDSNTKLIQWAEDGKSFIVTNREEFVHQILPKYFKHSNFASFVRQLNMYGWHKVQDVKSGSIQSSSDDKWQFENENFIRGREDLLEKIIRQKGSSNNHNSPSGNGNPANGSNIPLDNAAGSNNSNNNISSSNSFFNNGHLLQGKTLRLMNEANLGDKNDVTAILGELEQIKYNQIAISKDLLRINKDNELLWQENMMARERHRTQQQALEKMFRFLTSIVPHLDPKMIMDGLGDPKVNNEKLNSANNIGLNRDNTGTIDELKSNDSFINDDRNSFTNATTNARNNMSPNNDDNSIDTASTNTTNRKKNIDENIKNNNDIINDIIFNTNLANNLSNYNSNNNAGSPIRPYKQRYLLKNRANSSTSSENPSLTPFDIESNNDRKISEIPFDDEEEEETDFRPFTSRDPNNQTSENTFDPNRFTMLSDDDLKKDSHTNDNKHNESDLFWDNVHRNIDEQDARLQNLENMVHILSPGYPNKSFNNKTSSTNTNSNMESAVNVNSPGFNLQDYLTGESNSPNSVHSVPSNGSGSTPLPMPNDNDTEHASTSVNQGENGSGLTPFLTVDDHTLNDNNTSEGSTRVSPDIKFSATENTKVSDNLPSFNDHSYSTQADTAPENAKKRFVEEIPEPAIVEIQDPTEYNDHRLPKRAKK
Protein: Coiled-coil domain-containing protein 172 (TEKT2-binding protein 2) (Q810N9)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24394471}. Cell projection, cilium {ECO:0000250|UniProtKB:Q6AXT4}. Note=In caput spermatozoa, localized in the middle piece, predominantly concentrated at the mitochondrial sheath of the flagella and to a lesser extent with outer dense fibers (ODF) (By similarity). Colocalized with TEKT2 at the perinuclear region (PubMed:24394471). {ECO:0000250|UniProtKB:Q6AXT4, ECO:0000269|PubMed:24394471}.
Interaction partners:
Sequence:
MSLESLFQHIIFSEHQAEESRRVMREVRSEITRCRGKIKKATEDLSEEKIKLESKVQQLSEKSFLLELLKTHENALERQLSEIISERDTLLQACEAIKNKTTEEEERFIKEITDFNDNYEITKKRDTLMKENIEMEMADLDSQADVLRREMKSVERNRGQLWELQKLKNELLQELFTLQKKLKVLKDEETEAICITKQLEAEKTKVRDKPQHDPECVRLKRELDLYKAEDMESVYRALQAEVDLLELALAPKDPQDSNSLSHEPPHT
Protein: K-box region and MADS-box transcription factor family protein (F4KGH9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- COMPASS-like H3K4 histone methylase component WDR5A
- Inactive protein FRIGIDA
- SWR1 complex subunit 6
- Histone deacetylase 6
- Chromatin-remodeling ATPase INO80
- Cyclic dof factor 5
- Protein PHOTOPERIOD-INDEPENDENT EARLY FLOWERING 1
- SWR1-complex protein 4
- Protein TWIN SISTER of FT
- WD-40 repeat-containing protein MSI4
Sequence:
MGRRKVEIKRIENKSSRQVTFCKRRNGLMEKARQLSILCESSVALIIISATGRLYSFSSGDRGIEDQCTLFTFEINLGPLSIFLLNSNETPVDFMAKILSRYELEQADDLKTLDLEEKTLNYLSHKELLETIQCKIEEAKSDNVSIDCLKSLEEQLKTALSVTRARKTELMMELVKTHQEKEKLLREENQSLTNQLIKMGKMKKSVEAEDARAMSPESSSDNKPPETLLLLK
Protein: Phospholemman (FXYD domain-containing ion transport regulator 1) (Sodium/potassium-transporting ATPase subunit FXYD1) (I3LMB3)
Organism: Sus scrofa (Pig)
Function: Associates with and regulates the activity of the sodium/potassium-transporting ATPase (NKA) which transports Na(+) out of the cell and K(+) into the cell. Inhibits NKA activity in its unphosphorylated state and stimulates activity when phosphorylated. Reduces glutathionylation of the NKA beta-1 subunit ATP1B1, thus reversing glutathionylation-mediated inhibition of ATP1B1. Contributes to female sexual development by maintaining the excitability of neurons which secrete gonadotropin-releasing hormone.
Subcellular location: Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P56513}; Single-pass type I membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:O08589}; Single-pass type I membrane protein {ECO:0000255}. Membrane, caveola {ECO:0000250|UniProtKB:O08589}. Cell membrane, sarcolemma, T-tubule {ECO:0000250|UniProtKB:O08589}. Note=Detected in the apical cell membrane in brain. In myocytes, localizes to sarcolemma, t-tubules and intercalated disks. {ECO:0000250|UniProtKB:O08589}.
Interaction partners:
- Sodium/potassium-transporting ATPase subunit alpha-1
- Sodium/potassium-transporting ATPase subunit beta-1
Sequence:
MASLSHILVLWVGILTVVNAEAPQEHDPFTYDYQSLRIGGLIIAGILFILGILIVLSRRCRCKFNQQQSLGKMRSPHLAAQFSSESC
Protein: Protein transport protein Sec61 subunit gamma-3 (Q9SMP2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Necessary for protein translocation in the endoplasmic reticulum.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- F9K20.24 protein
- SecY protein transport family protein
- AT2G34250 protein
- Preprotein translocase Sec, Sec61-beta subunit protein
- Protein transport protein Sec61 subunit beta
- Protein transport protein Sec61 subunit beta
- Preprotein translocase subunit SCY1, chloroplastic
- Translocation protein SEC62
- DnaJ protein ERDJ2A
- Protein transport protein Sec61 subunit gamma-1
Sequence:
MEAIDSAIDPLRDFAKSSVRLVQRCHKPDRKEFTKVAVRTAIGFVVMGFVGFFVKLVFIPINNIIVGSS
Protein: Cell shape-determining protein MreC (Cell shape protein MreC) (Rod shape-determining protein MreC) (Q70AN6)
Organism: Cereibacter sphaeroides (Rhodobacter sphaeroides)
Function: Involved in formation and maintenance of cell shape.
Subcellular location: Cell inner membrane {ECO:0000305|PubMed:16484180}; Single-pass membrane protein {ECO:0000305|PubMed:16484180}. Note=Colocalizes with penicillin-binding protein PBP2 throughout the cell cycle. In newly formed and elongating cells, the foci form bands across the cell, which are predominately located at or near midcell. In cells undergoing septation, the foci are not observed at the site of septation but are positioned close to the midcell of the nascent or forming daughter cells.
Interaction partners:
Sequence:
MARDRTRPEDFTRPLRRILVGGLVLLLLGIFLIWRIDSPRVEQFRAALIDRVVPSFEWLMTPMTKVAGMVENFQSYTRIYEQNQELRRELQQMKAWKEAALQLEQKNARLLDLNQVRLDPKLTHVTGVVLADSGSPFRQSVLLNVGARDGIRDGWATMDGIGLVGRISGVGRTTSRVILLTDTSSRIPVTVQPSGQRALLTGDNSPSPPLEFLDKPDLVRPGDRVVTSGDGGVFPADLLVGQVAQGPDRRLRVRLAADYGRLEFLRVLRSHELEPISDPGKLVAEPPAPPAPAAVEGADG
Protein: Epididymal secretory glutathione peroxidase (EC 1.11.1.9) (Epididymis-specific glutathione peroxidase-like protein) (EGLP) (Glutathione peroxidase 5) (GPx-5) (GSHPx-5) (Major androgen-regulated protein) (arMEP24) (P21765)
Organism: Mus musculus (Mouse)
Function: Protects cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione. May constitute a glutathione peroxidase-like protective system against peroxide damage in sperm membrane lipids.
Subcellular location: Secreted.
Interaction partners:
- Glutathione reductase, mitochondrial
- Peroxisome proliferator-activated receptor gamma coactivator 1-alpha
- Glutathione synthetase
- Polyunsaturated fatty acid lipoxygenase ALOX15
- Polyunsaturated fatty acid 5-lipoxygenase
- Polyunsaturated fatty acid lipoxygenase ALOX8
- Glutathione-specific gamma-glutamylcyclotransferase 1
- Putative glutathione-specific gamma-glutamylcyclotransferase 2
- Thioredoxin
- Heme oxygenase 1
Sequence:
MVTELRVFYLVPLLLASYVQTTPRPEKMKMDCYKDVKGTIYDYEALSLNGKEHIPFKQYAGKHVLFVNVATYCGLTIQYPELNALQEDLKPFGLVILGFPCNQFGKQEPGDNLEILPGLKYVRPGKGFLPNFQLFAKGDVNGENEQKIFTFLKRSCPHPSETVVMSKHTFWEPIKVHDIRWNFEKFLVGPDGIPVMRWFHQAPVSTVKSDIMAYLSHFKTI
Protein: Protein croquemort (d-CD36) (Q27367)
Organism: Drosophila melanogaster (Fruit fly)
Function: Macrophage receptor for apoptotic cells.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- FI01909p
- Protein draper
Sequence:
MCCKCCGETQRKVWVFGLGSVFLLLGILIVVFWPGIADNLVEDGLTLKPGTDAYESWLEAPIPIYLSFYMFNWTNPEDIRNPDIKPNFVEMGPYTFLEKHKKENYTFYDNATVAYYERRTWFFDPERSNGTLDDMVTAAHAITATVADEMRDQRKIVKKIINFMLNHEGGKLYVTKPVGEWIFEGYQDNITDFLNLFNTTKIDIPYKRFGWLADRNESLTYDGLFTIHTGTDDISNLGRLTHWNGKSETGFYEMPCGIVNGTTGDMFPPKMNVNDEITIFATDACRFMNLRPRGTYENHGLTATKWVGTEETLDSGENYPNQACFCDEARFDECPKTGVVECKACRDKAPIYSSFPHFYLADQSYVDAVSGMKPEKEKHEFFLAVEPITGVPVQVHGRIQINMMIEPDDDFDIYRGVQKVLMPMFWFDQYAELSSELASKAKLAINLSSYGIIFGYSMIAFASVFLITGITLTVTKKWVRRTPEDEDILTN
Protein: Nucleus export protein BRR6 (Bad response to refrigeration protein 6) (P53062)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for mRNA nuclear export. Involved in the nuclear pore complex (NPC) distribution and nuclear envelope morphology.
Subcellular location: Nucleus membrane {ECO:0000269|PubMed:11483521, ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:11483521, ECO:0000269|PubMed:14562095}.
Interaction partners:
- Nuclear membrane organization protein APQ12
- Nucleoporin POM34
- Nucleus export protein BRL1
- Nucleoporin NUP188
- Nucleoporin POM152
- Nucleoporin NDC1
- Nucleoporin NUP133
Sequence:
MELRSFSRQPDGILANPRLGREEVLEGEHPQDARLARQSIWLSPSLIAEYIQLFFNFIIGTIGLSLAIKFILMIRNDVNLKLEHNVREELDKIATCKSRYFENQCEPHMRVPALEVRCNEWSKCMNKEIVSGSDYQWAKAWARTLAEVINAFFEAFSIRSFLFILISIIGIIFVTNTSFGSYRVYLNNKDTKSVRHA
Protein: Glucosidase 2 subunit beta (Glucosidase II subunit beta) (Protein PRIORITY IN SWEET LIFE 4) (Q9FM96)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Regulatory subunit of glucosidase II (By similarity). Essential for stable accumulation of the receptor EFR that determines the specific perception of bacterial elongation factor Tu (EF-Tu), a potent elicitor of the defense response to pathogen-associated molecular patterns (PAMPs). Required for sustained activation of EFR-mediated signaling, but not receptor FLS2-mediated signaling elicited by the bacterial flagellin flg22.
Subcellular location: Endoplasmic reticulum {ECO:0000255|PROSITE-ProRule:PRU10138}.
Interaction partners:
- Probable glucan 1,3-alpha-glucosidase
- Heteroglycan glucosidase 1
- alpha-D-xyloside xylohydrolase
- Alpha-xylosidase 1
- Jacalin-related lectin 5
- Nuclear pore complex protein NUP62
- Putative alpha-xylosidase 2
- Myrosinase-binding protein 2
- Jacalin-related lectin 34
- Jacalin-related lectin 33
Sequence:
MRVVVISSFVSVSLQLSFLLLLASAIRSSSSPPNDPFLGISPQDEKYYKSSSEIKCKDGSKKFTKAQLNDDFCDCSDGTDEPGTSACPTGKFYCRNAGHSPVILFSSRVNDGICDCCDGSDEYDGHVSCQNTCWEAGKAARENLKKKIETYNQGLVIRRQEIEQAKVGLEKDAAELKKLKSEQKILKGLVDQLKDRKEQIEKVEEKERLQKEKEEKEKKEAELAAQQGKGDAEEKTDDSEKVEESSHDEGTPAVSQHDETTHHDEIGNYKDYPSDEEPAAEGEPTSILDEATHTNPADEHVVERKEESTSSEDSSSPTDESQNDGSAEKEESDEVKKVEDFVTEKKEELSKEELGRLVASRWTGEKSDKPTEADDIPKADDQENHEHTPITAHEADEDDGFVSDGDEDTSDDGKYSDHEPEDDSYEEEYRHDSSSSYKSDADDDVDFSETTSNPTWLEKIQKTVKNILLAVNLFQTTPVDKSEADRVRKEYDESSSKLNKIQSRISSLEKKLKQDFGPEKEFYSFHGRCFESKQGKYTYKVCAYKEATQEEGYSKTRLGEWDKFENSYQFMSYTNGEKCWNGPDRSLKVKLRCGLKNELMDVDEPSRCEYAAILSTPARCLEDKLKELQQKLEKLMNQDKPQNHDEL
Protein: LEK1 (Q155P7)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MSWALEEWKEGLPSRALQKIQELEGQLEKLKKEKQQRQFQLDSLEAALQKQKQKVEDGKTEGADLKRENQRLMEICEHLEKSRQKLSHELQVKESQVNLQESQLSSCKKQIEKLEQELKRCKSEFERSQQVAQSADVSLNPCSTPQKLFATPLTPSSTYEDLKEKYNKEVEERKRLEEEVKALHAKKVSLPVSQATMNHRDIARHQASSSVFPWQQENTPSRLSSDALKTPLRRDGSAAHFLGEEVSPNKSSMKTGRGDCSSLPGEPHSAQLLHQAKAQNQDLKSKMTELELRLQGQEKEMRSQVNKCQDLQLQLEKTKVELIEKERILNKTRDEVVRSTAQYDQAAAKCTTLEQKLKTLTEELSCHRQNAESAKRSLEQRIKEKEKELQEELSRQHQSFQALDSEYTQMKTRLTQELQQVKHLHSTLQLELEKVTSVKQQLERNLEEIRLKLSRAEQALQASQVAENELRRSSEEMKKENSLIRSQSEQRTREVCHLEEELGKVKVSLSKSQNFAEEMKAKNTSQEIMLRDLQEKLNQQENSLTLEKLKLALADLERQRNCSQDLLKKREHHIDQLNNKLNKIEKEFETLLSALELKKKECEELKEEKNQISFWKIDSEKLINQIESEKEILLGKINHLETSLKTQQVSPDSNERIRTLEMERENFTVEIKNLQSMLDSKMVEIKTQKQAYLELQQKSESSDQKHQKEIENMCLKANKLTGQVESLECKLQLLSSEVVTKDQQYQDLRMEYETLRDLLKSRGSSLVTNEDNQRSSEDNQRSSEDNQRGSLAFEQQPAVSDSFANVMGRKGSINSERSDCSVDGGRSPEHIAILQNRVTSLESSLESQNQMNSDLQMRCEELLQIKGEVEENLSKAEQIHQNFVAETNQCISKLQEDAAVHQNIVAETLATLESKEKELQLLKEKLEAQQTEVQKLNKNNCLLEGTLKELQLLSDTLSSEKKEMNSIISLSKKNIEELTQANEALKEVNEALEQEKMNLLQKHEKITSCIAEQERSIAELSDQYKQERLQLLQRCEETEAVLEDLRGNYKTAQENNAKLECMLSECTALCENRKNELEQLKETFAKEQQEFLTKLAFAEEQNRKLMLELEIEQQTVRSEITNTNKHSMSATDGLRQECLTLNEEQNEQQNEVSNLTHENEQLMELTQTKHDSYLAVEPVENSVKATEDEIGKSSSQYQMDIDTKDISLDSYKAQLVHLEALVRILEVQLDQSEEENKKLHLELQTIREELETKSSQDPQSQARTGLKDCDTAEEKYVSMLQELSASQNENAHLQCSLQTAVNKLNELGKMCDVLRVEKLQLESELNDSRTECITATSQMTAEVEKLVSEMKMLNHESALSQNELMKDTSGGEFHDKANHSSVFLTPLDSSNFCEQMTLSSKEVRVHFAELQEKFSCLQSEHKILHDQHCEVSSKMSALRSYVDTLKAENSALSMSLRTLQGDLVKEGEPAAEGGHGLPLSFCGADSPSLTNFGETSFYKDVLEQTGDTCHLSLEGNASANSCDLDEEFSSSLEEETLTEKESPPAPGRTVEGLEVLCQVYLQSLKNLEEKTESQRIMKNKEIEELEQLLSSERKELSCLRKQYLSEKEQWQQKLTSVTLEMESKLAEEKQQTKTLSLELEVARLQLQELDLSSRSLLGTDLESVVRCQNDNYDIKESEVYISETTEKTPKQDTDQTCDKDIQQDLGLETSVTESETTRLTGEGCEEQPPKTNCEAPAEDKTQDCSECISELCSSSNVLVPMDVLEDQGSIQNLQLQKDTLNENLRLLPEVEDWDKKVESLLNEIMEADSKLSLQEVQLKMKIATCIQLEKIVKDLRKEKADLSEKLESLPCNQEVCLRVERSEEDLGFNLDMGANELLSKSTKDNATNTEDNYKEKFLDMERELTRIKSEKANIEHHILSVETNLEVVQAEKLCLERDTESKQKVIIDLKEELFTVISERNRLREELDNVSKESKALDQMSKKMKEKIEELESHQRESLRHIGAVESEVKDKADLIQTLSFNVGELTKDKAHLQEQLQNLQNDSQELSLAIGELEIQIGQLNKEKESLVKESQNFQIKLTESECEKQTISKALEVALKEKGEFAVQLSSAQEEVHQLRRGIEKLSVRIEADEKKHLSAVAKLKESQRESDSLKDTVETLERELERSEENQELAILDSENLKAEVETLKAQKDEMTKSLRIFELDLVTVRTERENLAKQLQEKQSRVSELDERCSSLRRLLEEKEQARVQMEEDSKSAMLMLQMQLKELREEVAALCNDQETLKAQEQSLDQPGEEVHHLKSSIRKLKVHIDADEKKHQNILEQLKESKHHADLLKDRVENLEQELILSEKNMIFQAEKSKAEIQTLKSEIQRMAQNLQDLQLELISTRSENENLIKELKKEQERVSDLETINPSIENLLKDKEQEKVQMKEEAKITVEMLQTQLKELNETVVSLCNDQEVSKTKEQNLGSQVQTLELEKAQLLQDLGEAKNKYIIFQSSVNALTQEVEAGKQKLEKGEKEIRTLKEQLKSQEQLVCKLAQVEGEQELWQKQKLELRNVTMALEQKVQVLQSENNTLQSTYEALQNSHKSLESELGLIKLEKVALVERVSTISGKEAELQRELRDMLQKTTQLSEDYNKEKNRLTEEVEVLREELQNTKAAHLKSVNQLEKELQRAQGKIKLMLKSCRQLEGEKEMLQKELSQLEAAQQQRAGSLVDSNVDEVMTENKALKETLEEKVKEADKYLDKYCSLLISHEELEKAKEILEIEVARLKSRQSRQDLQSSPLLNSSIPGPSPNTSVSEMKSASGQNKASGKRQRSSGVWEHGKRAAPSTAETFSKKSRKSDSKSTRPAEHEQETEFEPEGLPEVVKKGFADIPTGKTSPYILRRTTMATRTSPRFATQKLVGSSPSLGKENVVESSKPTAGGSRSQKVKVVQESSADSHTAFQELPAKSLTASNIPGRNSTESPREGLRAKRAYPASSPAAGPDPTNNENCRVQ
Protein: Sorting nexin (A0A0A0MRI2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRACAGPRLGAAMMEGLDDGPDFLSEEDRGLKAINVDLQSDAALQVDISDALSERDKVKFTVHTKSSLPNFKQNEFSVVRQHEEFIWLHDSFVENEDYAGYIIPPAPPRPDFDASREKLQKLGEGEGSMTKEEFTKMKQELEAEYLAIFKKTVAMHEVFLCRVAAHPILRRDLNFHVFLEYNQDLSVRGKNKKEKLEDFFKNMVKSADGVIVSGVKDVDDFFEHERTFLLEYHNRVKDASAKSDRMTRSHKSAADDYNRIGSSLYALGTQDSTDICKFFLKVSELFDKTRKIEARVSADEDLKLSDLLKYYLRESQAAKDLLYRRSRSLVDYENANKALDKARAKNKDVLQAETSQQLCCQKFEKISESAKQELIDFKTRRVAAFRKNLVELAELELKHAKGNLQLLQNCLAVLNGDT
Protein: Thymosin beta-10 (Q6ZWY8)
Organism: Mus musculus (Mouse)
Function: Plays an important role in the organization of the cytoskeleton. Binds to and sequesters actin monomers (G actin) and therefore inhibits actin polymerization (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
Sequence:
MADKPDMGEIASFDKAKLKKTETQEKNTLPTKETIEQEKRSEIS
Protein: Wurstfest, isoform B (A0A0B4JCT9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVTDAQDTVAPKTSSTKEVQCQHSGALDEPHVEELALPGPAPLATPKSGRVGIFNAEDFLSRAQLNDKINNILRSPTKAPNGVRQRSVFTNNNPSPQATMRFVSSMNSPLAPRMSSLSLTGGVKRGLERGNSSSSMGNSASVGTSTSVLAKECSSQTNSCGRSYMNMGMHASSHSGFGVLPQSGAGYETMGWNMDAGNITRSGKSLTGRFNSGYGYEVDGAYCMAHHTQQFPSPMPPPPFAMDRVSSRTFEFENNTPPPCPGSGPIAMSNGTIQLRLREGVRIDMTLDKAVRVLNQRSMVAAALSRNCSNSALIHPNGRILQSGSKVEIVTYDGMKANNFVRYAKMWYKGVSFTSESCALIYLVDTAGTRTTTDTFTDLTKDYTLAVFYDDSRHGPSFVSDAHDVIANSTYNCAEDGTEVYDINGFRITQAADGLVKVSRQHSKCLIRTSPGNGSATLTTTGIHCTASLGKTSHLFVRRNEKRMHFDGSCFIVRNAGHSAGFNENNLLIVY
Protein: Monoglyceride lipase (MGL) (EC 3.1.1.23) (Fatty acid ethyl ester hydrolase) (FAEE hydrolase) (Monoacylglycerol hydrolase) (MAG hydrolase) (MGH) (Monoacylglycerol lipase) (MAG lipase) (MAGL) (Serine hydrolase YJU3) (P28321)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Converts monoacylglycerides (MAG) to free fatty acids and glycerol. Has a strong preference for monounsaturated monoglycerides. Required for efficient degradation of MAG, short-lived intermediates of glycerolipid metabolism which may also function as lipid signaling molecules. Controls inactivation of the signaling lipid N-palmitoylethanolamine (PEA). Involved in fatty acid ethyl ester (FAEE) catabolism. FAEEs are non-oxidative metabolites of ethanol that are transiently incorporated into lipid droplets (LDs). Their mobilization by LD-resident FAEE hydrolases facilitates a controlled metabolism of these potentially toxic lipid metabolites.
Subcellular location: Lipid droplet {ECO:0000269|PubMed:10515935, ECO:0000269|PubMed:20554061, ECO:0000269|PubMed:21820081, ECO:0000269|PubMed:24868093}. Cytoplasm {ECO:0000269|PubMed:11914276}. Endoplasmic reticulum {ECO:0000269|PubMed:14562095}. Mitochondrion outer membrane {ECO:0000269|PubMed:16407407}. Note=Although the protein is identified in the cytoplasm, several membrane systems and lipid droplets, MGL activity is only measured in membrane fractions and lipid droplets. {ECO:0000269|PubMed:20554061}.
Interaction partners:
- Triacylglycerol lipase 4
- Triacylglycerol lipase 3
- Triacylglycerol lipase 5
- RNA polymerase I-specific transcription initiation factor RRN11
- Triacylglycerol lipase 2
- Diacylglycerol O-acyltransferase 1
- Bud site selection protein 22
- Acyl carrier protein, mitochondrial
- Protein SIP4
- Truncated non-functional calcium-binding mitochondrial carrier SAL1-1
Sequence:
MAPYPYKVQTTVPELQYENFDGAKFGYMFWPVQNGTNEVRGRVLLIHGFGEYTKIQFRLMDHLSLNGYESFTFDQRGAGVTSPGRSKGVTDEYHVFNDLEHFVEKNLSECKAKGIPLFMWGHSMGGGICLNYACQGKHKNEISGYIGSGPLIILHPHTMYNKPTQIIAPLLAKFLPRVRIDTGLDLKGITSDKAYRAFLGSDPMSVPLYGSFRQIHDFMQRGAKLYKNENNYIQKNFAKDKPVIIMHGQDDTINDPKGSEKFIQDCPSADKELKLYPGARHSIFSLETDKVFNTVFNDMKQWLDKHTTTEAKP
Protein: DUF3700 domain-containing protein (A0A178U6D3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MLAVFEKTVANSPEALQSPHSSESAFALKDGSLATHFASVNPNSVTLNFGSSGFVAYSLDNPDPRVPRLFAVVDDIFCLFQGHIENLPFLKQQYGLNKITNEAIIVIEAYRTLRDRGPYPVDKVVRDFHGKFAFILFDSVKKTVFAAADADGSVPFFWGTDAEGHLVFSDNTEMVKKGCAKSYGPFPKGCFFTSSGGLRSFEHPKNELKPVPRVDSSGDVCGATFKVDAETKREGTKMPRVDSSQNWAGHI
Protein: Glycogen debranching enzyme (EC 3.2.1.196) (Glycogen operon protein GlgX) (Limit dextrin alpha-1,6-maltotetraose-hydrolase) (P15067)
Organism: Escherichia coli (strain K12)
Function: Removes maltotriose and maltotetraose chains that are attached by 1,6-alpha-linkage to the limit dextrin main chain, generating a debranched limit dextrin. Shows only very little activity with native glycogen.
Interaction partners:
- Glucose-1-phosphate adenylyltransferase
- 4-alpha-glucanotransferase
- 1,4-alpha-glucan branching enzyme GlgB
- Glycogen phosphorylase
- Glycogen synthase
- Maltodextrin phosphorylase
- Phosphoglucomutase
- Periplasmic alpha-amylase
- Cytoplasmic alpha-amylase
- UTP--glucose-1-phosphate uridylyltransferase
Sequence:
MTQLAIGKPAPLGAHYDGQGVNFTLFSAHAERVELCVFDANGQEHRYDLPGHSGDIWHGYLPDARPGLRYGYRVHGPWQPAEGHRFNPAKLLIDPCARQIDGEFKDNPLLHAGHNEPDYRDNAAIAPKCVVVVDHYDWEDDAPPRTPWGSTIIYEAHVKGLTYLHPEIPVEIRGTYKALGHPVMINYLKQLGITALELLPVAQFASEPRLQRMGLSNYWGYNPVAMFALHPAYACSPETALDEFRDAIKALHKAGIEVILDIVLNHSAELDLDGPLFSLRGIDNRSYYWIREDGDYHNWTGCGNTLNLSHPAVVDYASACLRYWVETCHVDGFRFDLAAVMGRTPEFRQDAPLFTAIQNCPVLSQVKLIAEPWDIAPGGYQVGNFPPLFAEWNDHFRDAARRFWLHYDLPLGAFAGRFAASSDVFKRNGRLPSAAINLVTAHDGFTLRDCVCFNHKHNEANGEENRDGTNNNYSNNHGKEGLGGSLDLVERRRDSIHALLTTLLLSQGTPMLLAGDEHGHSQHGNNNAYCQDNQLTWLDWSQASSGLTAFTAALIHLRKRIPALVENRWWEEGDGNVRWLNRYAQPLSTDEWQNGPKQLQILLSDRFLIAINATLEVTEIVLPAGEWHAIPPFAGEDNPVITAVWQGPAHGLCVFQR
Protein: Integration host factor subunit alpha (IHF-alpha) (Q51472)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: This protein is one of the two subunits of integration host factor, a specific DNA-binding protein that functions in genetic recombination as well as in transcriptional and translational control.
Interaction partners:
- Integration host factor subunit beta
- HTH merR-type domain-containing protein
- RNA-binding protein Hfq
- MvaT
- Phenylalanine--tRNA ligase beta subunit
- Putative Fis-like DNA-binding protein
- Large ribosomal subunit protein bL35
- DNA-binding protein HU-beta
- Acyl carrier protein 1
- Large ribosomal subunit protein bL20
Sequence:
MGALTKAEIAERLYEELGLNKREAKELVELFFEEIRQALEHNEQVKLSGFGNFDLRDKRQRPGRNPKTGEEIPITARRVVTFRPGQKLKARVEAYAGTKS
Protein: Deoxynucleoside triphosphate triphosphohydrolase SAMHD1 (dNTPase) (EC 3.1.5.-) (Q502K2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Protein that acts both as a host restriction factor involved in defense response to virus and as a regulator of DNA end resection at stalled replication forks. Has deoxynucleoside triphosphate (dNTPase) activity, which is required to restrict infection by viruses: dNTPase activity reduces cellular dNTP levels to levels too low for retroviral reverse transcription to occur, blocking early-stage virus replication in dendritic and other myeloid cells. Functions during S phase at stalled DNA replication forks to promote the resection of gapped or reversed forks: acts by stimulating the exonuclease activity of MRE11, activating the ATR-CHK1 pathway and allowing the forks to restart replication. Its ability to promote degradation of nascent DNA at stalled replication forks is required to prevent induction of type I interferons, thereby preventing chronic inflammation. Ability to promote DNA end resection at stalled replication forks is independent of dNTPase activity.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9Y3Z3}. Chromosome {ECO:0000250|UniProtKB:Q9Y3Z3}. Note=Localizes to sites of DNA double-strand breaks in response to DNA damage. {ECO:0000250|UniProtKB:Q9Y3Z3}.
Interaction partners:
- Ribonuclease
- Ribonuclease H2 subunit C
- Uncharacterized protein.
- Ribonuclease H2, subunit B.
Sequence:
MENRIKRPRVDGECVKSINNGEFDRWDVEDTVAYLRGEGLQEWAQIFKDNGITGAGLLCLTEAHLEKMGVSPLGARLHILHCLQKLSQISTEPMKVFNDPIHGHIELHPLLLHFIDTPQFQRLRHIKQLGGTYLVFPGASHNRFEHSIGVGYLAGCLVKALNERQPELFITKQDILCVQIAGLCHDLGHGPFSHMFDGMFIPKARPADKWKHEIASVQMFDHLVEVNGLEAVMLHHGMRLPEDLIFIKEQIAGPLESAVLDQSQWPYKGRPVEKSFLYEVVANKRNGIDVDKWDYFARDCYHLGIQNNFDYQRFLRFARVCEVKGRKHICTRDKEVGNLYDMFHTRNCLHRRAYQHKVGNIIETMITEAFLKADPHIQIQGSSGRIFTISSAIEDMEAYSKLTDHIFEQILYSSGPELSEARAILQNIICRRLYKCVGQTTSETNVDVSQEKLLDWAKELARSKPTGTEGNLIAEDFVVSVIHMDYGMKEKNPINNVHFYCKNDPTKAIKIHKKQVSKLLPERFAEQLIRVYCKKTDDKSLEAAKKYFVQWCMDRNFTKPQDGDIIAPELTPLKQDWHAREDEDEEEEEKHRQNQTLPHHTPQRTGRNVKVDLFQARGETKL
Protein: NF-kappa-B inhibitor delta (NFKB inhibitor delta) (I-kappa-B-delta) (IkB-delta) (IkappaBdelta) (IkappaBNS) (T-cell activation NFKB-like protein) (TA-NFKBH) (Q8NI38)
Organism: Homo sapiens (Human)
Function: Regulates the expression of IL-2, IL-6, and other cytokines through regulation on NF-kappa-B activity. Functions in the regulation of inflammatory responses. Involved in the induction of T helper 17 cells (Th17) differentiation upon recognition of antigen by T cell antigen receptor (TCR). May also regulate TCR-induced negative selection of thymocytes.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q2TB02}.
Interaction partners:
- Proto-oncogene c-Rel
- Nuclear factor NF-kappa-B p100 subunit
- NF-kappa-B inhibitor beta
- Nuclear factor NF-kappa-B p105 subunit
- Transcription factor RelB
- Transcription factor p65
Sequence:
MEAGPWRVSAPPSGPPQFPAVVPGPSLEVARAHMLALGPQQLLAQDEEGDTLLHLFAARGLRWAAYAAAEVLQVYRRLDIREHKGKTPLLVAAAANQPLIVEDLLNLGAEPNAADHQGRSVLHVAATYGLPGVLLAVLNSGVQVDLEARDFEGLTPLHTAILALNVAMRPSDLCPRVLSTQARDRLDCVHMLLQMGANHTSQEIKSNKTVLHLAVQAANPTLVQLLLELPRGDLRTFVNMKAHGNTALHMAAALPPGPAQEAIVRHLLAAGADPTLRNLENEQPVHLLRPGPGPEGLRQLLKRSRVAPPGLSS