wanglab/gogpt-training-data huggingface dataset:
Protein: Peptidyl-prolyl cis-trans isomerase F, mitochondrial (PPIase F) (EC 5.2.1.8) (Cyclophilin D) (CyP-D) (CypD) (Cyclophilin F) (Rotamase F) (Q99KR7)
Organism: Mus musculus (Mouse)
Function: PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding (By similarity). Involved in regulation of the mitochondrial permeability transition pore (mPTP). It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probability of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated. In cooperation with mitochondrial p53/TP53 is involved in activating oxidative stress-induced necrosis. Involved in modulation of mitochondrial membrane F(1)F(0) ATP synthase activity and regulation of mitochondrial matrix adenine nucleotide levels. Has anti-apoptotic activity independently of mPTP and in cooperation with BCL2 inhibits cytochrome c-dependent apoptosis (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P29117}.
Interaction partners:
- ADP/ATP translocase 2
- Non-selective voltage-gated ion channel VDAC1
- ADP/ATP translocase 1
- Cellular tumor antigen p53
- Cytochrome c, somatic
- Cytochrome c, testis-specific
- Mitochondrial inner membrane m-AAA protease component paraplegin
- Hexokinase-2
- Heat shock protein HSP 90-alpha
- Heat shock protein HSP 90-beta
Sequence:
MLALRCGPRLLGLLSGPRSAPLLLSATRTCSDGGARGANSSSGNPLVYLDVGADGQPLGRVVLELKADVVPKTAENFRALCTGEKGFGYKGSTFHRVIPAFMCQAGDFTNHNGTGGRSIYGSRFPDENFTLKHVGPGVLSMANAGPNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDVVKKIESFGSKSGKTSKKIVITDCGQLS
Protein: Proline-rich protein 7 (Synaptic proline-rich membrane protein) (Q3V0I2)
Organism: Mus musculus (Mouse)
Function: Acts as a synapse-to-nucleus messenger to promote NMDA receptor-mediated excitotoxicity in neurons in a JUN-dependent manner (By similarity). Inhibits ubiquitination-mediated degradation and promotes phosphorylation and transcriptional activity of transcription factor JUN (By similarity). Might play a redundant role in the regulation of T cell receptor signaling. Might promote apoptosis in T cells (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q8TB68}; Single-pass type III membrane protein {ECO:0000305}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:P0C6T3}; Single-pass type III membrane protein {ECO:0000305}. Postsynaptic density membrane {ECO:0000250|UniProtKB:P0C6T3}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8TB68}. Synapse {ECO:0000250|UniProtKB:P0C6T3}. Cell projection, dendrite {ECO:0000250|UniProtKB:P0C6T3}. Nucleus {ECO:0000250|UniProtKB:P0C6T3}. Note=Enriched in postsynaptic plasma membrane and postsynaptic densities (PSD). Accumulates in spines along with synapse maturation and colocalizes with DLG4 in a punctate pattern. Translocates from synapses to nuclei following NMDA receptor activity (By similarity). {ECO:0000250|UniProtKB:P0C6T3}.
Interaction partners:
- Proline-rich protein 9
Sequence:
MVMSQGTYTFLTCFAGFWLIWGLIVLLCCFCSFLRRRLKRRQEERLREQNLRALELEPLELEGSLAGSPPGLAPPPPPHRSRLEAPVHAHSHVHVHPLLHHGPAPPHAHPHPHHHALPHPPPPHLAVPPRPWSYPRQAESDMSKPPCYEEAVLMAEPPPPYSEVLTDTRGLYRKIVTPFLSRRDSAEKQEQPPPSYKPLFLDRGYTSALHLPSAPRPAAPCPALCLQAERSRRVFPSWTDSELSSREPLEHGAWRLPVSIPLFGRTTAV
Protein: Acyl-CoA desaturase (EC 1.14.19.1) (Q5B5P5)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Elongation of fatty acids protein
- Acyl-CoA desaturase
- Elongation of fatty acids protein
- Very-long-chain 3-oxoacyl-CoA reductase
- Oleate delta-12 desaturase
- Bifunctional oelate/linoleic acid delta desaturase
- very-long-chain enoyl-CoA reductase
- Very-long-chain
- Membrane-tethered transcription factor
- Uncharacterized protein
Sequence:
MAGSKVVEKGSVDGAPAAKLHITELPMTWSNWYQHVNWLNCFFVLFIPLVGCIGAIWTPLRLHTAIFAIIYYFNAGLGITAGYHRLWAHCCYKATLPLQIYLALAGAGAGQGSIRWWSRGHRAHHRYTDTEKDPYSVRKGFWYSHIGWIIMKQNYKKVGRSDASDLDADPVVIWQHKNYINTALFMTLIFPTLVCGLGWGDWRGGFIYGGILRVFFIQQATNCVNSLAHWIGEQPFDDRNSPRDHVITALVTLGEGYHNFHHEFPSDYRNAIEWWQYDPTKWMIWIWKQVGLAYDLKQFRANEIEKGRLQQMQKKVDARRAALDWGVPLKELPVFSWDEFIAESANRALVAIGGVIHDVSDFIKEHPGGKTFISSAVGKDATAMFNGGVYQHSNAAHNLLAMKRVGVVRGGGEVEIWKDAKQPSKVSFPEMVRAGEQITRRTVPVLDRS
Protein: At2g45510 (Cytochrome P450, family 704, subfamily A, polypeptide 2) (Putative cytochrome P450) (O64631)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- 11-beta-hydroxysteroid dehydrogenase-like 2
- Nucleotide binding protein
- rRNA biogenesis protein RRP36
- Protein BRI1-5 ENHANCED 1
- At1g19540
- Disease resistance protein RPP2B
- Protein STRICTOSIDINE SYNTHASE-LIKE 9
Sequence:
MEILTSIAITVATTIFIVLCFTIYLMIRIFTGKSRNDKRYAPVHATVFDLLFHSDELYDYETEIAREKPTYRFLSPGQSEILTADPRNVEHILKTRFDNYSKGHSSRENMADLLGHGIFAVDGEKWRQQRKLSSFEFSTRVLRDFSCSVFRRNASKLVGFVSEFALSGKAFDAQDLLMRCTLDSIFKVGFGVELKCLDGFSKEGQEFMEAFDEGNVATSSRFIDPLWKLKWFFNIGSQSKLKKSIATIDKFVYSLITTKRKELAKEQNTVVREDILSRFLVESEKDPENMNDKYLRDIILNFMIAGKDTTAALLSWFLYMLCKNPLVQEKIVQEIRDVTFSHEKTTDVNGFVESINEEALDEMHYLHAALSETLRLYPPVPVDMRCAENDDVLPDGHRVSKGDNIYYIAYAMGRMTYIWGQDAEEFKPERWLKDGLFQPESPFKFISFHAGPRICLGKDFAYRQMKIVSMALLHFFRFKMADENSKVYYKRMLTLHVDGGLHLCAIPRTST
Protein: E3 ubiquitin-protein ligase RNF10 (EC 2.3.2.27) (RING finger protein 10) (Q8N5U6)
Organism: Homo sapiens (Human)
Function: Transcriptional factor involved in the regulation of MAG (Myelin-associated glycoprotein) expression. Acts as a regulator of Schwann cell differentiation and myelination.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16335786}. Nucleus {ECO:0000250|UniProtKB:Q5XI59}.
Interaction partners:
Sequence:
MPLSSPNAAATASDMDKNSGSNSSSASSGSSKGQQPPRSASAGPAGESKPKSDGKNSSGSKRYNRKRELSYPKNESFNNQSRRSSSQKSKTFNKMPPQRGGGSSKLFSSSFNGGRRDEVAEAQRAEFSPAQFSGPKKINLNHLLNFTFEPRGQTGHFEGSGHGSWGKRNKWGHKPFNKELFLQANCQFVVSEDQDYTAHFADPDTLVNWDFVEQVRICSHEVPSCPICLYPPTAAKITRCGHIFCWACILHYLSLSEKTWSKCPICYSSVHKKDLKSVVATESHQYVVGDTITMQLMKREKGVLVALPKSKWMNVDHPIHLGDEQHSQYSKLLLASKEQVLHRVVLEEKVALEQQLAEEKHTPESCFIEAAIQELKTREEALSGLAGSRREVTGVVAALEQLVLMAPLAKESVFQPRKGVLEYLSAFDEETTEVCSLDTPSRPLALPLVEEEEAVSEPEPEGLPEACDDLELADDNLKEGTICTESSQQEPITKSGFTRLSSSPCYYFYQAEDGQHMFLHPVNVRCLVREYGSLERSPEKISATVVEIAGYSMSEDVRQRHRYLSHLPLTCEFSICELALQPPVVSKETLEMFSDDIEKRKRQRQKKAREERRRERRIEIEENKKQGKYPEVHIPLENLQQFPAFNSYTCSSDSALGPTSTEGHGALSISPLSRSPGSHADFLLTPLSPTASQGSPSFCVGSLEEDSPFPSFAQMLRVGKAKADVWPKTAPKKDENSLVPPAPVDSDGESDNSDRVPVPSFQNSFSQAIEAAFMKLDTPATSDPLSEEKGGKKRKKQKQKLLFSTSVVHTK
Protein: Homeobox protein Hox-B2 (Homeobox protein Hox-2.8) (P0C1T1)
Organism: Mus musculus (Mouse)
Function: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
Interaction partners:
- Homeobox protein Hox-B5
- Homeobox protein Hox-B3
- Homeobox protein Hox-B6
- Homeobox protein Hox-B8
Sequence:
MNFEFEREIGFINSQPSLAECLTSFPAVLETFQTSSIKESTLIPPPPPLEQTFPSLQLGASTLQRPGSQKQAGDGPALRSPPPLPVAPPAPEFPWMKEKKSTKKPSQSAASPSPAASSVRASEVGSPSDGPGLPECGGSGSRRLRTAYTNTQLLELEKEFHFNKYLCRPRRVEIAALLDLTERQVKVWFQNRRMKHKRQTQHREPPEGEPGGPSAQDDAGEPAEEPTVSPGDVATHRLREACFHPAEAAQGPRGAPPSALPATTLESVGASSPGCTMLRAGGRQSEPLPEDACPERQDSPFLPDLNFFAADSCLQMSGGLSPSLQGSLDSPVPFSEEELDFFTSTLCAIDLQFP
Protein: Non-specific lipid transfer protein GPI-anchored 2 (AtLTPG-2) (Protein LTP-GPI-ANCHORED 2) (Xylogen-like protein 10) (AtXYLP10) (AtXYP5) (Q9LZH5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Lipid transfer protein that, together with LTPG1, binds to lipids and functions as a component of the cuticular lipid export machinery that performs extensive export of intracellular lipids (e.g. C29 alkane) from epidermal cells to the surface to build the cuticular wax layer and silique walls. Contributes to pre-invasive defense against some non-host powdery mildew pathogens by preventing the penetration of the epidermal cell wall by the fungal agents (e.g. Blumeria graminis f. sp. hordei (Bgh)). Involved in seed and ovule maturation and development, probably by regulating the fatty acids homeostasis during suberin and sporopollenin biosynthesis or deposition.
Subcellular location: Cell membrane {ECO:0000269|PubMed:22891199}; Lipid-anchor, GPI-anchor {ECO:0000255}. Note=Targeted to the plasma membrane via the vesicular trafficking system. {ECO:0000269|PubMed:22891199}.
Interaction partners:
- Probable pectinesterase/pectinesterase inhibitor 44
- ABC transporter G family member 11
- Non-specific lipid-transfer protein 5
- ABC transporter G family member 12
- At5g02890
- ABC transporter G family member 13
- Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein
Sequence:
MSNVVVIAVVLIVASLTGHVSAQMDMSPSSGPSGAPDCMANLMNMTGCLSYVTVGEGGGAAKPDKTCCPALAGLVESSPQCLCYLLSGDMAAQLGIKIDKAKALKLPGVCGVITPDPSLCSLFGIPVGAPVAMGDEGASPAYAPGSMSGAESPGGFGSGPSASRGSDAPSSAPYSLFLNLIIFPLAFAFYIFC
Protein: E3 ubiquitin-protein ligase (EC 2.3.2.26) (A0A0B4LGQ5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus, nucleoplasm {ECO:0000256|ARBA:ARBA00004642}.
Interaction partners:
Sequence:
MAESVKSQSLSALTEGQHDDGGSTATSATLANKTSGTNTTSASNHSSQRRRNNNTNSNRNKSHHKNEKRNAPATSGPAVSSSVDVVPATSTASATSTRRSRSQGRHSSAAALSSKESQIPKRSVGAIRSPSSPAFNSIPVVSDQSLSPGSRKRQLNQHNNSNNKASSSHQSAPGGDQLVCAPLKKRRLQQSLGSGICEGAVEINLGAASFDHTPRQASGDCVAQRTRSKTISPEELPSTSSAAAARHHQIRPSASSTSFSSSHRNKRKASIGGSIAAVETTPHRGTAAARAGRSGNLLNYYRKTRKVSHTRSSQKSEKQSIPAEDTTANRNGSAGSGSSSKSGVIPKNRKSLRHSQQNLLDTEAAEVESAAAETGGEQQSEHGNLDVIDQLPTPEAGPNQSEASGIHNQSQLEADRQPVVQDEDDEEDDEEEEEEEEEEVGFYGIVNSAGSSYEEDTQIVAEEDEITTEEEVDDEDDDEIEEEDLSESEFAQQLIGELGGAGPPPALFQQQAPPQLTRYTPATATTAATFVPPQQQQVVYNPQQQQHSSLRRSSRGKTGSCVSSAAAAQQQQHHQQQQHSSAAAAVQQQLLPPPGTYQYQQVGGNTVVVAVRHQQQLQQQQQQQQQLALHHQHQQQQHQQQQQQHQQQQHQQQQRATLVQPGFLFSYRSNQPQQQQQPAQQIHQGPKVTHSSGANSANLSIVAAALSAARDVGGGSDGGGSAGGATPATGASASSVGNTSAVGASSSSNSSAGQAASSNSNNVTATGSGSAPGGGPTSTGTTSGTQHGSGSGAAAAVDSESDDSEVGRLQALLEARGLPPHLFGALGPRVTHILHRTIGNSSSSKANQLLQGLQSHDESQQLQAAIEMCQMLVMGNEDTLAGFPIKQVVPALIQLLRMEHNFDIMNNACRALAYMLEALPRSSGTVVEAVPVFLEKLQVIQCMDVAEQSLSALEILSRRHNKAILQANGISACLTYLDFFSIVAQRAALAIAANCCLNMHPEEFHFVAESLPLLARLLSQQDKKCIESVCSAFCRLVESFQHDGQRLQQIASPDLLKNCQQLLLVTPAILNTGTFTAVVRMLSLMCCSCPDLAISLLRNDIAATLLYLLTGNAEPAAASATHVELISRSPSELYELTCLIGELMPRLPLDGIFAVDSLLDRPTLNTQDQVHWQWRDDRGSWHNYSTIDSRLIEAANQSSEDEISLSTFGRTYTVDFHAMQQINEDTGTTRPVQRRLNHNYVAPMSAGQDLTTTSAGSAAAGGASTSAAAAAASSNNNNNNNNNPPGNSVNLNQVKRRPSLDARIACLKEERGLAADFIKHIFNVLYEVYSSSAGPNVRYKCLRALLRMVYYATPELLRQVLKYQLVSSHIAGMLGSNDLRIVVGALQMAEILMRQLPDVFGTHFRREGVIYQFTQLTDPNNPICANPSPKPLSATATPTANAGGSQSAPASANSLQVNPFFMDSAPGLSSASTTPSSSKHQSYSVKSFSHAMNALTASAKGTPSGALDATSSSTTAGGYNYSSSAPSSSSGAPAAYFVTQQGDPRQYVHFQQPAVPAPPPQQELLPSGVQQQGQQVPQVIYQPHHQQPAHLVLASTSSGAASSSSSSSSSSSASALQHKMTDMLKRKAPPKRKSQSGGRAKSRQEDAAVAPAGSGPGGAPPSSSGSAMHELLSRATSLGSGNGGRSTPNSGGGSGSSKSRFNAGNSSNAGSSKSSFLASLNPARWGRQTHQNHHHHHQQSQQQHHGLSKDSGNSNSTGSGSGAGLAYTVSQHGAGSGAGGLNAAAVAASISKSISHANLLAAANRERARQWVREQAVDFVKRYTEQEAKRSKAASESGATQSGSSGVGLSSTGNTPLSTAGSTNVLERLSSILFKLNGSYHDCLDALLELKTILLESDISPFEVNHSGLIKAMLNYMTSETGLVERDARLRSFMHVFAGLPLEPLLQNVGQMPTIEPIAFGAFVAKLNGCVTQLEQFPVKVHDFPAGPGGRSNQSALRFFNTHQLKCNLQRHPQCNNLRQWKGGTVKIDPLAMVQAIERYLVVRGYGGIRADSDDDSEEDMDDNVAAVVLSQASFRHKLQFTIGDHVLPYNMTVYQAVKQFSPLVSEQPETDNESETLLGNASIWVQQHTIHYRPVEEEVTSGAAAGAASSSSSCSSGVQKQQSSSSSASSCVNATSSCSSSSGVASGGGSLTKKAHKSSSKFMRKKTELWHEGIAPVVISALKPFLSSSLPADVVTVQDASLDALCMLRVIHALNRHWDHLYGCVVRQNIIPQSDFIHPKIMAKANRQLQDPLVIMTGNLPQWLPQIGMACPFLFPFETRHLLFYATSFDRDRALQRLLDTTPDLNAAESSERVAPRLDRRKRAISRTEILKQAEHILQDFGHSKALLEIQYENEVGTGLGPTLEFYALVSAELQRTDLGLWNGSDSYKQNSVTIVDVVKANSAVLHIEDALEATTTDQNTPAVAGASLVSSSTTTTTTTAQQHQHPPTRSSSRSHVLRSGAGQQPVEHSSSSAGANENALNMVIAQQFSDTNSANPAAIDNPSSTTTATTVVQHNTTTNNSSIITTTTTTSYVHAVHGLFPLPLGKSSKLPQMTKAKAKFKFLGKFMAKAVMDSRMLDLPFSLPFYRWLVSEEHSIGLADLMRVAPEVQNTLVRLQDLVRQREYILSDPNIDAMEKTEKIEQLDLDGCPIADLGLDFVLPGHANIELCRGGRDTPVTVHNLHQYISLVTYWFLIEGVQKQFEALREGFDSVFPIQRLRMFYPEELECVFCGSGSEQQHSRWEIKMLQESCRTDHGFHQDSQAIQYLYEILASYNRDEQRAFLQFVTGSPRLPTGGFKALTPPLTIVRKTLDENQNPNDYLPSVMTCVNYLKLPDYSSREVMRQKLKVAANEGSMSFHLS
Protein: QueE (E7DN68)
Organism: Pneumococcus phage Dp-1 (Bacteriophage Dp-1)
Interaction partners:
Sequence:
MVNQYNQPERGKIRINVRDPEKMPIMEIFGPTIQGEGMVIGQKTIFIRTGGCDYHCNWCDSAFTWNGTTEPEYITGKEAASRILKLAFNDKGEQICNHVTLTGGNPALINEPMAKMISILKEHGFKFGLETQGTRFQEWFKEVSDITISPKPPSSGMRTNMKILEAIVDRMNDENLDWSFKIVIFDENDLAYARDMFKTFEGKLRPVNYLSVGNANAYEEGKISDRLLEKLGWLWDKVYEDPAFNNVRPLPQLHTLVYDNKRGV
Protein: Undecaprenyl phosphate N,N'-diacetylbacillosamine 1-phosphate transferase (EC 2.7.8.36) (Protein glycosylation C) (Q0P9D0)
Organism: Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Function: Glycosyl-1-phosphate transferase that mediates the first step in the biosynthesis of the undecaprenyl-linked heptasaccharide donor in the N-linked protein glycosylation pathway. Catalyzes the linking of uridine 5'-diphosphobacillosamine (UDP-Bac) to undecaprenyl phosphate to create the first membrane-associated intermediate undecaprenylpyrophosphate-linked Bac (Und-PP-Bac).
Subcellular location: Membrane {ECO:0000305|PubMed:16618123}; Single-pass membrane protein {ECO:0000305|PubMed:16618123}.
Interaction partners:
- UDP-N-acetylbacillosamine N-acetyltransferase
- N,N'-diacetylbacillosaminyl-diphospho-undecaprenol alpha-1,3-N-acetylgalactosaminyltransferase
- N-acetylgalactosamine-N,N'-diacetylbacillosaminyl-diphospho-undecaprenol 4-alpha-N-acetylgalactosaminyltransferase
- GalNAc-alpha-
- UDP-N-acetylbacillosamine transaminase
- GalNAc
- Protein glycosylation K
- Undecaprenyl-diphosphooligosaccharide--protein glycotransferase
- UDP-N-acetyl-alpha-D-glucosamine C6 dehydratase
- UDP-glucose 4-epimerase
Sequence:
MYEKVFKRIFDFILALVLLVLFSPVILITALLLKITQGSVIFTQNRPGLDEKIFKIYKFKTMSDERDEKGELLSDELRLKAFGKIVRSLSLDELLQLFNVLKGDMSFVGPRPLLVEYLPLYNKEQKLRHKVRPGITGWAQVNGRNAISWQKKFELDVYYVKNISFLLDLKIMFLTALKVLKRSGVSKEGHVTTEKFNGKN
Protein: Doublesex- and mab-3-related transcription factor 2 (Doublesex-like 2 protein) (DSXL-2) (Q9Y5R5)
Organism: Homo sapiens (Human)
Function: Transcriptional activator that directly regulates early activation of the myogenic determination gene MYF5 by binding in a sequence-specific manner to the early epaxial enhancer element of it. Involved in somitogenesis during embryogenesis and somite development and differentiation into sclerotome and dermomyotome. Required for the initiation and/or maintenance of proper organization of the sclerotome, dermomyotome and myotome (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00070}.
Interaction partners:
- Sex-determining region Y protein
Sequence:
MADPQAGSAAGDWEIDVESLELEEDVCGAPRSTPPGPSPPPADGDCEDDEDDDGVDEDAEEEGDGEEAGASPGMPGQPEQRGGPQPRPPLAPQASPAGTGPRERCTPAGGGAEPRKLSRTPKCARCRNHGVVSCLKGHKRFCRWRDCQCANCLLVVERQRVMAAQVALRRQQATEDKKGLSGKQNNFERKAVYQRQVRAPSLLAKSILEGYRPIPAETYVGGTFPLPPPVSDRMRKRRAFADKELENIMLEREYKEREMLETSQAAALFLPNRMVPGPDYNSYKSAYSPSPVEPPSKDFCNFLPTCLDLTMQYSGSGNMELISSNVSVATTYRQYPLSSRFLVWPKCGPISDTLLYQQCLLNATTSVQALKPGASWDLKGARVQDGLSAEQDMMPSKLEGSLVLPHTPEIQTTRSDLQGHQAVPERSAFSPPRRNFSPIVDTDSLAAQGHVLTKISKENTRHPLPLRHNPFHSLFQQTLTDKSGPELKTPFVKEAFEETPKKHRECLVKDNQKYTFTIDRCAKDLFVAKQVGTKLSVNEPLSFSVESILKRPSSAITRVSQ
Protein: NUT family member 1 (Nuclear protein in testis) (Q86Y26)
Organism: Homo sapiens (Human)
Function: Plays a role in the regulation of proliferation. Regulates TERT expression by modulating SP1 binding to TERT promoter binding sites.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17934517}. Nucleus {ECO:0000269|PubMed:17934517}. Note=Shuttles between nucleus and cytoplasm. {ECO:0000269|PubMed:17934517}.
Interaction partners:
- Bromodomain-containing protein 4
- Histone acetyltransferase p300
- Histone-lysine N-methyltransferase NSD3
- Bromodomain-containing protein 3
- Zinc finger protein 532
- H/ACA ribonucleoprotein complex subunit 3
Sequence:
MASDGASALPGPDMSMKPSAAPSPSPALPFLPPTSDPPDHPPREPPPQPIMPSVFSPDNPLMLSAFPSSLLVTGDGGPCLSGAGAGKVIVKVKTEGGSAEPSQTQNFILTQTALNSTAPGTPCGGLEGPAPPFVTASNVKTILPSKAVGVSQEGPPGLPPQPPPPVAQLVPIVPLEKAWPGPHGTTGEGGPVATLSKPSLGDRSKISKDVYENFRQWQRYKALARRHLSQSPDTEALSCFLIPVLRSLARLKPTMTLEEGLPLAVQEWEHTSNFDRMIFYEMAERFMEFEAEEMQIQNTQLMNGSQGLSPATPLKLDPLGPLASEVCQQPVYIPKKAASKTRAPRRRQRKAQRPPAPEAPKEIPPEAVKEYVDIMEWLVGTHLATGESDGKQEEEGQQQEEEGMYPDPGLLSYINELCSQKVFVSKVEAVIHPQFLADLLSPEKQRDPLALIEELEQEEGLTLAQLVQKRLMALEEEEDAEAPPSFSGAQLDSSPSGSVEDEDGDGRLRPSPGLQGAGGAACLGKVSSSGKRAREVHGGQEQALDSPRGMHRDGNTLPSPSSWDLQPELAAPQGTPGPLGVERRGSGKVINQVSLHQDGHLGGAGPPGHCLVADRTSEALPLCWQGGFQPESTPSLDAGLAELAPLQGQGLEKQVLGLQKGQQTGGRGVLPQGKEPLAVPWEGSSGAMWGDDRGTPMAQSYDQNPSPRAAGERDDVCLSPGVWLSSEMDAVGLELPVQIEEVIESFQVEKCVTEYQEGCQGLGSRGNISLGPGETLVPGDTESSVIPCGGTVAAAALEKRNYCSLPGPLRANSPPLRSKENQEQSCETVGHPSDLWAEGCFPLLESGDSTLGSSKETLPPTCQGNLLIMGTEDASSLPEASQEAGSRGNSFSPLLETIEPVNILDVKDDCGLQLRVSEDTCPLNVHSYDPQGEGRVDPDLSKPKNLAPLQESQESYTTGTPKATSSHQGLGSTLPRRGTRNAIVPRETSVSKTHRSADRAKGKEKKKKEAEEEDEELSNFAYLLASKLSLSPREHPLSPHHASGGQGSQRASHLLPAGAKGPSKLPYPVAKSGKRALAGGPAPTEKTPHSGAQLGVPREKPLALGVVRPSQPRKRRCDSFVTGRRKKRRRSQ
Protein: Dirigent protein 5 (AtDIR5) (Q9SH66)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Dirigent proteins impart stereoselectivity on the phenoxy radical-coupling reaction, yielding optically active lignans from two molecules of coniferyl alcohol in the biosynthesis of lignans, flavonolignans, and alkaloids and thus plays a central role in plant secondary metabolism. Enantiocomplementary dirigent protein that mediates the laccase-catalyzed enantioselective oxidative phenol coupling of (E)-coniferyl alcohol to (-)-pinoresinol.
Subcellular location: Secreted, extracellular space, apoplast {ECO:0000250}.
Interaction partners:
- Dirigent protein 9
- Dirigent protein 25
- Dirigent protein 16
- Dirigent protein 10
- Dirigent protein 24
- Dirigent protein 18
- Dirigent protein 4
- AT3g16670/MGL6_12
- Plant invertase/pectin methylesterase inhibitor superfamily protein
Sequence:
MVGQMKSFLFLFVFLVLTKTVISARKPSKSQPKPCKNFVLYYHDIMFGVDDVQNATSAAVTNPPGLGNFKFGKLVIFDDPMTIDKNFQSEPVARAQGFYFYDMKNDYNAWFAYTLVFNSTQHKGTLNIMGADLMMVQSRDLSVVGGTGDFFMSRGIVTFETDTFEGAKYFRVKMDIKLYECY
Protein: Zinc finger FYVE-type containing 1 (G3V5N8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSAQTSPAEKGLNPGLMCQESYACSGTDEAIFECDECCSLQCLRCEEELHRQERLRNHERIRLKPGHVPYCDLCKGLSGHLPGVRQRAIVRCQTCKINLCLECQKRTHSGGNKRRHPVTVYNVSNLQESLEAEEMDEETKRKKMTEKVVSFLLVDENEEIQVTNEEDFIRKLDCKPDQHLKVVSIFGNTGDGKSHTLNHTFFYGREVFKTSPTQESCTVGVWAAYDPVHKVAVIDTEGLLGATVNLSQRTRLLLKVLAISDLVIYRTHADRLHNDLFKFLGDASEAYLKHFTKELKATTARCGLDVPLSTLGPAVIIFHETVHTQLLGSDHPSEVPEKLIQDRFRKLGRFPEAFSSIHYKGTRTYNPPTDFSGLRRALEQLLENNTTRSPRHPGVIFKALKALSDRFSGEIPDDQMAHSSFFPDEYFTCSSLCLSCGVGCKKSMNHGKEGVPHEAKSRCRYSHQYDNRVYTCKACYERGEEVSVVPKTSASTDSPWMGLAKYAWSGYVIECPNCGVVYRSRQYWFGNQDPVDTVVRTEIVHVWPGTDGFLKDNNNAAQRLLDGMNFMAQSVSELSLGPTKAVTSWLTDQIAPAYWRPNSQILSCNKCATSFKDNDTKHHCRACGEGFCDSCSSKTRPVPERGWGPAPVRVCDNCYEARNVQLAVTEAQVDDEGGTLIARKVGEAVQNTLGAVVTAIDIPLGLVKDAARPAYWVPDHEILHCHNCRKEFSIKLSKHHCRACGQGFCDECSHDRRAVPSRGWDHPVRVCFNCNKKPAWTSLSVMTGKGPLC
Protein: Actin-related protein 3 (Actin-like protein 3) (Q9N4I0)
Organism: Caenorhabditis elegans
Function: Functions as ATP-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the pointed end of the daughter actin filament (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- Probable actin-related protein 2/3 complex subunit 2
- Actin-related protein 2/3 complex subunit
- Probable actin-related protein 2/3 complex subunit 3
- Actin-related protein 2/3 complex subunit 5
- Actin-related protein 2
- Probable actin-related protein 2/3 complex subunit 4
- Probable actin-related protein 2/3 complex subunit 5
- CRIB domain-containing protein
- SPIN90/Ldb17 leucine-rich domain-containing protein
- WH1 domain-containing protein
Sequence:
MSAHQLPACVIDNGTGYTKLGYAGNTEPQFIIPSAIAVKDKVASSNSQAMRWNNRVGAGIDDLDFFIGDEALSPAATNYTVKYPIRHGIVEDWDLMERYWEQCIFKYLRAEPEDHFFLLTEPPLNTPENREYTAEIMFESFNVPGLYIAVQAVLALTASWNSREANERSLTGLVIDSGDGVTHCIPVADGYVIGSCIKHIPIAGRDITYFIQSLLRDREHTIPAEQSYEVAKMIKEKFCYVCPDVMKEFVKYDTDAAKWLRTYDGINSITKKPFNVDVGYERFLGPEIFFHPEFCNPEFTTPISDTIDTLIQQCPIDVRRGLYENIVLSGGSTMFKDFARKLQRDVKRLSDGRLQMSETLSGGRLKPKPIDVQVISHKMQRYAVWFGGSMLASTSEFYQVSHTKAEYMERGPSICRYNPVFGALT
Protein: 2'-deoxymugineic-acid 2'-dioxygenase (EC 1.14.11.24) (Protein iron deficiency-specific 3) (Q40062)
Organism: Hordeum vulgare (Barley)
Function: Involved in the biosynthesis of mugineic acid family of phytosiderophores. Hydroxylates the C-2' positions of 2'-deoxymugineic acid (DMA) and 3-epihydroxymugineic acid (epiHDMA). May be involved in boron tolerance.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
Sequence:
MENILHATPAHVSLPESFVFASDKVPPATKAVVSLPIIDLSCGRDEVRRSILEAGKELGFFQVVNHGVSKQVMRDMEGMCEQFFHLPAADKASLYSEERHKPNRLFSGATYDTGGEKYWRDCLRLACPFPVDDSINEWPDTPKGLRDVIEKFTSQTRDVGKELLRLLCEGMGIQADYFEGDLSGGNVILNINHYPSCPNPDKALGQPPHCDRNLITLLLPGAVNGLEVSYKGDWIKVDPAPNAFVVNFGQQLEVVTNGLLKSIEHRAMTNSALARTSVATFIMPTQECLIGPAKEFLSKENPPCYRTTMFRDFMRIYNVVKLGSSLNLTTNLKNVQKEI
Protein: Threonine aldolase (A0A1D8PSW2)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Serine hydroxymethyltransferase, cytosolic
- Serine hydroxymethyltransferase
- Glycine cleavage system P protein
- Threonine synthase
- Threonine dehydratase
- L-serine ammonia-lyase
- L-serine ammonia-lyase
- 5-aminolevulinate synthase, mitochondrial
- Dao1p
- Ifg3p
Sequence:
MDFSTFDKQSPAHNDFRSDTFTTPTTSMIQSLAQTTLGDAVYNEDLKTIELEQKVAELTGKEAGLYCVSGTLSNQIAIRTNLYQPPFSVLCDYRAHVYVHEAGGLSTLSQAMAQPINPKNGIHLTLEDDILPNFIIDDGEIHGAPTKLICLENTLHGMIFPIEEIKKISKFCQQNNVKLHLDGARIWNASAETGISLKEYCSYFDSVSLCLSKTLGAPIGTVLVSDKKFILKANHFKKQNGGGIRQSGLLASMAIIAIDENFSKLKQTHIWAKELGKLCDENGIILEHPVQTNFVFIDIAANKINPEKLMEISDKYNVKIYSGRIAFHYQISQESFENAKKVVLEVIQYAKDHPYEEKTNFKFYTSENK
Protein: Nuclear Hormone Receptor family (O16346)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- C2H2-type domain-containing protein
- Seven TM Receptor
- Major sperm protein
- glucuronosyltransferase
- Nuclear hormone receptor family member nhr-49
- Nuclear receptor domain-containing protein
Sequence:
MLTSFLDPRPSSSSSSVSTSSMSSSPSTSSESCAVCGDSVNGKRYGAPACLGCIVFFRRAVINKSQYKCWKKGNCVITFASRCVCRCCRLRKCSHVGMKPEAIQRRDLLGPRKPKTILTNDISQSIDVALNFLSSPHSSCESDTGEYSNTTFDIDSLVRLQHDQRSQHEAYGIHHIDTIGCFQMKNSGKYHKRARASDINFVLKLGLENANEWGNQFEPYRRLSQTDKNSVLSEFGFAFLLIDQGYKTAQRADEGFWLLQNETFMHPNYFFALSVEDAMKENAEQKAELHHSFVNELVKCVSDPFKNLHIDEFECAILKTVLLLTPSFPGHVTYKDLQYLHNKCMSELMDHSIQRSPDAGPERFGEIILLISSIRCGVKAIYNQTRVSDMFHLMTFDPYVRNILLS
Protein: CD163 molecule (D3Z9U2)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Haptoglobin
- Macrosialin
- Macrophage mannose receptor 1
- Arginase-1
- Interleukin-6
- C-C motif chemokine 2
- Pancreatic secretory granule membrane major glycoprotein GP2
- Interleukin-10
- Hemopexin
- Macrophage colony-stimulating factor 1 receptor
Sequence:
MGKNRMVLLGGAGSPGYKGFVHLGFFVVAVSSLLSVSAVTQAPEGRKKELRLAGGENNCSGRVELKIHEKWGTVCGNGWSMNEVSVVCQQLGCPTLIKAPGWANASAGSGDIWMDKVSCTGNESALWDCKHEGWGKHNCTHEQDAGVTCADGSNLEMRLVNSGDNRCSGRVEIKFQGKWGTVCDDNFSKDHASVICKQLGCGSAISFSGSAKLGAGSGQIWLDDLACNGNESAIWDCKHRGWGRHNCDHAEDVGVICLDGADLSLRLVDGVSKCSGRLEVRFQGEWGTVCDDSWDRRDASVVCKQLGCPTAITAIGRVNASEGSGPIWLDSISCEGHEPALWECKHQEWGKHYCNHKEDAGVTCSDGADLELRLVGGGSRCAGMVEVEIQKLTGKVCSRGWTLTDADVVCRQLGCGSALQTQSKIYSKTKTEATNTWLFPGSCSGNETSLWQCKNWQWGGLSCDHFEEAQVTCSGHRKPRLVGGEIPCSGRVEVKHGDTWGSVCDFDLSLEAAGVVCRELQCGTVVSILGGAHFGEGSGQIWGEEFQCSGDESHLSLCSVAPPLDRTCSHSRDVSIVCSRYIDIRLADGKSSCEGRVELKTLGAWGPLCSSHWDIEDAHVLCQQLKCGVALSTPGGAHFGKGAGQVWRHKFHCTGTEEHIGDCPMTALGTPMCSDGQVASVICSGNQSHTLLPCSSSSSVQTTSSTIAKDSDVPCIASGQLRLVGGGGRCAGRVEVYHEGSWGTICDDSWDLTDANVVCKQLDCGVAINATGSAYFGEGTGDIWLDEIDCSGKESHIWQCHSHGWGRHNCRHKEDAGVVCSEFMSLRLTNEAHRVNCTGRLEVFYNGTWGSIGSSNMSPTTVGVVCRQLGCADNGTVKPTSSDKTPTRPMWTDSVQCPKGVDTLWQCPSSPWKQRQASPSQESWIVCDDKIRLQEGHTDCSGRVEIWHRGSWGTVCDDSWDLNDAEVACKQLGCGQAVEALKEAAFGPGTGPIWLNEMKCRGNESSLWDCPARPWSHSDCGHKEDASVKCLPRMTLESQHGTGHSTLTALLVCGAILLVLLIAFLLWTLKRRQTQRLTVSSRGEVLIHQVQYQEMDSKTDDLDLLKSSGQ