wanglab/gogpt-training-data huggingface dataset:
Protein: Respiratory burst oxidase homolog protein F (EC 1.11.1.-) (EC 1.6.3.-) (Cytochrome b245 beta chain homolog RbohAp108) (NADPH oxidase RBOHF) (AtRBOHF) (O48538)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Calcium-dependent NADPH oxidase that generates superoxide. Generates reactive oxygen species (ROS) during incompatible interactions with pathogens and is important in the regulation of the hypersensitive response (HR). Involved in abscisic acid-induced stomatal closing and in UV-B and abscisic acid ROS-dependent signaling.
Subcellular location: Cell membrane {ECO:0000269|PubMed:23335733, ECO:0000269|PubMed:9490748}; Multi-pass membrane protein {ECO:0000269|PubMed:23335733, ECO:0000269|PubMed:9490748}.
Interaction partners:
- CBL-interacting serine/threonine-protein kinase 26
- Serine/threonine-protein kinase SRK2E
- Calcium-dependent protein kinase 6
- Guard cell S-type anion channel SLAC1
- Calcineurin B-like protein 1
- Calcium-dependent protein kinase 5
- Calcium-dependent protein kinase 23
- Phospholipase D alpha 1
- Calcium-dependent protein kinase 3
- Nitrate reductase 1
Sequence:
MKPFSKNDRRRWSFDSVSAGKTAVGSASTSPGTEYSINGDQEFVEVTIDLQDDDTIVLRSVEPATAINVIGDISDDNTGIMTPVSISRSPTMKRTSSNRFRQFSQELKAEAVAKAKQLSQELKRFSWSRSFSGNLTTTSTAANQSGGAGGGLVNSALEARALRKQRAQLDRTRSSAQRALRGLRFISNKQKNVDGWNDVQSNFEKFEKNGYIYRSDFAQCIGMKDSKEFALELFDALSRRRRLKVEKINHDELYEYWSQINDESFDSRLQIFFDIVDKNEDGRITEEEVKEIIMLSASANKLSRLKEQAEEYAALIMEELDPERLGYIELWQLETLLLQKDTYLNYSQALSYTSQALSQNLQGLRGKSRIHRMSSDFVYIMQENWKRIWVLSLWIMIMIGLFLWKFFQYKQKDAFHVMGYCLLTAKGAAETLKFNMALILFPVCRNTITWLRSTRLSYFVPFDDNINFHKTIAGAIVVAVILHIGDHLACDFPRIVRATEYDYNRYLFHYFQTKQPTYFDLVKGPEGITGILMVILMIISFTLATRWFRRNLVKLPKPFDRLTGFNAFWYSHHLFVIVYILLILHGIFLYFAKPWYVRTTWMYLAVPVLLYGGERTLRYFRSGSYSVRLLKVAIYPGNVLTLQMSKPTQFRYKSGQYMFVQCPAVSPFEWHPFSITSAPEDDYISIHIRQLGDWTQELKRVFSEVCEPPVGGKSGLLRADETTKKSLPKLLIDGPYGAPAQDYRKYDVLLLVGLGIGATPFISILKDLLNNIVKMEEHADSISDFSRSSEYSTGSNGDTPRRKRILKTTNAYFYWVTREQGSFDWFKGVMNEVAELDQRGVIEMHNYLTSVYEEGDARSALITMVQALNHAKNGVDIVSGTRVRTHFARPNWKKVLTKLSSKHCNARIGVFYCGVPVLGKELSKLCNTFNQKGSTKFEFHKEHF
Protein: Protein TPX2 (AtTPX2) (Targeting protein for XKLP2) (F4I2H7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Regulates prospindle assembly during late prophase and at the onset of mitosis, before nuclear envelope breakdown (NEB). Is exported from the nucleus shortly before NEB and organized into two polar crescents. After NEB, is progressively associated with the forming spindle. Probably mediates AUR1 activation and localization to spindle microtubules. Has a microtubule binding capability and is able to trigger microtubule assembly induced by RanGTP in a heterologous system. Not involved in phragmoplast assembly, nuclear envelope reformation, and cortical microtubule assembly at the onset of G1. Involved in the formation of specific nuclear and perinuclear microtubular arrays in the nuclei of acentrosomal plant cells. Fungi and plants have acentrosomal microtubule arrays because they lack centrosomes. They use other microtubule organizing center (MTOC) structures to organize their microtubules. May function through interaction with importin.
Subcellular location: Nucleus, nucleoplasm. Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, phragmoplast. Note=Located in the nucleoplasm during interphase until late G2, in the perinuclear region during early prophase, and at the spindle during mitosis. Localized on a specific subset of phragmoplast microtubules in early telophase.
Interaction partners:
- Serine/threonine-protein kinase Aurora-1
- Importin subunit alpha-1
- Mitotic spindle checkpoint protein MAD2
- Importin subunit alpha-6
- Protein WVD2-like 1
- Importin subunit alpha-7
- Cell cycle regulated microtubule associated protein
- Importin subunit alpha-5
- Importin subunit alpha-8
- Importin subunit alpha-9
Sequence:
MEATAEESVSTLVTTMVDETYEFLAPRWFDFVNGETEDESRRAELWFQSALSCAPSPSVPRIKARRSFKVEAMCNFNEAEEETLKDKEPLEPVVPIVSLQSQPSQAKKAEVAPSKASTVKPSRISSKDAEVNNKTVDASDPTTEPIEDKENIAPACTPKPPMQFSLGAKSVDLKKQQTARKIASLLKNPSTLRPKNQSQAKGSHQKSVKGETNLNNIASTTNLIQENQAIKRQKLDDGKSRQILNPKPATLLHKTRNGLVNTGFNLCPSVTKHTPKENRKVYVREQIAPFVSTAELMKKFQTSTRDLFVQNRPKLTLTRPKEPEFVTSQRARPLRVKSSAELEEEMLAKIPKFKARPVNKKILAAPALPAPQRSTPHLPEFQEFHLQTMARANQHAETSSIASTEVSKQHNDQKHHLTEPKSPVLQTMLRARPTIAKTTAELEQEELEKAPKFKAKPLNKKIFESKGEMGIFCNTKKHITIPQEFHFATDERISRPESVLDIFDKLSLNSESCHEKPLPRNTAPNPFNLKTEERGAEKEKKFYMELMYKKLGDVKARVPKANPYPYTTDYPVVPPKPEPKQCTQPEPFQLESLVRHEEEMRREREERRRMETEEAQKRLFKAQPVIKEDPIPVPEKVRMPLTEIQEFNLHVEHRAVERADFDHKIKEKENQYKRYREESEAAKMVEEERALKQMRKTMVPHARPVPNFNKPFLPQKSNKGTTKAKSPNLRVIKRTERRTMMARPTISAATSASAVHCLMYPGSSFNKLKKKTVLTNIVHCLMYPDSSLLN
Protein: Thiohydroximate-O-sulfate sulfur/sulfate-lyase (nitrile-forming) NSP4 (EC 4.8.1.5) (Jacalin-related lectin 29) (Nitrile-specifier protein 4) (AtNSP4) (O04316)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Promotes simple nitriles, but not epithionitrile or thiocyanate formation. Converts allylglucosinolate and benzylglucosinolate to their corresponding simple nitriles in the presence of myrosinase.
Interaction partners:
- UPF0235 protein At5g63440
- Beta-glucosidase 19
- Probable cysteine protease RD21B
- Probable cysteine protease RD21C
- At1g09850
- Cysteine proteinase RD21A
- Beta-glucosidase 26, peroxisomal
- Beta-glucosidase 33
Sequence:
MAQKVEAQGGNGGNQWDDGSEYDAVTKIQVAAGGNGIEYVKFTYVKNGQTEEAPLRGVKGRSFEADPFVINHPEEHLVSVEGRYNPEGLILGLTFKSNKKTSDLIGYEDGTPFTLQVQDKKIVGFYGFAGNNLHSLGAYFAPLTNVTPLNAKKLEAKGGDTGDIWDDGVYDNVRKVYVGQAQYGIAFVKFEYVNGSQVVVGDEHGKKTELGVEEFEIDADDYIVYVEGYREKVNGMTSEMITFLSFKTYKGKTSQPIEQRPGIKFVLQGGKIVGFHGRSTDVLDSLGAYISLSPTPNLHGKWTKVDENGDGPGLRCSHDIAQVGNKIYSFGGEFTPNQPIDKHLYVFDIESRTWSISPATGDIPTLSCLGVCMVSIGSTLYVFGGRDASRQYNGFYSFDTTTNEWKLLTPVEEGPTPRSFHSMAADEENVYVFGGVSATARLNTLDSYNIVDKKWFHCSTPGDSLTARGGAGLEVVQGKVWVVYGFNGCEVDDVHYYDPVQDKWTQVETFGVRPSERSVFASAALGKHIVIFGGEIAMDPLAHVGPGQLTDGTFALDTETLQWERLDKFGGEEETPSSRGWTASTTATIGGKKGLVMHGGKAPTNDRFDDLFFYGIDSA
Protein: Uncharacterized protein (Q387E7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSGYGESMHSLREPVSPCPRRRSLASTPLERQRSYSRGGMVGSPVPDDMSFTLSPLPYFPKRTRSVTFEESDEVPVREERPYYSWDDRHGLSDKRGFDDNGAAVAVRDGGEECHYARSGAAGRREEGDQRYRPFVVAGTTFKIPRSRSQSRQHREAEEKLAMSTFSYPEIRKVEDFCTQLLRPLEENEPPQREGYRGAHTNEGVNAGNDAGQPPEITPIRKAKATLKSGLKTDYVSRANCDLQRTVADHLPRRRGRSNKREASRPKEEESGEEGYSMEASVAPHEAKQKTTRCVTTATPQCGVGVGGASRRRTRCESVEEGVVHSTTQKCIHVIDIHNAEEEIKSLPTEITATVSCVVKGLLDDLSNQSFPIIIKPCKSGGLKQVEVHLVDGMGDEEHGDWMPQRVVASAPQNRKRAPQKRAAERSVPSVSCKKESSATPLVAPEVVPVAKRSLPRPAAPPLIDELNGGEEPVLLRRSGTMQKRPARSVSYISVDTDDMAEANETSATVRRPQSAPKSTTTTTRRCRKASATAVEAPTCHPPLSNVTHSSPIPPDPFLATEEDLESIVEEPVTLRRNGHLNKPTSDWNSFANDDSDVLDNFLVKFVPENAGLMLARANICTRKGRRKTRGAALSLPPSIGGRTR
Protein: Calmodulin-1 (P0DP26)
Organism: Mus musculus (Mouse)
Function: Calmodulin acts as part of a calcium signal transduction pathway by mediating the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Calcium-binding is required for the activation of calmodulin. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases, such as myosin light-chain kinases and calmodulin-dependent protein kinase type II (CaMK2), and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis. Is a regulator of voltage-dependent L-type calcium channels. Mediates calcium-dependent inactivation of CACNA1C. Positively regulates calcium-activated potassium channel activity of KCNN2. Forms a potassium channel complex with KCNQ1 and regulates electrophysiological activity of the channel via calcium-binding. Acts as a sensor to modulate the endoplasmic reticulum contacts with other organelles mediated by VMP1:ATP2A2.
Subcellular location: Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P0DP23}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:P0DP23}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P0DP23}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:29025071}. Note=Distributed throughout the cell during interphase, but during mitosis becomes dramatically localized to the spindle poles and the spindle microtubules. {ECO:0000250|UniProtKB:P0DP23}.
Interaction partners:
- Nitric oxide synthase 1
- Ryanodine receptor 2
- Voltage-dependent L-type calcium channel subunit alpha-1C
- Protein phosphatase 3 catalytic subunit alpha
- Ryanodine receptor 1
- Nitric oxide synthase, inducible
- GTPase KRas
- Calmodulin-4
- Calcium/calmodulin-dependent protein kinase type II subunit gamma
- Calmodulin 5
Sequence:
MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK
Protein: Uncharacterized fimbrial-like protein YfcR (P76501)
Organism: Escherichia coli (strain K12)
Function: Part of the yfcOPQRSUV fimbrial operon. Could contribute to adhesion to various surfaces in specific environmental niches. Increases adhesion to eukaryotic T24 bladder epithelial cells in the absence of fim genes.
Interaction partners:
- Uncharacterized fimbrial-like protein YfcP
- Uncharacterized protein YfcO
- Probable fimbrial chaperone YfcS
- Uncharacterized fimbrial-like protein YfcQ
- Probable fimbrial chaperone YehC
- Uncharacterized fimbrial-like protein YadK
Sequence:
MTGGVMSQKFVVGAGLLVCSVCSLSAMAGSKPVDLILRVLVDAPPPCSIKGSQVEFGNMIADNVDGTNYRQDAKYTLNCTNSLANDLRMQLKGNTSTINGETVLSTNITGLGIRIENSADNSLFAVGENSWTPFNINNQPQLKAVPVKASGAQLAAGEFNASLTMVVDYQ
Protein: Solute carrier family 25 member 10 isoform 2 (A0A0S2Z382)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MAAEARVSRWYFGGLASCGAACCTHPLDLLKVHLQTQQEVKLRMTGMALRVVRTDGILALYSGLSASLCRQMTYSLTRFAIYETVRDRVAKGSQGPLPFHEKVLLGSVSGLAGGFVGTPADLVNVRMQNDVKLPQGQRRNYAHALDGLYRVAREEGLRRLFSGATMASSRGALVTVGQLSCYDQAKQLVLSTGYLSDNIFTHFVASFIAGGCATFLCQPLDVLKTRLMNSKGEYQGVFHCAVETAKLGPLAFYKGLVPAGIRLIPHTVLTFVFLEQLRKNFGIKVPS
Protein: Protein suppressor of variegation 3-7 (P20193)
Organism: Drosophila melanogaster (Fruit fly)
Function: Dose-limiting factor in position-effect variegation, the inactivation in some cells of a gene translocated next to heterochromatin. It could play a role in chromosome condensation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Histone-lysine N-methyltransferase Su
- Chromosomal serine/threonine-protein kinase JIL-1
- Heterochromatin protein 1
- Dosage compensation regulator mle
- Protein suppressor of underreplication
Sequence:
MDRDSSMQAKNLDAQCNPDLKMASANSETLASATHELKIMDVEGGALVDPDHIEEVETSMVIVVDDDDGDVAMVVEEDKHPMRDDPCIEDIMDDEHAPLVAELQSALNNPDDKQASEDPLLEDQEREPDAMSTKTEPSSDAESSHSYHDPMGLLERIEIHDPGDSQDDDDEDDESSNGGGVDGGMRRKMPRAQRWLLWMKRWPWILHEDSDGTLAFCLYCNISINVNNRSRHIQQHNVSLSHQERECNYLAFKKSEEETRGAISDNEIKHEFGTKSYVAAMKQKRISETEAFNNFNWLRWLRWHPWLERSMPTGTIGTCRICSVRMNVEFVYLRKRHETTKGHMEALRNLDSDKRSRKRKRSKSNSVTNSGGDEAEREKESEPEVGPEDAQDTPVVMMNGDVDSGDDPGKWCALIPDTNPQQCRCTLCNCTMAITSFLRHCKTRAHCHMLSTPAEKGSSDIRGIWAVFADMHPWLIADPEDPSIGYCSVCRKRFMYGNSEIKRKNHEKSEKHTLALASAKAGIEVGSADGRGGDNMDEEEAAASDQAQSSQTDDSEDNDDDNWSEIQKLGKGFAHKSSSEPRKATVRAGVRFYPWLCYSKDRKTQICKFCRVRFHNEAAKARHELSARHVKLVKQFKMRQAKLHQGTNTQTKHNAQDDEESQEQDEEYGEEEEDAEEDSQSNFDLGTVQARKTARADNKLFVKPIPATMKGKVMVWKGRFPWLSYKKNEQRGNYAWCKLCEVSLYLPSSKWASKHQRTSRHIRLRIDRKRNGGNPLKTSNKNSGEISTVVATASALASAEARQKAAMAELQAKYDWLDPDANDENHCHCRVCDSRLPIKVFYLRQHDASRKHVENKERQRANAAAAANAPSVSPTSTVDAERQESGMDKESENDMSVRSDGSTAEPLAKRSRRSMEVRRIIRALRDSMGKRQEERSQMDMARDMICSSFDIVTRLRTLERESVAHNESMAQAPPSVTVSPIKPPEPRHVMDLFFDSISPTMKSLPPDLAAEGKSKIMQLVCSLELRAMQRNATTPTPATVSASSKWPSSTTVTPVKTPPAPISAPLASVDADLHSSVVTTPHEYNNGQNNNNDKETVPKEPVTGASSAQVTINGSAKDLPENIRRILTSNQTQVTNRLETDSVRCVPLDKLTTQSRTNVNGRLSQGGTSEAPSTPQADLSNGNTLAMIRQIRVNNNNSSKITVTNTPQMQQPQQAQASITSSTPIMRGGPSSNGCQITTFRTMVNHNRRP
Protein: Zinc finger protein 592 (Zfp-592) (Q8BHZ4)
Organism: Mus musculus (Mouse)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Zinc finger, MYND-type containing 8
- Integrator complex subunit 5
- Integrator complex subunit 3
- Integrator complex subunit 6
- Zinc finger protein 687
- Zinc finger protein 532
Sequence:
MGDMKTPDFDDLLAAFDIPDPTSLDAKEAIQAPSEENESPLKSSGMCIDENVSLSHSGSAPDVPAVSVIVKNTSRQESFEAEKDHIAPSLLHNGFRGSDLPPDSHHCGKFDSTFINGDSARSFTSKLEPSKSEPLPTFNQFSPISSPEPEDPVKDNGFGIKSKHSDSYFPPPPGTVGGPVLEALSKFPVPELHMFDHFCKKEPKPEPLPLESQQEHEQGGQKVVEPHKDLDSSRFFGEALEFNSHPSNSIGEPKKLAPELSACSSVPPRQRLKPAHSKLSSCVAALVALQAKRVANVTKEDQPGHTKDSSGPTKEGSKGSPKMPKSPKSPRSPLEATRKSIKPSDSPRSICSDSSSKGSPSVAASSPPAIPKVRIKTIKTSSGEIKRTVTRILPDPDDPSKSPAESPAGSTITEAPSEAPGDEGTAMPVEEHFSEAGIHSGSPQGDRKGDENMIKTSDSSSPCRISGSRVPKGSALNSQASKKQQSTAPQASTPAASLLPKAVHLANLNLVPHSVAASVTAKSSAQRRSQPQVTQMTVPLVHQVKKAAPLIVEVFNKVLHSSNPVPLYAPNLSPPADSRIHVPASGYCCLECGDAFALEKSLSQHYSRRSVHIEVLCTLCSKTLLFFNKCSLLRHARDHKSKGLVMQCSQLLVKPISADQMFVAAPVNSTAPATPAASSSPKPSPTLDNASSVIPALPLYPDPVRLIRYGTKCPECHKQMRDYMVLATHFQRTTEETEGLTCQVCQMLLPNQCSFCAHQRIHAHKSPYCCPECGVLCRSAYFQTHVKENCLHYARKVGYRCIHCGVIHLTLALLKSHIQERHCQVFHKCAFCPMAFKTASSTMDHSTTQHPTQPHKPSQLIYKCSCEMVFNKKRHIQQHFYQNVSKTQAGVFKCPECPLLFLQKPELMQHVKNTHGVPRNVEELSSLQSSTDTSSNRPGSRAPAEPPATNVAARGSSLTAGRWGRPEAHRRAEARPRMRSTGWTCQECQEWVPDRESYVSHMKKSHGRTLKRYPCRQCEQSFHNPSSLRKHIRNNHDTVKKVYTCGYCTEDSPSFPRPSLLESHISLMHGIRNPDLSQTSKVRHPGGPSPQVNHLKRPVSRMADAPGTSNGATVSSTKRHKSLFQCAKCTFATDSELEFQSHIPQHQVDSSTAQCLLCGLCYTSTSSLNRHLFIVHKVRDQEEGGEDIVEVKVEAPDSEACSGEEVAMETKENGLEECASEPLVTDLGGQQGLALDEDSAQDPQNQPQASQDQNSHALSPQV
Protein: Trailer hitch, isoform C (M9PF14)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSGGLPELGSKISLISKADIRYEGRLYTVDPQECTIALSSVRSFGTEDRDTQFQIAPQSQIYDYILFRGSDIKDIRVVNNHTLPHHNDPAIMQAQLQNGPPQMPQHFPMPSGMSGPPQQQQVPSQQPPQMPSGGGSGGAGGAGAPGGGGPGYGNGNPFGNLGGPNLANMVGNAGGSLAPGSGAPGSGPFMHIGGNQQQPKPQQQKQPISVLDMLAGASRSTTPISLIVSPTAELTQQQQLHQQQNAGQGGNGRDAGHKRQNHQQQQNQQHQQRGGPSHNNMQQQQQRGGGSGTDFYNQQRDRRDSGRQMDNNYSNNYNNNNNNQRNRGGGNGMQQQQRGGNGGSGGGGGNGGGNNPAWNMHRGNQNSNNMMNMRNRGMGSRGPMRPNQGYRPQSANNQNKPRNKIKFEGDFDFEQANNKFEELRSQLAKLKVAEDGAPKPATNATAATATATNEQVGEKVEGVHTLNGETDKKDDSGNETGAGEHEPEEDDVAVCYDKTKSFFDNISCEAAQDRSKNKKNDWRQERKLNTETFGVSSTRRGSYRGRNQYYNNNGNGGINSGYGGAPGYNRNNYRMGGGGGNFRNRSNNRNNGGGRGGNGMPNITNGNTAAALKAANNAAGHGSNATDSSAPNATTATTKSTSLLPEQTQQVAAVSQ
Protein: Bifunctional protein GlmU [Includes: UDP-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23) (N-acetylglucosamine-1-phosphate uridyltransferase); Glucosamine-1-phosphate N-acetyltransferase (EC 2.3.1.157)] (P9WMN3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01631}.
Interaction partners:
- Phosphoglucosamine mutase
- UDP-N-acetylglucosamine 1-carboxyvinyltransferase
- Ribose-phosphate pyrophosphokinase
- Phosphate acetyltransferase
- Glutamine--fructose-6-phosphate aminotransferase
- UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
- UDP-N-acetylmuramate--L-alanine ligase
- UDP-N-acetylmuramoylalanine--D-glutamate ligase
- Serine/threonine-protein kinase PknB
- Putative lipoprotein LpqT
Sequence:
MTFPGDTAVLVLAAGPGTRMRSDTPKVLHTLAGRSMLSHVLHAIAKLAPQRLIVVLGHDHQRIAPLVGELADTLGRTIDVALQDRPLGTGHAVLCGLSALPDDYAGNVVVTSGDTPLLDADTLADLIATHRAVSAAVTVLTTTLDDPFGYGRILRTQDHEVMAIVEQTDATPSQREIREVNAGVYAFDIAALRSALSRLSSNNAQQELYLTDVIAILRSDGQTVHASHVDDSALVAGVNNRVQLAELASELNRRVVAAHQLAGVTVVDPATTWIDVDVTIGRDTVIHPGTQLLGRTQIGGRCVVGPDTTLTDVAVGDGASVVRTHGSSSSIGDGAAVGPFTYLRPGTALGADGKLGAFVEVKNSTIGTGTKVPHLTYVGDADIGEYSNIGASSVFVNYDGTSKRRTTVGSHVRTGSDTMFVAPVTIGDGAYTGAGTVVREDVPPGALAVSAGPQRNIENWVQRKRPGSPAAQASKRASEMACQQPTQPPDADQTP
Protein: Transmembrane 9 superfamily member 1 (70 kDa endomembrane protein) (Endomembrane protein EMP70) [Cleaved into: Protein p24a (Acidic 24 kDa late endocytic intermediate component)] (P32802)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: With TMN2 and TMN3, plays a critical role in the late stages of a nutrient-controlled pathway notably regulating FLO11 gene expression. Acts downstream of RAS2 and TOR. Essential for cell adhesion and filamentous growth. May play a role as effector of cellular copper homeostasis.
Subcellular location: Endosome membrane {ECO:0000269|PubMed:8314797}; Multi-pass membrane protein. Vacuole membrane {ECO:0000269|PubMed:20681974}; Multi-pass membrane protein.
Interaction partners:
Sequence:
MIYKMAHVQLLLLYFFVSTVKAFYLPGVAPTTYRENDNIPLLVNHLTPSMNYQHKDEDGNNVSGDKENFLYSYDYYYNRFHFCQPEKVEKQPESLGSVIFGDRIYNSPFQLNMLQEKECESLCKTVIPGDDAKFINKLIKNGFFQNWLIDGLPAAREVYDGRTKTSFYGAGFNLGFVQVTQGTDIEATPKGAETTDKDVELETRNDRNMVKTYELPYFANHFDIMIEYHDRGEGNYRVVGVIVEPVSIKRSSPGTCETTGSPLMLDEGNDNEVYFTYSVKFNESATSWATRWDKYLHVYDPSIQWFSLINFSLVVVLLSSVVIHSLLRALKSDFARYNELNLDDDFQEDSGWKLNHGDVFRSPSQSLTLSILVGSGVQLFLMVTCSIFFAALGFLSPSSRGSLATVMFILYALFGFVGSYTSMGIYKFFNGPYWKANLILTPLLVPGAILLIIIALNFFLMFVHSSGVIPASTLFFMVFLWFLFSIPLSFAGSLIARKRCHWDEHPTKTNQIARQIPFQPWYLKTIPATLIAGIFPFGSIAVELYFIYTSLWFNKIFYMFGFLFFSFLLLTLTSSLVTILITYHSLCLENWKWQWRGFIIGGAGCALYVFIHSILFTKFKLGGFTTIVLYVGYSSVISLLCCLVTGSIGFISSMLFVRKIYSSIKVD
Protein: Transcription initiation factor TFIID subunit 7 (RNA polymerase II TBP-associated factor subunit F) (Transcription initiation factor TFIID 55 kDa subunit) (TAF(II)55) (TAFII-55) (TAFII55) (Q9R1C0)
Organism: Mus musculus (Mouse)
Function: The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription. TFIID recognizes and binds promoters with or without a TATA box via its subunit TBP, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC). The TFIID complex consists of TBP and TBP-associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13. TAF7 forms a promoter DNA binding subcomplex of TFIID, together with TAF1 and TAF2. Part of a TFIID complex containing TAF10 (TFIID alpha) and a TFIID complex lacking TAF10 (TFIID beta).
Subcellular location: Nucleus {ECO:0000269|PubMed:10438527}.
Interaction partners:
- Transcription initiation factor TFIID subunit 1
- Transcription initiation factor TFIID subunit 2
- TATA-box-binding protein
- Transcription initiation factor TFIID subunit 6
- Transcription initiation factor TFIID subunit 8
- Transcription initiation factor TFIID subunit 10
- Transcription initiation factor TFIID subunit 12
- Transcription initiation factor TFIID subunit 13
- TATA-box binding protein associated factor 4
- Transcription initiation factor TFIID subunit 9
Sequence:
MSKNKDDAPHELESQFILRLPPEYAATVRRAVQSGHVNLKDKLSIELHPDGRHGIVRVDRVPLAAKLVDLPCVTESLKTIDKKTFYKTADISQMLVATVDGDLYPPVEEAAATADPKANKKKDKDKEKKFVWNHGITLPLKNVRKRRFRKTAKKKYIESPDVEKEVKRLLSTDAEAVSTRWEIIAEDETKETENQGLDISSPGMSGHRQGHDSLEHDELREIFNDLSSSSEDEEDVNILDTEEDLERQLQDKLNESDEQHQENEGTNQLVMGIQKQIDNMKGKLQETQDRAKRQEDLIMKVENLALKNRFQAVLDELKQKEDREKEQLSSLQEELESLLEK
Protein: Glycolate permease GlcA (Q46839)
Organism: Escherichia coli (strain K12)
Function: Uptake of glycolate across the membrane. Can also transport L-lactate and D-lactate. Seems to be driven by a proton motive force.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Glycolate oxidase subunit GlcD
- Protein GlcG
- Malate synthase G
- L-lactate dehydrogenase
- Glc operon transcriptional activator
- Glycolate oxidase iron-sulfur subunit
Sequence:
MVTWTQMYMPMGGLGLSALVALIPIIFFFVALAVLRLKGHVAGAITLILSILIAIFAFKMPIDMAFAAAGYGFIYGLWPIAWIIVAAVFLYKLTVASGQFDIIRSSVISITDDQRLQVLLIGFSFGALLEGAAGFGAPVAITGALLVGLGFKPLYAAGLCLIANTAPVAFGALGVPILVAGQVTGIDPFHIGAMAGRQLPFLSVLVPFWLVAMMDGWKGVKETWPAALVAGGSFAVTQFFTSNYIGPELPDITSALVSIVSLALFLKVWRPKNTETAISMGQSAGAMVVNKPSSGGPVPSEYSLGQIIRAWSPFLILTVLVTIWTMKPFKALFAPGGAFYSLVINFQIPHLHQQVLKAAPIVAQPTPMDAVFKFDPLSAGGTAIFIAAIISIFILGVGIKKGIGVFAETLISLKWPILSIGMVLAFAFVTNYSGMSTTLALVLAGTGVMFPFFSPFLGWLGVFLTGSDTSSNALFGSLQSTTAQQINVSDTLLVAANTSGGVTGKMISPQSIAVACAATGMVGRESELFRYTVKHSLIFASVIGIITLLQAYVFTGMLVS
Protein: CD81 antigen (26 kDa cell surface protein TAPA-1) (Target of the antiproliferative antibody 1) (Tetraspanin-28) (Tspan-28) (CD antigen CD81) (P60033)
Organism: Homo sapiens (Human)
Function: Structural component of specialized membrane microdomains known as tetraspanin-enriched microdomains (TERMs), which act as platforms for receptor clustering and signaling. Essential for trafficking and compartmentalization of CD19 receptor on the surface of activated B cells. Upon initial encounter with microbial pathogens, enables the assembly of CD19-CR2/CD21 and B cell receptor (BCR) complexes at signaling TERMs, lowering the threshold dose of antigen required to trigger B cell clonal expansion and antibody production. In T cells, facilitates the localization of CD247/CD3 zeta at antigen-induced synapses with B cells, providing for costimulation and polarization toward T helper type 2 phenotype. Present in MHC class II compartments, may also play a role in antigen presentation. Can act both as positive and negative regulator of homotypic or heterotypic cell-cell fusion processes. Positively regulates sperm-egg fusion and may be involved in acrosome reaction (By similarity). In myoblasts, associates with CD9 and PTGFRN and inhibits myotube fusion during muscle regeneration (By similarity). In macrophages, associates with CD9 and beta-1 and beta-2 integrins, and prevents macrophage fusion into multinucleated giant cells specialized in ingesting complement-opsonized large particles. Also prevents the fusion of mononuclear cell progenitors into osteoclasts in charge of bone resorption (By similarity). May regulate the compartmentalization of enzymatic activities. In T cells, defines the subcellular localization of dNTPase SAMHD1 and permits its degradation by the proteasome, thereby controlling intracellular dNTP levels. Also involved in cell adhesion and motility. Positively regulates integrin-mediated adhesion of macrophages, particularly relevant for the inflammatory response in the lung (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:1383329, ECO:0000269|PubMed:1695320, ECO:0000269|PubMed:20237408, ECO:0000269|PubMed:22307619, ECO:0000269|PubMed:2398277, ECO:0000269|PubMed:26354436}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000269|PubMed:20375010}; Multi-pass membrane protein {ECO:0000255}. Note=Associates with CLDN1 and the CLDN1-CD81 complex localizes to the basolateral cell membrane. {ECO:0000269|PubMed:20375010}.
Interaction partners:
- Prostaglandin F2 receptor negative regulator
- Interferon-induced transmembrane protein 1
- B-lymphocyte antigen CD19
- Claudin-1
- Complement receptor type 2
- Claudin-7
- Immunoglobulin superfamily member 8
- CD9 antigen
- Tumor susceptibility gene 101 protein
- Integrin beta-1
Sequence:
MGVEGCTKCIKYLLFVFNFVFWLAGGVILGVALWLRHDPQTTNLLYLELGDKPAPNTFYVGIYILIAVGAVMMFVGFLGCYGAIQESQCLLGTFFTCLVILFACEVAAGIWGFVNKDQIAKDVKQFYDQALQQAVVDDDANNAKAVVKTFHETLDCCGSSTLTALTTSVLKNNLCPSGSNIISNLFKEDCHQKIDDLFSGKLYLIGIAAIVVAVIMIFEMILSMVLCCGIRNSSVY