wanglab/gogpt-training-data huggingface dataset:
Protein: Carboxypeptidase E (CPE) (EC 3.4.17.10) (Carboxypeptidase H) (CPH) (Enkephalin convertase) (Prohormone-processing carboxypeptidase) (P16870)
Organism: Homo sapiens (Human)
Function: Sorting receptor that directs prohormones to the regulated secretory pathway. Acts also as a prohormone processing enzyme in neuro/endocrine cells, removing dibasic residues from the C-terminal end of peptide hormone precursors after initial endoprotease cleavage.
Subcellular location: [Isoform 1]: Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniProtKB:Q00493}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:P15087}; Peripheral membrane protein {ECO:0000250|UniProtKB:P15087}. Secreted {ECO:0000250|UniProtKB:P15087}. Note=Associated with the secretory granule membrane through direct binding to lipid rafts in intragranular conditions. {ECO:0000250|UniProtKB:Q00493}.
Interaction partners:
- Pro-opiomelanocortin
- Insulin
- ProSAAS
- Neuroendocrine convertase 1
- Chromogranin-A
- Neuroendocrine convertase 2
- Carboxypeptidase B
- Carboxypeptidase B2
- Secretogranin-3
- Secretogranin-2
Sequence:
MAGRGGSALLALCGALAACGWLLGAEAQEPGAPAAGMRRRRRLQQEDGISFEYHRYPELREALVSVWLQCTAISRIYTVGRSFEGRELLVIELSDNPGVHEPGEPEFKYIGNMHGNEAVGRELLIFLAQYLCNEYQKGNETIVNLIHSTRIHIMPSLNPDGFEKAASQPGELKDWFVGRSNAQGIDLNRNFPDLDRIVYVNEKEGGPNNHLLKNMKKIVDQNTKLAPETKAVIHWIMDIPFVLSANLHGGDLVANYPYDETRSGSAHEYSSSPDDAIFQSLARAYSSFNPAMSDPNRPPCRKNDDDSSFVDGTTNGGAWYSVPGGMQDFNYLSSNCFEITVELSCEKFPPEETLKTYWEDNKNSLISYLEQIHRGVKGFVRDLQGNPIANATISVEGIDHDVTSAKDGDYWRLLIPGNYKLTASAPGYLAITKKVAVPYSPAAGVDFELESFSERKEEEKEELMEWWKMMSETLNF
Protein: Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 3 (EC 4.2.1.134) (3-hydroxyacyl-CoA dehydratase 3) (HACD3) (Butyrate-induced protein 1) (B-ind1) (Protein-tyrosine phosphatase-like A domain-containing protein 1) (Q8K2C9)
Organism: Mus musculus (Mouse)
Function: Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. Thereby, it participates in the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. Involved in Rac1-signaling pathways leading to the modulation of gene expression. Promotes insulin receptor/INSR autophosphorylation and is involved in INSR internalization (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9P035}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9P035}.
Interaction partners:
- Very-long-chain enoyl-CoA reductase
- Very-long-chain 3-oxoacyl-CoA reductase
- Very long chain fatty acid elongase 5
- Very long chain fatty acid elongase 4
- Very long chain fatty acid elongase 2
- Very-long-chain
- Very-long-chain
- Acyl-CoA
- Very-long-chain
- Trans-2,3-enoyl-CoA reductase-like
Sequence:
METQVLTPHVYWAQRHRELYLRVELSDVQNPAISITDNVLHFKAQGHGAKGDNVYEFHLEFLDLVKPEPAYRLTQRQVNITVQKKGSHWWERLTKQEKRPLFLAPDFDRWLDESDAEMELRAKEEERLNKLRLEREGSPETLTNLKKGYLFMYNLVQLLGFSWIFVNLTVRFFILGKESFYDTFHNVADMMYFCQMLALVETLNAAIGVTSTPVLPALIQFLGRNFILFLVFGTMEEMQNKAVVFFVFYSWSAIEIFRYPFYMLSCIDMDWKVLTWLRYTMWIPLYPLGCLSEAVAVIQSIPVFNESGRFSFTLPYPVKMKVRFSFFLQVYLVMLFLGLYINFRHLYKQRRRRYGQKKKKLH
Protein: Zinc finger protein 713 (Q8N859)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MPSQNAVFSQEGNMEEEEMNDGSQMVRSQESLTFQDVAVDFTREEWDQLYPAQKNLYRDVMLENYRNLVALGYQLCKPEVIAQLELEEEWVIERDSLLDTHPDGENRPEIKKSTTSQNISDENQTHEMIMERLAGDSFWYSILGGLWDFDYHPEFNQENHKRYLGQVTLTHKKITQERSLECNKFAENCNLNSNLMQQRIPSIKIPLNSDTQGNSIKHNSDLIYYQGNYVRETPYEYSECGKIFNQHILLTDHIHTAEKPSECGKAFSHTSSLSQPQMLLTGEKPYKCDECGKRFSQRIHLIQHQRIHTGEKPFICNGCGKAFRQHSSFTQHLRIHTGEKPYKCNQCGKAFSRITSLTEHHRLHTGEKPYECGFCGKAFSQRTHLNQHERTHTGEKPYKCNECGKAFSQSAHLNQHRKIHTREKLCEYKCEQTVRHSPSFSST
Protein: Sulfite reductase, dissimilatory-type subunit alpha (Desulfoviridin subunit alpha) (Dissimilatory sulfite reductase subunit alpha) (dSiR alpha) (Hydrogensulfite reductase subunit alpha) (P45574)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Function: Part of the complex that catalyzes the reduction of sulfite to sulfide. The alpha and beta subunits may have arisen by gene duplication. They both bind 2 iron-sulfur clusters, but the alpha subunit seems to be catalytically inactive, due to substitutions along the putative substrate access channel, and because it binds sirohydrochlorin (the dematallated form of siroheme) instead of siroheme.
Interaction partners:
- Sulfite reductase, dissimilatory-type subunit gamma
- Sulfite reductase, dissimilatory-type subunit beta
- Adenylylsulphate reductase, beta subunit
- Adenylyl-sulphate reductase, alpha subunit
- Protein DsvD
- Cysteine synthase
- Thiosulfate reductase, putative
- Carbon monoxide dehydrogenase
- Phosphoadenosine phosphosulfate reductase, putative
- cytochrome-c3 hydrogenase
Sequence:
MAKHATPKLDQLESGPWPSFVSDIKQEAAYRAANPKGLDYQVPVDCPEDLLGVLELSYDEGETHWKHGGIVGVFGYGGGVIGRYCDQPEKFPGVAHFHTVRVAQPSGKYYSADYLRQLCDIWDLRGSGLTNMHGSTGDIVLLGTQTPQLEEIFFELTHNLNTDLGGSGSNLRTPESCLGKSRCEFACYDSQAACYELTMEYQDELHRPAFPYKFKFKFDACPNGCVASIARSDFSVIGTWKDDIKIDAEAVKAYVAGEFKPNAGAHSGRDWGKFDIEAEVVNRCPSKCMKWDGSKLSIDNKECVRCMHCINTMPRALHIGDERGASILCGAKAPILDGAQMGSLLVPFVAAEEPFDEIKEVVEKIWDWWMEEGKNRERLGETMKRLSFQKLLEVTEIAPVPQHVKEPRTNPYIFFKEEEVPGGWDRDITEYRKRHLR
Protein: 4-aminobutyrate aminotransferase, mitochondrial (EC 2.6.1.19) (EC 2.6.1.22) ((S)-3-amino-2-methylpropionate transaminase) (GABA aminotransferase) (Gamma-amino-N-butyrate transaminase) (L-AIBAT) (X5D8S1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MASMLLAQRLACSFQHSYRLLVPGSRHISQAAAKVDVEFDYDGPLMKTEVPGPRSQELMKQLNIIQNAEAVHFFCNYEESRGNYLVDVDGNRMLDLYSQISSVPIGYSHPALLKLIQQPQNASMFVNRPALGILPPENFVEKLRQSLLSVAPKGMSQLITMACGSCSNENALKTIFMWYRSKERGQRGFSQEELETCMINQAPGCPDYSILSFMGAFHGRTMGCLATTHSKAIHKIDIPSFDWPIAPFPRLKYPLEEFVKENQQEEARCLEEVEDLIVKYRKKKKTVAGIIVEPIQSEGGDNHASDDFFRKLRDIARKHGCAFLVDEVQTGGGCTGKFWAHEHWGLDDPADVMTFSKKMMTGGFFHKEEFRPNAPYRIFNTWLGDPSKNLLLAEVINIIKREDLLNNAAHAGKALLTGLLDLQARYPQFISRVRGRGTFCSFDTPDDSIRNKLILIARNKGVVLGGCGDKSIRFRPTLVFRDHHAHLFLNIFSDILADFK
Protein: Probable dolichyl-phosphate-mannose--protein mannosyltransferase 7 (EC 2.4.1.109) (Q06644)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Probable protein O-mannosyltransferase involved in O-glycosylation which is essential for cell wall rigidity. Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P33775}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MKDLRLQGPYRKYIPYNIFQQCGIGHLKTLDYIFAFLIVITNFTLIWKSHSSSFWNRPWDNNSEQELSQLIQFYLDKAFYIHELPPFTIQFYSIIRRLKIAENLRYVSLFLNSSTLGFLFLITRRINCSRLISATGLLILSNWETFRNEGTIISFDSLEWCLFSVVIYSFISISIAKLGTTNWFANVITLSISLGLAISSKFIGIVTWAFVILSFVRQFDRLISDVKVTTIQIIKFVILCLLFVLIIPGSIFIISYSNLLSNFKTDTPQFSKYMSTYFKSYLRGPQVQPSRLYYGSTITLRHLDSMVGYLASHDISYPSDVDEQLVALSFEEFAADNEWLIEHPTLNLSFSEVYHADQLIPVEFGQSIKLRHKSTGKLLRASTAKPPISEQDYDFQISCTKDSNYEGGMDERWDVLLIKDEINNDKKDNADDKYIKPLQSEIRFYNNGQRCGLLGHDLRLPEWGRFEQEVLCMEYPVIPRTTFLIDSVQLPVDFQVPMIEYYIGKISSSAEFNHTLSWSQFLYLFKEYIFKQYKYNYYIKYGKNKVTFEDAFAVEKWPITLDTDSPVWFNFAWYGSLLSMIIFMCVQCKRMISWNPWTTAEPSFSIKWEVYNEFGWECIVGWFLHFYIFTMSPHFNLGKKLYFQSFFFSVLCLLESLDCLAK
Protein: [histone H3]-trimethyl-L-lysine(4) demethylase (EC 1.14.11.67) (A0A3B3ITJ7)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEAATTLHPGPRPALPLGGPGPLGEFLPPPECPVFEPSWEEFADPFAFIHKIRPIAEQTGICKVRPPPDWQPPFACDVDKLHFTPRIQRLNELELVAEEGGFAVVCKDRKWTKIATKMGFAPGKAVGSHIRGHYERILNPYNLFLSGDSLRCLQKPNLTTDTKDKEYKPHDIPQRQSVQPSETCPPARRAKRMRAEAMNIKIEPEETTEARTHNLRRRMGCPTPKCENEKEMKSSIKQEPIERKDYIVENEKEKPKSRSKKATNAVDLYVCLLCGSGNDEDRLLLCDGCDDSYHTFCLIPPLHDVPKGDWRCPKCLAQECSKPQEAFGFEQAARDYTLRTFGEMADAFKSDYFNMPVHMVPTELVEKEFWRLVSTIEEDVTVEYGADIASKEFGSGFPVRDGKIKLSPEEEEYLDSGWNLNNMPVMEQSVLAHITADICGMKLPWLYVGMCFSSFCWHIEDHWSYSINYLHWGEPKTWYGVPGYAAEQLENVMKKLAPELFVSQPDLLHQLVTIMNPNTLMTHEVPVYRTNQCAGEFVITFPRAYHSGFNQGFNFAEAVNFCTVDWLPLGRQCVEHYRLLHRYCVFSHDEMICKMASKADVLDVVVASTVQKDMAIMIEDEKALRETVRKLGVIDSERMDFELLPDDERQCVKCKTTCFMSAISCSCKPGLLVCLHHVKELCSCPPYKYKLRYRYTLDDLYPMMNALKLRAESYNEWALNVNEALEAKINKKKSLVSFKALIEESEMKKFPDNDLLRHLRLVTQDAEKCASVAQQLLNGKRQTRYRSGGGKSQNQLTVNELRQFVTQLYALPCVLSQTPLLKDLLNRVEDFQQHSQKLLSEETPSAAELQDLLDVSFEFDVELPQLAEMRIRLEQARWLEEVQQACLDPSSLTLDDMRRLIDLGVGLAPYSAVEKAMARLQELLTVSEHWDDKAKSLLKARPRHSLNSLATAVKEIEEIPAYLPNGAALKDSVQRARDWLQDVEGLQAGGRVPVLDTLIELVTRGRSIPVHLNSLPRLETLVAEVQAWKECAVNTFLTENSPYSLLEVLCPRCDIGLLGLKRKQRKLKEPLPNGKKKSTKLESLSDLERALTESKETASAMATLGEARLREMEALQSLRLANEGKLLSPLQDVDIKICLCQKAPAAPMIQCELCRDAFHTSCVAVPSISQGLRIWLCPHCRRSEKPPLEKILPLLASLQRIRVRLPEGDALRYMIERTVNWQHRAQQLLSSGNLKFVQDRVGSGLLYSRWQASAGQVSDTNKVSQPPGTTSFSLPDDWDNRTSYLHSPFSTGRSCIPLHGVSPEVNELLMEAQLLQVSLPEIQELYQTLLAKPSPAQQTDRSSPVRPSSEKNDCCRGKRDGINSLERKLKRRLEREGLSSERWERVKKMRTPKKKKIKLSHPKDMNNFKLERERSYELVRSAETHSLPSDTSYSEQEDSEDEDAICPAVSCLQPEGDEVDWVQCDGSCNQWFHQVCVGVSPEMAEKEDYICVRCTVKDAPSRK
Protein: Pivalyl-CoA mutase large subunit (PCM large subunit) (EC 5.4.99.-) (Pivalyl-CoA mutase, substrate-binding subunit) (A7IQE5)
Organism: Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2)
Function: Together with Xaut_5044, catalyzes the reversible isomerization between pivalyl-CoA and isovaleryl-CoA, using radical chemistry. Does not exhibit isobutyryl-CoA mutase (ICM) activity.
Interaction partners:
Sequence:
MNQAAVQLPLPGFEQASGQWRSDYSRQVAGEKPVRNRSGIEVQPLYSPRDWAGERYLDDLGFPGQYPFTRGIYPSMHRGRTWTQRQLIGLGTPQDYNVRVRRIIDAGATAISLLPCCSGFRGIDCDEVDPVLLGTCGTVVNTTDHMDAALDGVPLGTISTAMNDPSPFTLLAFTLGVARRRGIDWRSITGTSNQSDYISHFIANHQFYRLSLPGSRRVLLDHIEFCRRALPNWNPLSVVGQHMQQAGATPAETMGFTLSSAIQYAQDCIERGMDVDDVLRRFTFFFDISISFFEEIAKFRAGRRIWARIARERLGAKDPACWRFKFHGQTSGVDLTQQQPLNNIARVSVQAMAGILSGLQSMHTDAYDEAIACPSEETARIAVATQNILRDEAQLCAVIDPLGGSYYVERLTDQMEAEIEAVIARIDAAGGMYKAAEVGLVQTMIGESALAFQEQLETGERKIVGVNCYQVEEDPTIPPAERPDPEAMERHVERFKVFKRERSQDAVARALDALARAANSERENVFEKVVEAAEAGVTHGEMVGCLRRELGFGHPLIIA
Protein: Retinol dehydrogenase 5 (A0A0G2K1R4)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Retinoid isomerohydrolase
- Lecithin retinol acyltransferase
- Retinaldehyde dehydrogenase 3
- Retinal dehydrogenase 2
- Aldehyde dehydrogenase 1A1
- Retinol dehydrogenase 10
- NADP-retinol dehydrogenase
- Diacylglycerol O-acyltransferase 1
- Aldehyde oxidase 2
- Aldehyde oxidase 4
Sequence:
MWLPLLLGALLWAVLWLLRDRQSLPARDAVIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGETGLFGLVNNAGVAGIIGPTPWLTQDDFQRVLNVNTLGPIGVTLALLPLLQQARGRVVNITSVLGRIAANGGGYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVTNLESLENTLKACWARLPPATQAHYGEAFLTTYLQVQRRIMNLICDPDLTKVTSCLEHALTARHPRTRYSPGWDAKLLWLPASYLPARVVDAVLAWVLPRPAQSIY
Protein: GID complex subunit 5 (Glucose-induced degradation protein 5) (Vacuolar import and degradation protein 28) (P40547)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for the adaptation to the presence of glucose in the growth medium; mediates the degradation of enzymes involved in gluconeogenesis when cells are shifted to glucose-containing medium. Required for proteasome-dependent catabolite degradation of fructose-1,6-bisphosphatase (FBP1).
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}. Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- GID complex subunit 9
- GID complex substrate-recognition subunit 4
- GID complex subunit 1
- GID complex subunit 8
- GID complex subunit 7
- E3 ubiquitin-protein ligase RMD5
- GID complex substrate-recognition subunit 10
- GID complex associated protein 12
- Fructose-1,6-bisphosphatase
- Ubiquitin-conjugating enzyme E2-24 kDa
Sequence:
MTVAYSLENLKKISNSLVGDQLAKVDYFLAPKCQIFQCLLSIEQSDGVELKNAKLDLLYTLLHLEPQQRDIVGTYYFDIVSAIYKSMSLASSFTKNNSSTNYKYIKLLNLCAGVYPNCGFPDLQYLQNGFIQLVNHKFLRSKCKIDEVVTIIELLKLFLLVDEKNCSDFNKSKFMEEEREVTETSHYQDFKMAESLEHIIVKISSKYLDQISLKYIVRLKVSRPASPSSVKNDPFDNKGVDCTRAIPKKINISNMYDSSLLSLALLLYLRYHYMIPGDRKLRNDATFKMFVLGLLKSNDVNIRCVALKFLLQPYFTEDKKWEDTRTLEKILPYLVKSFNYDPLPWWFDPFDMLDSLIVLYNEITPMNNPVLTTLAHTNVIFCILSRFAQCLSLPQHNEATLKTTTKFIKICASFAASDEKYRLLLLNDTLLLNHLEYGLESHITLIQDFISLKDEIKETTTESHSMCLPPIYDHDFVAAWLLLLKSFSRSVSALRTTLKRNKIAQLLLQILSKTYTLTKECYFAGQDFMKPEIMIMGITLGSICNFVVEFSNLQSFMLRNGIIDIIEKMLTDPLFNSKKAWDDNEDERRIALQGIPVHEVKANSLWVLRHLMYNCQNEEKFQLLAKIPMNLILDFINDPCWAVQAQCFQLLRNLTCNSRKIVNILLEKFKDVEYKIDPQTGNKISIGSTYLFEFLAKKMRLLNPLDTQQKKAMEGILYIIVNLAAVNENKKQLVIEQDEILNIMSEILVETTTDSSSNGNDSNLKLACLWVLNNLLWNSSVSHYTQYAIENGLEPGHSPSDSENPQSTVTIGYNESVAGGYSRGKYYDEPDGDDSSSNANDDEDDDNDEGDDEGDEFVRTPAAKGSTSNVQVTRATVERCRKLVEVGLYDLVRKNITDESLSVREKARTLLYHMDLLLKVK
Protein: Serine/threonine-protein phosphatase UIS2 (Up-regulated in infective sporozoite protein 2) (EC 3.1.3.16) (A0A509AQ20)
Organism: Plasmodium berghei (strain Anka)
Function: Protein phosphatase which dephosphorylates 'Ser-59' of translation factor eIF2alpha during the liver stage, thus enabling protein translation.
Interaction partners:
- riboflavin kinase
Sequence:
MNISKFFLIFIPLVLFKYPANNELINYNVILKYDVKDLFKRVLQEQNEDIKDDNDENDEGDEEDEYYSYLKNRGTNEFDKVKYKYAEYVRFSIFKSKNIYTHIFNELLVFLGAQYGTEEEIVVHVKLIDILSLLFTHYKDNLSKFGHILNSFQDRSKLMNSVENEFMNEFINERDNYIYDVKNAYNKSDNNDDEWIETVLNKKNMLYDKFLKEWRIDGSNFYSIHNKKKTYLPKKVFQNKQNYIPDFENMEHVDLVCKPISDSAIDEKSAEKYEDKELNINEQNEQSNSKKEQTGNDNVSETKMHKEESSDSSNKTDESNVCKSENKYIKKTNNNKKIKEERHGFIYKMRNDFFLSDASLNVISLINSITSNEENKIVKKLYTGLKKLKITTFDNLIRYTNIIGIFFSYDIFDELYLQIKLIKEYFGLIPRNNDELSIVSKSKNVSKIKVYGKYNITDDEMFVPPVCLSAYCKLRSVWMQNRDFNFKIEKYSSNSINFMTLGDIGRGFKKENSYDEEQMLKLIGFNELKSTSNAMKDWHASNNADFVINLGDNVPEVDELDYLKNFEWHKIMRELFTFRKQDEDEEKNDADSYSITKDNIQEFYKEVEKQMNNTNTDDKNQHNDISTTPINNYTDGNEGNNNSENNNGFREYINDNTKDYNIYKNETTEKEETYDSIPFFSIFGEKDYFYFPSEQIQEHYAKRIPGYFFPNNYYRINYDFVYNNKEKNGVQEKFKASFIFIDTWSLMIGFPIIRNYRSFREQFNWINKALLESAKESDWIFVVGHHPFISSGRRSDNYSFEELSFHNIIRNFFFYYNIDGYFSAHDNLMEYLNFGPLNLFVNGSSSRVLFDKSTILGRGYFGKMVGSIYPVTCYLLTTIHSALRPKGCDISKYSKWSNKYDIGFSAHKLSKDELVTEFINSRSGKPVSQKIVIKNKKDKRRKFYDLDGYTNDKIKQFENKIYEFSSKNPNFIKYKIEEFKENDKKLNIIMNNLKSEEEKDAFRSLMFLNNLIFGISSHISNISFDQLKLMCYLANKYRTFFNKKLIKFLGEELKIAVQKMEVKTTNETPHNSNEILNTNENESIQPNDPTMKVEQIMELIDTLGYKPDEFLEKYDAMTQEEKDALKEKLGNDVSLEDYLSKVKMYIHKKKLSAEELKEYEENEENIKIAEVPDESKEDDNTNSQPEDTIDQENKDDINDIINAPNEVHKNYKELVEKEKKLTENEHALLMLSSLKTYDEMKYSLNILSKKEVIKEEAHPYGLYYIEKHKTFFQVSLELCPDIKRIISNLGKVGTKLAFYDYINNLYNKIMDLKNSIDKIAIF
Protein: UDP-N-acetylglucosamine diphosphorylase (EC 2.7.7.23) (Q386Q8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Phosphoacetylglucosamine mutase
Sequence:
MSDRDVCIQRLTGANQDHILTALEHGSEAERASLTAQITNELAGVDFRHFNDVLRESLEISKNCSTASLAEPPAKDSFFDISSVDRRRGQAKRIKNLEAVGYKAIQKGQIAFLILAGGSGTRLGFDKPKGFFTCDGLQQRKSLFMMHCEKIRRRQEIAESISGSGRKARVQLLVMTSGQNDAETQRFFEENSYFGLEREQVHFFAQSSVPCYDENTGRIIMENRGRICAAPGGNGAVFAALAAPRATKDKDGTLQVKESLLQHLRKLGIAYVQIGNIDNLLANVADPVFIGYAIEEEAHVVVKTCPKRGPDERVGVFVRASGKWGVVEYTEIGDRAKEIDDATGELKFNCANISSNLCSLHFMSLAAERMKSFTQYHAARKKIPTIKGPVMGIKLEAFLFDLFRFVDECDHPPKDSGAFRIMQVDRDDEFGPVKNADGAASDTPADAVRLLLSQHTRWLITALETAAMSDEQESIRGGVDVTEAKEAVAVMRSCSIKAEISPLVSVGGEGLRQHLPRVIHQLLRNPPPVIFIRRDDEVVSESSNM
Protein: Mediator of RNA polymerase II transcription subunit 20 (Mediator complex subunit 20) (A0A1D8PLN4)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU364152}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 18
- Mediator of RNA polymerase II transcription subunit 31
- Mediator of RNA polymerase II transcription subunit 7
- Mediator of RNA polymerase II transcription subunit 10
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 11
- Mediator of RNA polymerase II transcription subunit 4
- Mediator of RNA polymerase II transcription subunit 6
- Mediator of RNA polymerase II transcription subunit 21
Sequence:
MVTAVLLVQKANLETITQFHDQISNELPTAKGKWNFNFKIFRNNQYSIPQELVDTHEQAPESKFLFTLSPSYLRDSTITLINGKSAGVFTNSIEEELSELGHPSDLSIPNDHLRRGATTGLNDKFDNFIGAKLQSLWTQRQLIKGDGGQIYELENGNLCIRTSNVFLHGNFRGLLIQIEMSNSLCDTNNHNSFKEHFNKIVEKYGFPEGNLCCDVLDKKNLDKYGDLCLQYSKILNF
Protein: Cytochrome P450 4A12B (EC 1.14.14.1) (A2A974)
Organism: Mus musculus (Mouse)
Function: A cytochrome P450 monooxygenase involved in the metabolism of fatty acids and their oxygenated derivatives (oxylipins). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase). Catalyzes predominantly the oxidation of the terminal carbon (omega-oxidation) of saturated and unsaturated fatty acids. May act as a major omega-hydroxylase for dodecanoic (lauric) acid in kidney. Participates in omega-hydroxylation of (5Z,8Z,11Z,14Z)-eicosatetraenoic acid (arachidonate) to 20-hydroxyeicosatetraenoic acid (20-HETE), a signaling molecule acting both as vasoconstrictive and natriuretic with overall effect on arterial blood pressure. Acts as an omega-hydroxylase and epoxidase toward (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoc acid (EPA). Catalyzes the epoxidation of the last double bond of EPA with no preferred stereoselectivity, producing both (R,S) and (S,R) stereoisomers. Can also catalyze the omega-1 and omega-2 oxidation of fatty acids with lower efficiency.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:17112342}; Peripheral membrane protein. Microsome membrane {ECO:0000269|PubMed:17112342}; Peripheral membrane protein.
Interaction partners:
- Cytochrome P450 1A2
- Cytochrome P450 2E1
- Cytochrome P450 2U1
- Cytochrome P450 1A1
- Polyunsaturated fatty acid lipoxygenase ALOX8
- Polyunsaturated fatty acid lipoxygenase ALOX15
- Prostaglandin G/H synthase 1
- Prostaglandin G/H synthase 2
- Polyunsaturated fatty acid lipoxygenase ALOX12
- Polyunsaturated fatty acid
Sequence:
MSASALSSIRFPGSISEYLQVASVLSLLLLLFKTAQLYLHRQWLLSSTQQFPSPPSHWLFGHKILKDQDLQDILTRIKNFPSACPQWLWGSKVRIQVYDPDYMKLILGRSDPKAHGSYRFLAPWIGRGLLLLDGQTWFQHRRMLTPAFHYDILKPYTEIMADSVHVMLDKWEQIVGQDSTLEIFQHITLMTLDTIMKCAFSHEGSVQLDRKYKSYIQAVEDLNNLFFLRVRNIFHQNDIIYRVSSNGCLANSACQLAHDHTDQVIKSRRSQLQDEEELEKLKKKRRLDFLDILLFARMENGKSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGASITWNDLDKMPYTTMCIKEALRIYPPVPSVSRELSSPVTFPDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPGSSRHSHSFLPFSGGARNCIGKQFAMNELKVAVALTLLRFELLPDPTRVPIPIPRIVLKSKNGIHLHLKKLQ
Protein: AT4g04650 protein (RNA-directed DNA polymerase (Reverse transcriptase)-related family protein) (T19J18.5 protein) (Q9S9V5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MCKLRVVARPFIVCEVGSGVTAKFWHDNWIGLGPLIEVIGPLGPRTVGLPIDAVVRDALRGTSWWIASSRSRNPIIVQLKNLLPEAQGLLDCQHDDSFLWKTDLHAPSNRFSAPRTWSALHPQSHTVPWHKAVWFKNHVPKHAFICWVVAWNRLHTRDRLQNWGLSIPAECLLCNAHDDSRAHLFFECQFSGVVWRFFTASTNLNPPAQLMDCLNWLLSPSREKNICLIIRLAFHSCVYAIWRERNQRLHSGVSRSTESILKDIQLIIRARLDPLSRSTAHQPNALSLLGTCEPEITVYKAPEIEVKLDNFNEKTDIYSFGIVFLSLALFWI
Protein: Uncharacterized transcriptional regulatory protein C2H10.01 (O94392)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Uncharacterized transcriptional regulatory protein C530.11c
- Serine/threonine-protein kinase oca2
- Transcription factor cbf12
- Transcription factor fil1
- Uncharacterized transcriptional regulatory protein C15D4.02
Sequence:
MTQKNTGPRRRTAVACDRCRRRKIRCTGSDIPGQPCLACQKAHADCHFSTTSWRACRKKSAPLHCPSTNGKTNVLPSYASTPSLSPMTSSHFPYASDGTLISATNHCDDCSYNPHYLPVNSNGSSPSHTSSLDSIPGYASGSGPFKTPYRPVAVSESSSRSSFSMGSSEFASSTWSQSPMQSSLYVSPSSQPLDRFSPASFPSKETLTSSSLSSSVPRSVSLSNFADSNTSNYPESSLLPAAKVGNNGFVGSNVLGSMSYSNVEDSVRFQTDSVSQMSSKSLEHLPMLSEMTLSSSASFGASVSPKSTPGSNSTGAAVDTNSVHSNGGSDLDYSSYLTDSSAVDSPSLDADEVLRSFNLANDPIGAVDPLTLEIDQGSGSQLLGQQSFANDSLNAKQSSGKLGPLPPQSFNSSDYISFDEPSRYLSDDASLWPDQYVDKVQPLATMKTCNPAVFSSNTSLDDMFFFIRDFDEDHPIQTAY
Protein: Lysosomal cobalamin transporter ABCD4 (EC 7.6.2.8) (ATP-binding cassette sub-family D member 4) (PMP70-related protein) (P70R) (Peroxisomal membrane protein 1-like) (PXMP1-L) (Peroxisomal membrane protein 69) (PMP69) (O14678)
Organism: Homo sapiens (Human)
Function: Lysosomal membrane protein that transports cobalamin (Vitamin B12) from the lysosomal lumen to the cytosol in an ATP-dependent manner. Targeted by LMBRD1 lysosomal chaperone from the endoplasmic reticulum to the lysosomal membrane. Then forms a complex with lysosomal chaperone LMBRD1 and cytosolic MMACHC to transport cobalamin across the lysosomal membrane.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:27456980}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:22922874, ECO:0000269|PubMed:25535791, ECO:0000269|PubMed:27456980, ECO:0000269|PubMed:28572511, ECO:0000269|PubMed:33845046}; Multi-pass membrane protein {ECO:0000255}. Note=Targeted by LMBRD1 lysosomal chaperone to the lysosomal membrane. {ECO:0000269|PubMed:27456980, ECO:0000269|PubMed:28572511}.
Interaction partners:
- Lysosomal cobalamin transport escort protein LMBD1
- ATP-binding cassette sub-family A member 2
- ATP-binding cassette sub-family B member 6
- ATP-binding cassette sub-family G member 5
- ATP-binding cassette sub-family G member 8
- DNA repair protein RAD51 homolog 1
- Long-chain-fatty-acid--CoA ligase ACSBG1
- Mitochondrial potassium channel ATP-binding subunit
- Long-chain fatty acid transport protein 2
- Cyanocobalamin reductase / alkylcobalamin dealkylase
Sequence:
MAVAGPAPGAGARPRLDLQFLQRFLQILKVLFPSWSSQNALMFLTLLCLTLLEQFVIYQVGLIPSQYYGVLGNKDLEGFKTLTFLAVMLIVLNSTLKSFDQFTCNLLYVSWRKDLTEHLHRLYFRGRAYYTLNVLRDDIDNPDQRISQDVERFCRQLSSMASKLIISPFTLVYYTYQCFQSTGWLGPVSIFGYFILGTVVNKTLMGPIVMKLVHQEKLEGDFRFKHMQIRVNAEPAAFYRAGHVEHMRTDRRLQRLLQTQRELMSKELWLYIGINTFDYLGSILSYVVIAIPIFSGVYGDLSPAELSTLVSKNAFVCIYLISCFTQLIDLSTTLSDVAGYTHRIGQLRETLLDMSLKSQDCEILGESEWGLDTPPGWPAAEPADTAFLLERVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQMLTDFGPHGVLFLPQKPFFTDGTLREQVIYPLKEVYPDSGSADDERILRFLELAGLSNLVARTEGLDQQVDWNWYDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVESELYRIGQQLGMTFISVGHRQSLEKFHSLVLKLCGGGRWELMRIKVE
Protein: Nidogen (C7FZU3)
Organism: Caenorhabditis elegans
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000256|ARBA:ARBA00004302}.
Interaction partners:
Sequence:
MKHKKMLILLFLYLLIETTTANPAFYPYGQPAGDNRLDYSMEQSAIALKIPLTYMEQSVDELFLSHNGIVGLGKPTPEKIGGLMTISTPAIAVFYVPVTSGVIDYRVSSDDQGLLTKLTQDVKQVFADAVEFHGLQAVIITWTQIENAEKDGPASFQLAIVSDGISTYAIFRYESLPWSSSMGYYAQAGFVRSIGKIQTNVNSGGPDVKELVNLSNNQFGNFFIFRVSGSAIEDPKDEGADDYDYNNYDQEYEGEHPADCPKDKFVDNCPAECRTVRDERGCERCICAERPHAPRAPQEPRPELENTVEDDEDDEQVDGTRYEEPARQAQEQHHQQHHQPDQPQQQPQRSQEGSLPKMSCSQRDDKSCHANSVCQDFEGGFCCNCDTGFYGNGKECLPKGEPQRISGSFEGVINRIPIDKTELHTFATSTDGNVHTAVSKIPSDLGHPLRFLYSIGGVMGWLFADVQSPNVYNGFQLTGGLFNRTVALHIEQNYYVTIKQEFSGRNIHDYFKSHLFVSGTLPDIAPGSEVIFPDYEEEYVRERRGYLTSKAAFDVIVRDGGNVQTYRMSVDQQITFEECPNKEFDRDHSMKLHVKRINVVYNDDEGVVRYGAKNFATRSVGPAVSAPSGGHFDRRQHGQSNMASERPIEIPSQSESISTDSVCAPGRHQCTLPNMKCRVVDPSYRCECEPGYQAAHDASSHIGWICQDLDECQRGDHNCDQHAKCTNRPGSFSCQCLQGYQGDGRSCIREHQASHHEHNQQTPQEMAGVGATTEGFCTAHNQCHQWGECVFTSEHPTGRCKCRGWYVGDGVNHCGPPEENMPKHNANIPQRGGQACGSYVCDVNAECMPEPSGGSECVCKAGFSGNGVTCESLLDDRHAHSSHNRHEQQQQTGSLGKVCRSHDECSEHGSCAYHHSLGYYQCACTEPYVGNGVECTLPGSSASVPQLPSEPAVLSTASCNPNCGPDAQCVYDDHNRQYRCECYAAFMGDGYNCVPLAKPNMVPAQPKTCVESSDCHINGHCVINEHGAGEYICQCLPGFSGDGFINCRGADQCNPSNPSACYQNAHCVYDAILNAHACKCVDGFKGDGTSCVPYAPATNCNLEPRICHANAQCVMHHDTNAYECICKPGSSGDGYTKCDVIETPRCTNCSIHAYCAQNPTSGAYQCKCNAGYNGNGHLCVSMSSCLDDRSLCDENADCVPGEAGHYVCNCHYGYHGDGRSCSPESSTRSDKLLVARGMAIFERSTNPDEYGKQLIVIPHHIPVGIDFDCKEEKIVWSDMSGHSIRTSSLNGTEHKSYFNKELSSPEGIAVDWSSRNVYYADSMNDEIGVASLNGKFKKSLVTEGLVNPRSVVLDLYGRHLYYSDWHRENPYIGRVDMDGKNNRVFLNEDVHLPNGLTILPNRRELCWVDAGNHRLSCIQYNGAGRRTVFSSLQYPFGLTHDEEQKFYWTDWKDNRIHSVGVYGEGYRSFQISLGGSGKVFGILAVPKSCVGPSTPCSEDNGGCQHLCLPGQNGAVCECPDNVKVKGC