wanglab/gogpt-training-data huggingface dataset:
Protein: Dihydromonacolin L monooxygenase LovA (EC 1.14.14.124) (EC 1.14.14.125) (Dihydromonacolin L hydroxylase) (Lovastatin biosynthesis cluster protein A) (Monacolin L hydroxylase) (Q9Y7C8)
Organism: Aspergillus terreus
Function: Dihydromonacolin L monooxygenase; part of the gene cluster that mediates the biosynthesis of lovastatin (also known as mevinolin, mevacor or monacolin K), a hypolipidemic inhibitor of (3S)-hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR). The first step in the biosynthesis of lovastatin is the production of dihydromonacolin L acid by the lovastatin nonaketide synthase lovB and the trans-acting enoyl reductase lovC via condensation of one acetyl-CoA unit and 8 malonyl-CoA units. Dihydromonacolin L acid is released from lovB by the thioesterase lovG. Next, dihydromonacolin L acid is oxidized by the dihydromonacolin L monooxygenase lovA twice to form monacolin J acid. The 2-methylbutyrate moiety of lovastatin is synthesized by the lovastatin diketide synthase lovF via condensation of one acetyl-CoA unit and one malonyl-CoA unit. Finally, the covalent attachment of this moiety to monacolin J acid is catalyzed by the transesterase lovD to yield lovastatin. LovD has broad substrate specificity and can also convert monacolin J to simvastatin using alpha-dimethylbutanoyl-S-methyl-3-mercaptopropionate (DMB-S-MMP) as the thioester acyl donor, and can also catalyze the reverse reaction and function as hydrolase in vitro. LovD has much higher activity with LovF-bound 2-methylbutanoate than with free diketide substrates.
Subcellular location: Membrane {ECO:0000305|PubMed:21495633}; Single-pass membrane protein {ECO:0000305|PubMed:21495633}. Endoplasmic reticulum membrane {ECO:0000305|PubMed:21495633}; Single-pass type II membrane protein {ECO:0000305|PubMed:21495633}.
Interaction partners:
Sequence:
MTVDALTQPHHLLSLAWNDTQQHGSWFAPLVTTSAGLLCLLLYLCSSGRRSDLPVFNPKTWWELTTMRAKRDFDANAPSWIESWFSQNDKPIRFIVDSGYCTILPSSMADEFRKMKELCMYKFLGTDFHSHLPGFDGFKEVTRDAHLITKVVMNQFQTQAPKYVKPLANEASGIITDIFGDSNEWHTVPVYNQCLDLVTRTVTFIMVGSKLAHNEEWLDIAKHHAVTMAIQARQLRLWPVILRPLVHWLEPQGAKLRAQVRRARQLLDPIIQERRAERDACRAKGIEPPRYVDSIQWFEDTAKGKWYDAAGAQLAMDFAGIYGTSDLLIGGLVDIVRHPHLLEPLRDEIRTVIGQGGWTPASLYKLKLLDSCLKESQRVKPVECATMRSYALQDVTFSNGTFIPKGELVAVAADRMSNPEVWPEPAKYDPYRYMRLREDPAKAFSAQLENTNGDHIGFGWHPRACPGRFFASKEIKMMLAYLLIRYDWKVVPDEPLQYYRHSFSVRIHPTTKLMMRRRDEDIRLPGSL
Protein: Postreplication repair E3 ubiquitin-protein ligase RAD18 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase RAD18) (Radiation sensitivity protein 18) (P10862)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: E3 RING-finger protein, member of the UBC2/RAD6 epistasis group. Associates to the E2 ubiquitin conjugating enzyme UBC2/RAD6 to form the UBC2-RAD18 ubiquitin ligase complex involved in postreplicative repair (PRR) of damaged DNA. The UBC2-RAD18 complex cooperates with RAD5 and the UBC13-MMS2 dimer to attach mono-ubiquitin chains on 'Lys-164' of POL30, which is necessary for PRR. The UBC2-RAD18 complex is also involved in prevention of spontaneous mutations caused by 7,8-dihydro-8-oxoguanine.
Subcellular location: Nucleus {ECO:0000269|PubMed:10880451}.
Interaction partners:
- Ubiquitin-conjugating enzyme E2 2
- DNA repair protein RAD5
- Proliferating cell nuclear antigen
- ATP-dependent DNA helicase SRS2
- DNA polymerase zeta catalytic subunit
- Ubiquitin-conjugating enzyme E2 13
- DNA polymerase eta
- DNA repair protein REV1
- Ubiquitin-conjugating enzyme variant MMS2
- DNA repair protein RAD51
Sequence:
MDHQITTASDFTTTSIPSLYQLDTLLRCHICKDFLKVPVLTPCGHTFCSLCIRTHLNNQPNCPLCLFEFRESLLRSEFLVSEIIQSYTSLRSSLLDALRIPKPTPVPENEEVPGPENSSWIELISESESDSVNAADDDLQIVATSERKLAKRSMTDILPLSSKPSKRNFAMFRSERIKKKSKPNEQMAQCPICQQFYPLKALEKTHLDECLTLQSLGKKPKISTTFPTESNPHNKSSSRFKVRTPEVDKSSCGETSHVDKYLNSMMSAEHQRLPKINFTSMTQSQIKQKLSSLGLSTNGTRQNMIKRYNHYEMLWNSNFCDSLEPVDEAELKRQLLSWDVSHNKTPQNSSNKGGISKLMIMKSNGKSSSYRKLLENFKNDKFNRKGWMVMFRKDFARLIREAKMKIKTGSSDSSGSVGHSNDGDGVEKVQSDQGTEDQQMEKDQDTVINEDRVAGERNLPNEDSTDADLSRELMDLNEYSKDPPGNN
Protein: Alkaline ceramidase YPC1 (EC 3.5.1.-) (Acyl-CoA-independent ceramide synthase) (P38298)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Alkaline ceramidase that hydrolyzes phytoceramide and also dihydroceramide into phytosphingosine or dihydrosphingosine. Prefers phytoceramide. Has also reverse activity as acyl-CoA-independent ceramide synthase, catalyzing synthesis of phytoceramide and dihydroceramide from palmitic acid and phytosphingosine or dihydrosphingosine. Is not responsible for the breakdown of unsaturated ceramide. Preferentially uses very long chain fatty acids (C-24 and C-26) in vivo compared to C-16 in vitro.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10900202, ECO:0000269|PubMed:24866405}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to the cortical ER. {ECO:0000269|PubMed:24866405}.
Interaction partners:
- Ceramide synthase LAG1
- Ceramide synthase LAC1
- Sphingoid long chain base kinase 5
- Sphingoid long chain base kinase 4
- Sphingolipid C4-hydroxylase SUR2
- Inositol phosphosphingolipids phospholipase C
- Serine palmitoyltransferase 1
- Dihydrosphingosine 1-phosphate phosphatase YSR3
- Inositol phosphorylceramide synthase catalytic subunit AUR1
- Serine palmitoyltransferase 2
Sequence:
MGIFRWNYPESSVPGVWGETTSTIDWCEENYVVSPYIAEWSNTLTNSVFILSAIYTTYSAYKNKLEKRFLLIGFGYGLVGVGSWLFHMTLKYRFQLLDELPMIYAMCIPTWSLVCEAKEALLNGDNHKKVPLFEQIFIGVIIGLAVTTASILYVIYKNVDIHQILFGVQIVVVAATAGSLTYRYVHDPLAKRNLKASMALGAILFLSGYISWLLDIHYCSFWVHVRRSILALPLGVLLEPHGWWHILTGMGIYFYIVSLEHLRVITLNVSCNYQFIWRWKVFPELIWKGRKPSTRYSLELFGPYVEDQSIEVKKEK
Protein: Small ribosomal subunit protein uS17A (40S ribosomal protein S11-A) (P0CT73)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein eS7
- Large ribosomal subunit protein eL43A
- Small ribosomal subunit protein eS27
- Elongation factor 3
- Large ribosomal subunit protein uL2A
- Small ribosomal subunit protein uS14
Sequence:
MATELVVQSERAFQKQPHIFQNAKKGAGRRWYKDVGLGFKTPAEAIYGEYVDKKCPFVGQVSIRGRILTGTVVSTKMHRTIIIRREYLHFIPKYNRYEKRHKNLAAHVSPAFRINEGDVVTVGQCRPLSKTVRFNVLRVVKHTEGPKQFGKF
Protein: Amine oxidase (EC 1.4.3.-) (Q5B038)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Aromatic-L-amino-acid decarboxylase, putative
- Amine oxidase
- catechol O-methyltransferase
- catechol O-methyltransferase
- catechol O-methyltransferase
- Lactoylglutathione lyase
- Lactoylglutathione lyase
- Aldehyde dehydrogenase
- Aldehyde dehydrogenase family
- aldehyde dehydrogenase
Sequence:
MKLPLSFSGGIALLLIGSLAGDVVATKLDPSRDLVRQKSRGRKNQMRSLVGRSNQHITHQSRPYTNEYASPCQITPPQEIKAPKENVWYGLTDDETADVAKWLFGRPELNLTTTENAGEWDNTIALIELHRPNKSEAIPYLDGSGPAPTRHAHVRLNNRATTDPYFADILVGPLPVSNATTWEPLEFPYTRKTQGQVRNVEPDGETVYSEWLFKISASIADITLDLWNGTALGLENDTLDIWGIDPLWQDDGRIIRWDMFWNMADDEFDSETLLPLGLYLKSDVTGRDPSQWKLLGWMYNDIFYETTEEFRKAYWSPGFVKLKPNVDGAWAHTEQRGPVPPQDRKQPPVMIAPDGARYSVDAERKYVTWMDFSFYIAFNRDTGLSLFDIKYKGQRVLYELGLQEALAHYAANDPVQSSVAYLDSYYGFGPYAFELLKGYDCPSYASYLNTSFYKDEETHTHVDSLCLFEFDADYPMARHSTSEFVSVTKNVYFTLRSVSTIGNYDYMFSYNFHMDGTIGVEVRASGYIQSAYYANNQDFGYQIHDSLSGSMHDHVLNFKADFDILGPNNTIELVSVVPVTKQFSWSGNKTRNTMQLGRSFIHSEDEARLNWGFNGQTQLHVVNQDKPNKFGEPRGYRILPSAGTAHLTVLNSSNLVHAAHWAEYDVQVTRQHDFEPTSAHPYNSQDIHNPPVDFSTFFNGESLNQTDLVVWLNLGMHHVPHTGDLPNTVFTTAHSGVAFTPLNYLPGDPSRETVNMVRVDYSDGAATAVRTFGQSNETCSVVLQPVENELWSYQGDVVVRKFPYDPNDPFYETDSDA
Protein: Platelet-activating factor acetylhydrolase IB subunit alpha2 (EC 3.1.1.47) (PAF acetylhydrolase 30 kDa subunit) (PAF-AH subunit beta) (V9HW44)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MSQGDSNPAAIPHAAEDIQGDDRWMSQHNRFVLDCKDKEPDVLFVGDSMVQLMQQYEIWRELFSPLHALNFGIGGDTTRHVLWRLKNGELENIKPKVIVVWVGTNNHENTAEEVAGGIEAIVQLINTRQPQAKIIVLGLLPRGEKPNPLRQKNAKVNQLLKVSLPKLANVQLLDTDGGFVHSDGAISCHDMFDFLHLTGGGYAKICKPLHELIMQLLEETPEEKQTTIA
Protein: Putrescine hydroxycinnamoyltransferase 2 (OsPHT2) (EC 2.3.1.-) (Q5SMQ0)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Hydroxycinnamoyl transferase that catalyzes the transfer of an acyl from p-coumaryol-CoA to putrescine, to produce coumaroyl putrescine.
Interaction partners:
- 4-coumarate--CoA ligase 2
- 4-coumarate--CoA ligase-like 9
- Hydrolase, alpha/beta fold family protein, putative, expressed
- Nitrate reductase
- Nitrate reductase
- Nitrate reductase 1
- Os12g0262700 protein
- Os01g0315700 protein
- Probable 5'-adenylylsulfate reductase 1, chloroplastic
- Os01g0820000 protein
Sequence:
MATVEVLTSEVVAPAEETPAGAVWLSNLDLAARRGYTPTVYFYRRNGDDEAAFFAADAVRDGLARALVPFYPLAGRLGLAGGGEDGRVQIDCTGEGAVFVTARSGHYALDDLMNEFVPCDEMRDLFVPPTPPPNPPCALLLVQVTHLRCGGVVLGMALHHSVVDARSAAHFAETWASIVRGAPAGDAPVPPCFDHKLLAARPARAVLYDHPEYKPEPAPAPAHAATASTYASAIITLTKQQVGALKAACAGASTFRAVVALVWQCACRARSLPPDKANLFLLYKYISEDWVDIQLNIQQRDNCIYAPTLKANCCFTPTF
Protein: Hypothetical proline and serine rich protein (O53178)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- GCN5-related N-acetyltransferase
Sequence:
MGRAVSVRHGSGALDLPGAAASRRLRVGQPIQPSPAPLARGSVDSIVEISCCPSAGPRGPYDNDLDSSSPANRDISSITSRSRRGGTIVVAGQKCGFGSAVSLRPRRYREPNHANIVTPDTDLSPSWPWSGI
Protein: Syntaxin 17, isoform B (M9PEM1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- LD03592p
- Vesicle-associated membrane protein 7
- Autophagy-related 14
- LD34211p
- LD27967p
- Vacuolar protein sorting-associated protein 39 homolog
- Syntaxin 8
- Autophagy protein 5
- Secretory 22, isoform B
- Neuronal synaptobrevin, isoform J
Sequence:
MTRDEKLPLKQAEVSIQRFQDVAVPHHLSLLKNHRSNIEKSLALGDWQKIKKEELNAMRVIKQIKNLLLEMDALREKVREEDLERFDDLMKPGRDTAFAGMKEFAELQLKSPTSTLSSQYDDDLDNQPQEVDMNSLPAHRHMPQLQLNFQLEEHQLAQRQACLDQMENLQQEIYDLHGMFQGMRQLTAEQSVAVEKIADNAEEALENVQQGELNLRRALTYKKAMYPVVGALLGTCVGGPIGLVAGMKAGGLAAVGCGILGFTGGSVLKANPNVMHGNIEEEQVEPDSESTERLELKEKPEXPAGGSARSASTALATTHIWSANTRRLEAATNGVICSVRSYCSVQ
Protein: Metaxin-2 (Mitochondrial outer membrane import complex protein 2) (O75431)
Organism: Homo sapiens (Human)
Function: Involved in transport of proteins into the mitochondrion.
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:10381257}. Mitochondrion {ECO:0000269|PubMed:25997101}.
Interaction partners:
- Sorting and assembly machinery component 50 homolog
- Metaxin-1
- MICOS complex subunit MIC60
- MICOS complex subunit MIC25
- MICOS complex subunit MIC19
- Metaxin-3
- MICOS complex subunit MIC27
- MICOS complex subunit MIC10
- MICOS complex subunit MIC13
- Endoplasmic reticulum junction formation protein lunapark
Sequence:
MSLVAEAFVSQIAAAEPWPENATLYQQLKGEQILLSDNAASLAVQAFLQMCNLPIKVVCRANAEYMSPSGKVPFIHVGNQVVSELGPIVQFVKAKGHSLSDGLEEVQKAEMKAYMELVNNMLLTAELYLQWCDEATVGEITHARYGSPYPWPLNHILAYQKQWEVKRKMKAIGWGKKTLDQVLEDVDQCCQALSQRLGTQPYFFNKQPTELDALVFGHLYTILTTQLTNDELSEKVKNYSNLLAFCRRIEQHYFEDRGKGRLS
Protein: Heterogeneous nuclear ribonucleoprotein K, isoform E (E1JGN7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKREMNDEGEGPQDQKRNRRNEETVRILIPSSIAGAVIGKGGQHIQKMRTQYKATVSVDDSQGPERTIQISADIESTLEIITEMLKYFEERDEDFDVRLLIHQSLAGCVIGKGGQKIKEIRDRIGCRFLKVFSNVAPQSTDRVVQTVGKQSQVIEAVREVITLTRDTPIKGAIHNYDPMNFDRVYADEYGGYGTGSGSTRPSQRGNNRNGGGAGGVAGGAAGGNGGGFNAGGARGNAGGRGGADRFGGAAGGAVAGAGMGQRDNPFINPWANGGGGDVDGFGNNAGGAGGFAGNSFGGGAGGPFGGGSFGNNGFGGGPSDFGGNSGNFGQAQGTNSLPSLGSFSQNQGGTSSLPSLGSFGQNPGGPGGLGNGLSGGANGGVGTLGGANGAGGFNAVGGANGGPNGSPNAATNVPQGHDPNNSTQVTIPKELAGAIIGKGGGRIRRIRNESSAYITIDEPLPNSNDRIITISGTPKQIQMAQYLLQQRLVSQSE
Protein: Interleukin-12 subunit alpha (IL-12A) (E9PGR3)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU363133}.
Interaction partners:
Sequence:
MCPARSLLLVATLVLLDHLSLARNLPVATPDPGMFPCLHHSQNLLRAVSNMLQKARQTLEFYPCTSEEIDHEDITKDKTSTVEACLPLELTKNGSCLASRKTSFMMALCLSSIYEDLKMYQVEFKTMNAKLLMDPKRQIFLDQNMLAVIDELMQALNFNSETVPQKSSLEEPDFYKTKIKLCILLHAFRIRAVTIDRVMSYLNAS
Protein: Lectin/endochitinase 1 (EC 3.2.1.14) (Agglutinin) (UDA) (chia5.1.1) [Cleaved into: Lectin 1] (P11218)
Organism: Urtica dioica (Great nettle) (Stinging nettle)
Function: Functions both as a chitinase and as a N-acetyl-D-glucosamine binding lectin. Inhibits the growth of several phytopathogenic chitin-containing fungi. Possesses also insecticidal activity and superantigenic properties.
Interaction partners:
Sequence:
MMMRFLSAVVIMSSAMAVGLVSAQRCGSQGGGGTCPALWCCSIWGWCGDSEPYCGRTCENKCWSGERSDHRCGAAVGNPPCGQDRCCSVHGWCGGGNDYCSGSKCQYRCSSSVRGPRVALSGNSTANSIGNVVVTEPLFDQMFSHRKDCPSQGFYSYHSFLVAAESFPAFGTIGDVATRKREVAAFLAHISQATSGERSDVENPHAWGLCHINTTTVTENDFCTSSDWPCAAGKKYSPRGPIQLTHNFNYGLAGQAIGEDLIQNPDLVEKDPIISFKTALWFWMSQHDNKPSCHDIVLNANSAANRIPNKGVIGNIISRAFGHDDFAVRSSSIGFYKRYCDMLGVSYGHDLKYWFDNTPSSEFQRIQMRVAA
Protein: Uncharacterized protein, isoform F (M9MSJ5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MFDQPPENELQKSHDHNPGALSEHQLRVQASLQRLNIPDWFRHYNKGPEKAADGENACTSATGGGYRPGNFTRKRAQESGRWQGLNSKTTSLSSLGSQRSDRSPLLMSPSAHSHHGGQSSYSCGSTTIHGPAPVQIGMGATRWSTSHLNSTQMSPGASQRGSFTRGAPINSSFISVASGSGLLRNSYRQPYLGWRSTEKLSQRTPHERLANSLLTQRTAPPSTRAGNETRTLHSVSTEIQSSIKEVTSAIVHFVNDQQQSQHPRSRSTSPNSRCWLESSFVGTRTLDSPQTPVIDNSPPELARKQQQLHPHQVHLDVGLSPVVSAGQLPHRMNGINRIGNGGAPERSLSSASLEDVLASLLGLPTTLLSGQNSNSYSSYTPNAATTGMNLMRSFSAAAGGAISRRTAAASSPE
Protein: At3g49310 (Major facilitator superfamily protein) (Putative transporter; 8780-5873) (Q9CA11)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MEVFYYLVFGVMAAVVAALELSKTNKDRINTSSSFNSFKNNYLLVFSIMMAGDWLQGPYVYYLYSTYGFGKGDIGQLFIAGFGSSMLFGTIVGSLADKQGRKRACVTYCIVYILSCITKHSPQYKVLMVGRILGGIATSLLFSAFESWLIAEHNKRNFEQQWLSLTFSKAVFLGNGLVAILSGLFGNLLVDTFSFGPVAPFDAAACFLAIGMAIILGTWSENFGDPSDSKDLLTQFKVAAIAIASDEKIALLGAIQSLFEASMYTFVFLWTPALSPNDEEIPHGFVFATFMLASMLGSSLAARLMSRSSLRVENYMQIVFLVSAASLLLPITTSVLVTPSKVKDEGLSLTSSIQLLGFCVFESCVGIFWPSIMKMRSQYIPEEARSTIMNFFRVPLNIFVCIVLYNVDAFPITIMFGMCSIFLFVASILQRRLMVISEKPKAEDWSPMKERNSEVDPLTL
Protein: Protein RER1 (Q6PE45)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Si:ch211-255f4.7.
- Family with sequence similarity 113
- ATP-dependent RNA helicase DDX51
- Tumor protein p63-regulated 1-like
- AP2-associated kinase 1a.
- HEPACAM family member 2
- peptidylprolyl isomerase
- Exonuclease 3'-5' domain-containing 3.
Sequence:
MPEGDSAGESIHGKPSAIGNFFKRLGQIYQSWLDKSTPFSAVRWASTLILTAIYMIRVYILQGWYIVTYALGIYHLNLFIAFLSPKVDPSLLDDPDEGPALPTKQNEEFRPFIRRLPEFKFWHSATKGIVIAMICTFFDAFNVPVFWPILVMYFIMLFCITMKRQIKHMIKYRYLPFTHGKRTYRGKDDTGKTFAS
Protein: Ras-associating and dilute domain-containing protein (Q69Z89)
Organism: Mus musculus (Mouse)
Function: Downstream effector of Rap required for cell adhesion and migration of neural crest precursors during development.
Interaction partners:
Sequence:
MGSSIFLGLQPSPSHWLKSSVVIHEDAPTMFYGTQLIMSPPTKNKLKRQSQLLSTMLSRTLSYKYRDLDSTFCSLGASDDPSELSTQLSAPGVLKVFGDSVCTGTHYKSVLATGSSSAQELVKEALERYALDPECAGQYVLCDVVGQAGDSGQRWQAQCFRVFGDNEKPLLIQELWKPREGLSRRFELRKKSDVEELASRDVDTTTAGINAQARRLQRIRAKGTPALTSEAAQSSPPTRLRRTVSETSLSPAPSLPEAAQRPEEPVPEAMRYSLYQCPHLLLLQGYSQQHDSLVYVLSKERHTVGQRTPSSKPSISLSAPDILPLHCTIRRHQSPEGGPAGTRLVLEPITGASVSVNFSEVGRNPVVLQHGDLLSLGLYYLLLFKDPGQAQPLPACALARLGAAPQSCRMCGAVLRARGAPSLPAAVVRRRSLLLEFEPDVEDTLLQRIMTLIEPGGDDHKLTPAFLLCLCIQHSAMHFQPGTFRHLLLKISKRVRDTVWEKTKELAEKQAQLQEPISWASFPMADLVPDLQHILFWMSNSIELLYFIQQKSPLYVQSMEEELDVTGSKESLFSCTLTASEEAMAALEEVVLYAFQQCVYYLSKCLYVCLPALLECPPFQTERRESWRSGPALPEELRRVVSVFQATLDLLQQLQMHPEVASQMLAYLFFFSGTLLLNQVLDKGPSLSCFHWPRGVQVCARLQQFLEWARSAGLGAPAERFFRKLSCTLHLLATPRAQLIQMSWATLRVTFPALNPAQLHRLLTQYQLASAMGPVSAWEPGAPDGPEAFQSEDILESYENPPPIVLPSQGFQVDLEADCVEDSIYQHLLYIRHFLWGLRGQASPDSGPAQPESIEGLYHTIPEGHLEGHGCPLANRDPGRVAVETAPPHSLPVTGAPRAQGPPGRQPTRGDRRGSQAGSLHTDSSCMLTPPSTPLGLEPAGPSWPEPSGLCGRAVLDGQRNGPGGLPGAVLEGDAIQDAEPPAEASSPSSSAEDFCYVFMVELERGPSGLGMGLIDGMHTPLGAQGLYIQTLLPGSPAASDGRLSLGDQILEVNGSSLRGVSYMRAVDLIRHGGKKMRFLVAKSDMETAKKIRFRNPPS
Protein: Gem nuclear organelle associated protein 4 (I3L2C7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTILHGGFLLAEQLFHPKALAELTKSDWERVGRPIVEALREISSAAAHSQPFAWKKKALIIIWAKVLQPHPVTPSDTETRWQEDLFFSVGNMIPTINHTILFELLKSLEASGLFIQLLMALPTTICHAELERFLEHVTVDTSAEDVAFFLDVWWEVMKHKGHPQDPLLSQFSAMAHKYLPALDEFPHPPKRLRSDPDACPTMPLLAMLLRGLTQIQSRILGPGRKCCALANLADMLTVFALTEDDPQEVSATVYLDKLATVISVWNSDTQNPYHQQALAEKVKEAERDVSLTSLAKLPSETIFVGCEFLHHLLREWGEELQAVLRSSQGTSYDSYRLCDSLTSFSQNATLYLNRTSLSKEDRQVVSELAECVRDFLRKTSTVLKNRALEDITASIAMAVIQQKMDRHMEVCYIFASEKKWAFSDEWVACLGSNRALFRQPDLVLRLLETVIDVSTADRAIPESQIRQVIHLILECYADLSLPGKNKVLAGILRSWGRKGLSEKLLAYVEGFQEDLNTTFNQLTQSASEQGLAKAVASVARLVIVHPEVTVKKMCSLAVVNLGTHKFLAQILTAFPALRFVEEQGPNSSATFMVSCLKETVWMKFSTPKEEKQFLELLNCLMSPVKPQGIPVAALLEPDEVLKEFVLPFLRLDVEEVDLSLRIFIQTLEANACREEYWLQTCSPFPLLFSLCQLLDRFSKYWQLPKEKRCLSLDRKDLAIHILELLCEIVSANAETFSPDVWIKSLSWLHRKLEQLDWTVGLRLKSFFEGHFKCEVPATLFEICKLSEDEWTSQAHPGYGAGTGLLAWMECCCVSSGISERMLSLLVVDVGNPEEVRLFSKGFLVALVQVMPWCSPQEWQRLHQLTRRLLEKQLLHVPYSLEYIQFVPLLNLKPFAQELQLSVLFLRTFQFLCSHSCRDWLPLEGWNHVVKLLCGSLTRLLDSVRAIQAAGPWVQGPEQDLTQEALFVYTQVFCHALHIMAMLHPEVCEPLYVLALETLTCYETLSKTNPSVSSLLQRAHEQRFLKSIAEGIGPEERRQTLLQKMSSF
Protein: UDP-N-acetylglucosamine diphosphorylase 2 (EC 2.7.7.23) (N-acetylglucosamine-1-phosphate uridylyltransferase 2) (UDP-N-acetylgalactosamine diphosphorylase 2) (EC 2.7.7.83) (UTP--glucose-1-phosphate uridylyltransferase 2) (EC 2.7.7.9) (O64765)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Uridylyltransferase involved in the biosynthesis of UDP-glucosamine, an essential precursor for glycoprotein and glycolipid synthesis. Can use UDP-glucosamine, the 4-epimer UDP-galactosamine and UDP-glucose as substrates. Acts redundantly with GLCNAC1PUT1. Required for gametogenesis and embryo development.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Phosphoacetylglucosamine mutase
- UDP-N-acetylglucosamine diphosphorylase 1
- UTP--glucose-1-phosphate uridylyltransferase 1
- UTP--glucose-1-phosphate uridylyltransferase 2
- Glucosamine 6-phosphate N-acetyltransferase
- E3 ubiquitin-protein ligase RZF1
- Vacuole membrane protein KMS1
- ADP-glucose phosphorylase
- Thylakoid lumenal P17.1 protein
Sequence:
MKEPTTEIEIETSAVATILPPPLPPTASPHQALVERLKDYGQEDVFSLWDELSPEERDLLLRDIENLDLPRIDRIIRCSLHSQGLPVAAIEPVPENCVSTVEERTKEDREKWWKMGLKAIYEGKLGVVLLSGGQGTRLGSSDPKGCYNIGLPSGKSLFQIQAERILCVQRLASQAMSEASPTRPVTIQWYIMTSPFTHEPTQKFFKSHKYFGLEPDQVTFFQQGTLPCISKDGKFIMETPFSLSKAPDGNGGVYTALKSSRLLEDMASRGIKYVDCYGVDNVLVRVADPTFLGYFIDKSAASAAKVVRKAYPQEKVGVFVRRGKGGPLTVVEYTELDQSMASATNQQTGRLQYCWSNVCLHMFTLDFLNQVANGLEKDSVYHLAEKKIPSINGDIVGLKLEQFIFDCFPYAPSTALFEVLREEEFAPVKNANGSNYDTPESARLLVLRLHTRWVIAAGGFLTHSVPLYATGVEVSPLCSYAGENLEAICRGRTFHAPCEISL
Protein: Peroxisomal membrane protein PEX14 (PTS1 receptor-docking protein) (Peroxin-14) (Peroxisomal membrane anchor protein PEX14) (O75381)
Organism: Homo sapiens (Human)
Function: Component of the PEX13-PEX14 docking complex, a translocon channel that specifically mediates the import of peroxisomal cargo proteins bound to PEX5 receptor. The PEX13-PEX14 docking complex forms a large import pore which can be opened to a diameter of about 9 nm (By similarity). Mechanistically, PEX5 receptor along with cargo proteins associates with the PEX14 subunit of the PEX13-PEX14 docking complex in the cytosol, leading to the insertion of the receptor into the organelle membrane with the concomitant translocation of the cargo into the peroxisome matrix. Plays a key role for peroxisome movement through a direct interaction with tubulin.
Subcellular location: Peroxisome membrane {ECO:0000269|PubMed:19197237}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q642G4}.
Interaction partners:
- Peroxisomal targeting signal 1 receptor
- Peroxisomal biogenesis factor 19
- PEX5-related protein
- Peroxisomal membrane protein PEX13
- Peroxisomal targeting signal 2 receptor
- Peroxisome assembly protein 12
- Peroxisome biogenesis factor 2
- Peroxisomal ATPase PEX6
- Peroxisome biogenesis factor 10
- Peroxisomal biogenesis factor 3
Sequence:
MASSEQAEQPSQPSSTPGSENVLPREPLIATAVKFLQNSRVRQSPLATRRAFLKKKGLTDEEIDMAFQQSGTAADEPSSLGPATQVVPVQPPHLISQPYSPAGSRWRDYGALAIIMAGIAFGFHQLYKKYLLPLILGGREDRKQLERMEAGLSELSGSVAQTVTQLQTTLASVQELLIQQQQKIQELAHELAAAKATTSTNWILESQNINELKSEINSLKGLLLNRRQFPPSPSAPKIPSWQIPVKSPSPSSPAAVNHHSSSDISPVSNESTSSSPGKEGHSPEGSTVTYHLLGPQEEGEGVVDVKGQVRMEVQGEEEKREDKEDEEDEEDDDVSHVDEEDCLGVQREDRRGGDGQINEQVEKLRRPEGASNESERD
Protein: Macrophage-stimulating protein receptor (MSP receptor) (EC 2.7.10.1) (CDw136) (Protein-tyrosine kinase 8) (p185-Ron) (CD antigen CD136) [Cleaved into: Macrophage-stimulating protein receptor alpha chain; Macrophage-stimulating protein receptor beta chain] (Q04912)
Organism: Homo sapiens (Human)
Function: Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to MST1 ligand. Regulates many physiological processes including cell survival, migration and differentiation. Ligand binding at the cell surface induces autophosphorylation of RON on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with the PI3-kinase subunit PIK3R1, PLCG1 or the adapter GAB1. Recruitment of these downstream effectors by RON leads to the activation of several signaling cascades including the RAS-ERK, PI3 kinase-AKT, or PLCgamma-PKC. RON signaling activates the wound healing response by promoting epithelial cell migration, proliferation as well as survival at the wound site. Also plays a role in the innate immune response by regulating the migration and phagocytic activity of macrophages. Alternatively, RON can also promote signals such as cell migration and proliferation in response to growth factors other than MST1 ligand.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Hepatocyte growth factor-like protein
- Hepatocyte growth factor
- Hyaluronidase-2
- E3 ubiquitin-protein ligase CBL
- Serine/arginine-rich splicing factor 1
- Hyaluronidase PH-20
- Epidermal growth factor receptor
- Catenin beta-1
- Growth factor receptor-bound protein 2
- Plexin-B1
Sequence:
MELLPPLPQSFLLLLLLPAKPAAGEDWQCPRTPYAASRDFDVKYVVPSFSAGGLVQAMVTYEGDRNESAVFVAIRNRLHVLGPDLKSVQSLATGPAGDPGCQTCAACGPGPHGPPGDTDTKVLVLDPALPALVSCGSSLQGRCFLHDLEPQGTAVHLAAPACLFSAHHNRPDDCPDCVASPLGTRVTVVEQGQASYFYVASSLDAAVAASFSPRSVSIRRLKADASGFAPGFVALSVLPKHLVSYSIEYVHSFHTGAFVYFLTVQPASVTDDPSALHTRLARLSATEPELGDYRELVLDCRFAPKRRRRGAPEGGQPYPVLRVAHSAPVGAQLATELSIAEGQEVLFGVFVTGKDGGPGVGPNSVVCAFPIDLLDTLIDEGVERCCESPVHPGLRRGLDFFQSPSFCPNPPGLEALSPNTSCRHFPLLVSSSFSRVDLFNGLLGPVQVTALYVTRLDNVTVAHMGTMDGRILQVELVRSLNYLLYVSNFSLGDSGQPVQRDVSRLGDHLLFASGDQVFQVPIQGPGCRHFLTCGRCLRAWHFMGCGWCGNMCGQQKECPGSWQQDHCPPKLTEFHPHSGPLRGSTRLTLCGSNFYLHPSGLVPEGTHQVTVGQSPCRPLPKDSSKLRPVPRKDFVEEFECELEPLGTQAVGPTNVSLTVTNMPPGKHFRVDGTSVLRGFSFMEPVLIAVQPLFGPRAGGTCLTLEGQSLSVGTSRAVLVNGTECLLARVSEGQLLCATPPGATVASVPLSLQVGGAQVPGSWTFQYREDPVVLSISPNCGYINSHITICGQHLTSAWHLVLSFHDGLRAVESRCERQLPEQQLCRLPEYVVRDPQGWVAGNLSARGDGAAGFTLPGFRFLPPPHPPSANLVPLKPEEHAIKFEYIGLGAVADCVGINVTVGGESCQHEFRGDMVVCPLPPSLQLGQDGAPLQVCVDGECHILGRVVRPGPDGVPQSTLLGILLPLLLLVAALATALVFSYWWRRKQLVLPPNLNDLASLDQTAGATPLPILYSGSDYRSGLALPAIDGLDSTTCVHGASFSDSEDESCVPLLRKESIQLRDLDSALLAEVKDVLIPHERVVTHSDRVIGKGHFGVVYHGEYIDQAQNRIQCAIKSLSRITEMQQVEAFLREGLLMRGLNHPNVLALIGIMLPPEGLPHVLLPYMCHGDLLQFIRSPQRNPTVKDLISFGLQVARGMEYLAEQKFVHRDLAARNCMLDESFTVKVADFGLARDILDREYYSVQQHRHARLPVKWMALESLQTYRFTTKSDVWSFGVLLWELLTRGAPPYRHIDPFDLTHFLAQGRRLPQPEYCPDSLYQVMQQCWEADPAVRPTFRVLVGEVEQIVSALLGDHYVQLPATYMNLGPSTSHEMNVRPEQPQFSPMPGNVRRPRPLSEPPRPT