wanglab/gogpt-training-data huggingface dataset:
Protein: ceramide glucosyltransferase (EC 2.4.1.80) (F4ITI0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Glycosyltransferase
- Sphingolipid delta
- Acetolactate synthase small subunit 1, chloroplastic
- Acetolactate synthase small subunit 2, chloroplastic
- Dihydroxy-acid dehydratase, chloroplastic
- At5g65170
- Succinate dehydrogenase iron-sulfur subunit 3, mitochondrial
- Sterol 3-beta-glucosyltransferase UGT80A2
- Ferritin/ribonucleotide reductase-like family protein
- Sterol 3-beta-glucosyltransferase UGT80B1
Sequence:
MSTLDSIDAILFSLSRAFTSPFAVFVQIQGCTICLLLALGWLLAEYVRNREVKRIKNSIKAGNSLAFLYQDINELEHSRQVKLPRVSVVMPLKGFGEHNLHNWRSQITSLYGGPLEFLFVVESTEDPAYHAVSRLLSMYQDHVEAKVVVAGLSTTCSQKIHNQLIGVEKMHKDTKYVLFLDDDVRLHPGTIGALTTEMEKNPEIFIQTGYPLDLPSGTLGSYCIYEYHMPCSMGFATGGRTFFLWGGCMMMHADDFRQDRYGVVSGLRDGGYSDDMTLASLAGAHKRLITSPPVAVFPHPLASDLSFGRYWNYLRKQTFVLESYISKVNWIMNKALFAVHCYLSWGFVAPYVMAIIHITSALRIYIKGYHQLEDTTSASGGMMLVITLAICTFIELLSMWNLTRREVQLCNMLSPEAPRLSLATYNWGLVFVAMLVDNFLYPISAFRSHFSQSINWSGIRYHLKDGKIFKIERRKDMGPTKTDLGGKHLYGKKGAPQKASFLSSLGRNLAHWRQPKKFDV
Protein: Diacylglycerol lipase-alpha (DAGL-alpha) (DGL-alpha) (EC 3.1.1.116) (Neural stem cell-derived dendrite regulator) (Sn1-specific diacylglycerol lipase alpha) (Q6WQJ1)
Organism: Mus musculus (Mouse)
Function: Serine hydrolase that hydrolyzes arachidonic acid-esterified diacylglycerols (DAGs) to produce the principal endocannabinoid (eCB), 2-arachidonoylglycerol (2-AG). Preferentially hydrolyzes sn-1 fatty acids from diacylglycerols (DAG) that contain arachidonic acid (AA) esterified at the sn-2 position to biosynthesize 2-AG. Has negligible activity against other lipids including monoacylglycerols and phospholipids. Plays a key role in regulating 2-AG signaling in the central nervous system (CNS). Controls the activity of 2-AG as a retrograde messenger at neuronal synapses. Supports axonal growth during development and adult neurogenesis. Plays a role for eCB signaling in the physiological regulation of anxiety and depressive behaviors. Regulates also neuroinflammatory responses in the brain, in particular, LPS-induced microglial activation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:17584991}; Multi-pass membrane protein {ECO:0000255}. Cell projection, dendritic spine membrane {ECO:0000269|PubMed:16723519}; Multi-pass membrane protein {ECO:0000255}. Postsynaptic density membrane {ECO:0000250|UniProtKB:Q9Y4D2}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:Q9Y4D2}; Multi-pass membrane protein {ECO:0000255}. Note=Cycles between the cell surface and an intracellular endosomal compartment. Internalized by early endosomes via a clathrin-independent pathway before transport back to the postsynaptic membrane surface in a PKC-dependent manner. {ECO:0000250|UniProtKB:Q9Y4D2}.
Interaction partners:
- Diacylglycerol lipase-beta
- N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D
- Fatty-acid amide hydrolase 1
- Monoglyceride lipase
Sequence:
MPGIVVFRRRWSVGSDDLVLPAIFLFLLHTTWFVILSVVLFGLVYNPHEACSLNLVDHGRGYLGILLSCMIAEMAIIWLSMRGGILYTEPRDSMQYVLYVRLAILVIEFIYAIVGIVWLTQYYTSCNDLTAKNVTLGMVVCNWVVILSVCITVLCVFDPTGRTFVKLRATKRRQRNLRTYNLRHRLEEGQATSWSRRLKVFLCCTRTKDSQSDAYSEIAYLFAEFFRDLDIVPSDIIAGLVLLRQRQRAKRNAVLDEANNDILAFLSGMPVTRNTKYLDLKNSHEMLRYKEVCYYMLFALAAYGWPMYLMRKPTCGLCQLARSCSCCLCPARPRFAPGVTIEEDNCCGCNAIAIRRHFLDENMTAVDIVYTSCHDAVYETPFYVAVDHDKKKVVISIRGTLSPKDALTDLTGDAERLPVEGHRGTWLGHKGMVLSAEYIKKKLEQEMVLSQAFGRDLGRGTKHYGLIVVGHSLGAGTAAILSFLLRPQYPTLKCFAYSPPGGLLSEDAMEYSKEFVTAVVLGKDLVPRIGLSQLEGFRRQLLDVLQRSTKPKWRIIVGATKCIPKSELPEDQVEVTTLASTRLWTHPSDLTIALSASTPLYPPGRIIHVVHNHPAEQCCCCEQEEPTYFAIWGDNKAFNEVIISPAMLHEHLPYVVMEGLNKVLENYNKGKTALLSAAKVMVSPTEVDLTPELIFQQQPLPTGPPLPTGLALELPATEHRNSSVRSKSQSEMSLEGFSEGRLLSPVAAASAARQDPVELLLLSTQERLAAELQSRRAPLATMESLSDTESLYSFDSRRSSGFRSIRGSPSLHAVLERDEGHLFYIDPAIPEENPSLSSRTELLAADSLSKHSQDTQPLEAALGSGGVTPERPPSATIEEEEAAGGSEGGGVAPRGELALHNGRLGDSPSPQVLEFAEFIDSLFNLDSKSSSFQDLYCMMVPESPTSDYTEGPKSPSQQEILLRAQFEPNLVPKPPRLFAGSAEPSSGISLSPSFPLSSSGELMDLTPTGLSSQECLATDKIRTSTPTGHGASPTKQDDLVISAR
Protein: Transcription factor PDR8 (Pleiotropic drug resistance protein 8) (Q06149)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Up-regulates the transcription of the genes for ATP-binding cassette (ABC) transporters YOR1 and PDR15, for major facilitator superfamily transporter AZR1, for pleiotropic drug resistance SNG1, for alpha-glucosidase YJL216C and for YLL056C.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227, ECO:0000269|PubMed:14562095}.
Interaction partners:
- Transcription factor PDR3
- Transcription factor PDR1
Sequence:
MDGSHFPMKSTTGEPVSSGKKGKRRKVIKSCAFCRKRKLKCSQARPMCQQCVIRKLPQCVYTEEFNYPLSNTELFEQVPNVALVQKIENLQTLLKENDNNNAKPVYCRSSENPLRSLRTSVLGDNGSRYVFGPTSWKTLSLFEQNKFQTEFQNLWKVLKPLPECTKSQLNENDVVADLPSFPQMESCIKSFFAGPLFGILHIFNQDDILSLLDRLFIRDTTDKNLVILLDLQGNAKDKYNLGIVLQILCLGYYNQDIPSSVSHFLHTLSAASLSSSSSNFVEKLQFFLLSYISVMINCTDGVWDATQGVDLINELCQGCISLGLNDIDKWYLNESEETKQNLRCIWFWALFLDVSTSYDIGNPPSISDDLLDLSIFTAQNFQSPSIDFRRVKLMHDFLDVSRFTTREIHKREMNEKLTTFSLRLIEFIQSNFSPIEHYTNSVYYSDIDPFDILILSRSLSIVASIYNIEMIIAQQSRIIDKNRMVQFLLISISVCVNTMVFHFKEPINDQENVLTEGLKLSIILINPLLIRIVSQVYSLAFNRLIFREKAFLFLIDLDTGKKIQFIKYEEENFDELLTGFDVRTDKFLSFSGTIIRFYEIIDSIFAVNERNKRLLKAVSNFYQLTSTLAFERVSRVLFDKASQARIETEKIWLKKGINMEHFSDLMIEDFINDVWKTFKEISKDLWSIDKKKFYKQYHFDL
Protein: MICAL-like protein 2 (Junctional Rab13-binding protein) (Molecule interacting with CasL-like 2) (MICAL-L2) (Q3TN34)
Organism: Mus musculus (Mouse)
Function: Effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecules transport to the plasma membrane and actin cytoskeleton reorganization. Regulates the endocytic recycling of occludins, claudins and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. In parallel, may regulate actin cytoskeleton reorganization directly through interaction with F-actin or indirectly through actinins and filamins. Most probably involved in the processes of epithelial cell differentiation, cell spreading and neurite outgrowth.
Subcellular location: Cell membrane; Peripheral membrane protein. Cell junction, tight junction {ECO:0000269|PubMed:18094055, ECO:0000269|PubMed:18332111, ECO:0000269|PubMed:23100251, ECO:0000269|PubMed:23890175}. Recycling endosome {ECO:0000269|PubMed:16525024}. Cell projection, neuron projection {ECO:0000269|PubMed:20008558}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:23100251, ECO:0000269|PubMed:23890175}.
Interaction partners:
- Ras-related protein Rab-13
- Ras-related protein Rab-8A
- Alpha-actinin-4
- Ras-related protein Rab-8B
- Ras-related protein Rab-12
- Alpha-actinin-1
Sequence:
MAAIKALQEWCRQQCEGYRDVSITNMTTSFRDGLAFCAILHRHRPDLINFSALRKENIYENNKLAFQVAEEQLGIPALLDAEDMVALKVPDRLSILTYVSQYYNYFHGRSPIGGMAGIKRPSSDSTEELSGKKGLSQPAKLPSPAQTQRSPLSPARTNPVVQRNEGGSQRPSPKAAPGTAGSSVSSICGVCGKHVHLVQRHLADGRLYHRSCFRCKQCSSTLHSGAYRATGEPGVFVCTHHSSEVTSVSPKSSNLASRKPGGVTADTRPFGVSWTVQEANGEGTPLRVRTAAWEHAGGNTTAKGFVQTELKPPSTSQVHVGSSAGPKLPTITVTTTSVTSKALTHVTNSSPIGWSSPAQSSPANFNSRPVVSPSARNTHLPGSQGQTASKGVKTQLNLNSESSNTAVTPAWTSSASKTQQAREKFFQTPPSAPAPASAPAPAPTSKVPTVVTVPTSKVPNVVTAPTSKVPTVVTVPTSKVPTVVSAPTSKVPTVVSAPTSKVPTVVNSTNSRVTTVVNAPTSKVPTVVSATNGRVPTVVTAHTGRVPAVMNTSASKVSPVVDAPAQESSREQALSVLRKALPALTGSGTQAPNRSFPATSSVLVTLPKNEVPQKVPSDKLSALTTQTPNFTIKLEPSAPVNVGNTAVFLQAGKKSPSISPRVGKTSVGSRPQAEVAGVKGPGPISQEGQEEGPEGWRARLKPVDKKTPAGRSLEQKEPVLAEPRIGDTSRKASSSSDSSVHITLTSIQHKRKPCPAGSGPSPAALSPSPSHRKKLAVPPSLDVSADWLQPEPKKQEDGTRSCKEEKSPTRWSRERSAVLDSGLAPPGEAVTSPVRLHPDYIPQEELQRQLQDIESQLDALELRGVELEKRLRAAEGDASEDSLMVDWFRLIHEKQLLLRLESELMYKSKDQRLEEQQLDLQGELRRLMDKPEGLKSPQDRQREQELLSQYVNTVNDRSDIVDFLDEDRLREQEEDQMLENMIQNLGLQRKKSKSFLSKIWSSKSKSGQA
Protein: GH02705p (P130CAS, isoform B) (P130CAS, isoform F) (Q95U71)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MMSSPRQNASGSEFETYDIPKPATPVPLNYDSPRSGLPKASNSTTTSSSSLGTRFETLKSVAASIAEESYDVPRPLILGSNQLQQQMSQMTPSSSASSLLTSDSLSLSFSSSNRSSLANMPDYDIPRRNPLPVRRQQSGLTYDFPLPPLQEQVPRVLCTPSTVTTTKELPLELSSALETLAKLQLQTTAAINRLLSFVVPNWRTRAQLEPAIMDLKLAALRLRTTLHDLAEFGEGALGNATRSEDRNLALKLRPLVRALRDANKLIHDSSESLDAQGAWSIDQLARSDEKHGCRPPDALDQLMVCAQTLTEDVRSTTSFIQGNASLLFKRQLTVGHNGGSGTGVLEGSRGSAEWLEDYDYVAFESKDAAARKNEALREAIPADLKTQFDTVIRTAESSAMGAGSGSIPTTPTARTTPTTPCKSPEMTDKDKKLVRYYAQQISTHMGNLMQAIDSFLETVEKNQPPKFFIAYGKFVVVSAHNLVTIGDNVYRNISKEALREKILRCTNALSDALKTCVLKSKKAAAHFPSGSAVQEMVDSVVHINNLARDLKSVMLQAVHLSTAAGVGA
Protein: Protein bric-a-brac 2 (Q9W0K4)
Organism: Drosophila melanogaster (Fruit fly)
Function: Probably acts as a transcriptional regulator. Required for the specification of the tarsal segment. Also involved in antenna development.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00320, ECO:0000269|PubMed:11973274}.
Interaction partners:
- TBP-associated factor 3
Sequence:
MDMTKQIVDFEIKSELIGEIDQFEASDYTMAPPEEPKMVEESPQLGHLEDQNRKYSPEREVEPTLQDPSEVVDQMQKDTESVGEVKSPEKDVETELVKSKASPMNDQALTPPPRPLTSSEVVGLRDPEHTELRMCLEAKKSRSLPVSPQPQPNLKLAGSALFEFGQRSSPVETKIKTNPETKPPRRKIVPPSGEGQQFCLRWNNYQSNLTNVFDELLQSESFVDVTLSCEGHSIKAHKMVLSACSPYFQALFYDNPCQHPIIIMRDVSWSDLKALVEFMYKGEINVCQDQINPLLKVAETLKIRGLAEVSAGRGEGGASALPMSAFDDEDEEEELASATAILQQDGDADPDEEMKAKRPRLLPEGVLDLNQRQRKRSRDGSYATPSPSLQGGESEISERGSSGTPGQSQSQPLAMTTSTIVRNPFASPNPQTLEGRNSAMNAVANQRKSPAPTATGHSNGNSGAAMHSPPGGVAVQSALPPHMAAIVPPPPSAMHHHAQQLAAQHQLAHSHAMASALAAAAAGAGAAGAGGAGSGSGSGASAPTGGTGVAGSGAGAAVGSHHDDMEIKPEIAEMIREEERAKMIESGGHGGWMGAAAAATGAASVAADSYQYQLQSMWQKCWNTNQQNLVQQLRFRERGPLKSWRPEAMAEAIFSVLKEGLSLSQAARKFDIPYPTFVLYANRVHNMLGPSLDGGADPRPKARGRPQRILLGMWPEELIRSVIKAVVFRDYREIKEDMSAHQYANGQGHGTYIGGGTTTNGYHSAAAAKLAAQNAALAPPDAGSPLSSMTETLRRQILSQQQQHQQHHQQQAHHQQQPSHHQQQSPHAQSMNMYKSPAYLQRSEIEDQVSAAAAVAAAAAKHQQQQGERRGSENLPDLSALGLMGLPGLNVMPSRGSGGGSGGAAPNSAASYARELSRERERDRERERERELSRQYGSQSRGSSSGSGSAKSLTASQRPGAASPYSAAHYAKHQASAYNKRFLESLPAGIDLEAFANGLLQKSVNKSPRFEDFFPGPGQDMSELFANPDASAAAAAAAYAPPGAIRESPLMKIKLEQQHATELPHED
Protein: S-adenosylmethionine synthase (AdoMet synthase) (EC 2.5.1.6) (MAT) (Methionine adenosyltransferase) (Q729A3)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Function: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00086}.
Interaction partners:
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
- Methionine synthase
- Adenosylhomocysteinase
- Cytosine-specific methyltransferase
- Cytosine-specific methyltransferase
- Cytosine-specific methyltransferase
- 6,7-dimethyl-8-ribityllumazine synthase
- Methylenetetrahydrofolate reductase
- Serine hydroxymethyltransferase
- GMP synthase
Sequence:
MIPSKGKYYFTSESVTEGHPDKVADQISDAVLDVLLAQDPNSRVACETLVTTGMAVIAGEITTRGYADLPHVVRETIRNIGYNSSEMGFDWQTCAVISSIDKQSADIAQGVDRATNEDQGAGDQGMMFGFACDETATLMPAPIYWAHQLSQRLTEVRKDGTVDIFRPDGKTQVSFEYVDGKPVRINNVVVSTQHKDSASQADIIDAVKTHVIRPILEPSGFFDEKACDIFINTTGRFVIGGPMGDCGLTGRKIIQDTYGGMGHHGGGAFSGKDASKVDRSGAYMARYIAKNVVASGLAPKCEVQIAYCIGVAEPVSVLVSSQGTASVPDEVLTRAVREVFDLRPFHITRRLDLLRPIYGKTSCYGHFGRELPEFTWEHTDAAADLRTAAKV
Protein: Histone-lysine N-methyltransferase, H3 lysine-9 specific SUVH8 (EC 2.1.1.-) (EC 2.1.1.367) (Histone H3-K9 methyltransferase 8) (H3-K9-HMTase 8) (Protein SET DOMAIN GROUP 21) (Suppressor of variegation 3-9 homolog protein 8) (Su(var)3-9 homolog protein 8) (Q9C5P0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Histone methyltransferase. Methylates 'Lys-9' of histone H3. H3 'Lys-9' methylation represents a specific tag for epigenetic transcriptional repression.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00358}. Chromosome, centromere {ECO:0000250}. Note=Associates with centromeric constitutive heterochromatin. {ECO:0000250}.
Interaction partners:
- Histone H3.1
- Histone H3-like 3
- Histone H3-like 4
- Histone H3-like 1
- Histone H3-like 2
- Histone H3-like 5
- Histone H3.3
- Histone H3-like centromeric protein CENH3
- Histone-lysine N-methyltransferase ATXR3
- Fimbrin-4
Sequence:
MVSTPPTLLMLFDDGDAGPSTGLVHREKSDAVNEEAHATSVPPHAPPQTLWLLDNFNIEDSYDRDAGPSTGPVHRERSDAVNEEAHATSIPPHAPPQTLWLLDNFNIEDSYDRDAGPSTSPIDREASHEVNEDAHATSAPPHVMVSPLQNRRPFDQFNNQPYDASAGPSTGPGKRGRGRPKGSKNGSRKPKKPKAYDNNSTDASAGPSSGLGKRRCGRPKGLKNRSRKPKKPKADDPNSKMVISCPDFDSRITEAERESGNQEIVDSILMRFDAVRRRLCQLNYRKDKILTASTNCMNLGVRTNMTRRIGPIPGVQVGDIFYYWCEMCLVGLHRNTAGGIDSLLAKESGVDGPAATSVVTSGKYDNETEDLETLIYSGHGGKPCDQVLQRGNRALEASVRRRNEVRVIRGELYNNEKVYIYDGLYLVSDCWQVTGKSGFKEYRFKLLRKPGQPPGYAIWKLVENLRNHELIDPRQGFILGDLSFGEEGLRVPLVNEVDEEDKTIPDDFDYIRSQCYSGMTNDVNVDSQSLVQSYIHQNCTCILKNCGQLPYHDNILVCRKPLIYECGGSCPTRMVETGLKLHLEVFKTSNCGWGLRSWDPIRAGTFICEFTGVSKTKEEVEEDDDYLFDTSRIYHSFRWNYEPELLCEDACEQVSEDANLPTQVLISAKEKGNVGRFMNHNCWPNVFWQPIEYDDNNGHIYVRIGLFAMKHIPPMTELTYDYGISCVEKTGEDEVIYKGKKICLCGSVKCRGSFG
Protein: Tryptophan synthase alpha chain (EC 4.2.1.20) (Indole synthase) (Indole-3-glycerol-phosphate lyase) (EC 4.1.2.8) (O22765)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate (By similarity). Contributes to the tryptophan-independent indole biosynthesis, and possibly to auxin production.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18844775}.
Interaction partners:
- Tryptophan synthase beta chain 1, chloroplastic
- Tryptophan synthase
- Tryptophan synthase beta chain 2, chloroplastic
- indole-3-glycerol-phosphate synthase
- tryptophan synthase
- Indole-3-glycerol phosphate synthase, chloroplastic
- Anthranilate phosphoribosyltransferase, chloroplastic
- N-
- N-
- Anthranilate phosphoribosyltransferase
Sequence:
MDLLKTPSSTVGLSETFARLKSQGKVALIPYITAGDPDLSTTAKALKVLDSCGSDIIELGVPYSDPLADGPAIQAAARRSLLKGTNFNSIISMLKEVIPQLSCPIALFTYYNPILRRGVENYMTVIKNAGVHGLLVPDVPLEETETLRNEARKHQIELVLLTTPTTPKERMNAIVEASEGFIYLVSSVGVTGTRESVNEKVQSLLQQIKEATSKPVAVGFGISKPEHVKQVAEWGADGVIVGSAMVKILGESESPEQGLKELEFFTKSLKSALVS
Protein: Putative uncharacterized oxidoreductase YDR541C (EC 1.1.1.-) (Q03049)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Uncharacterized oxidoreductase YDL114W
- Small ribosomal subunit protein uS19
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein eL32
- Large ribosomal subunit protein uL23
- Small ribosomal subunit protein eS21B
- Small ribosomal subunit protein uS15
- Ubiquitin-ribosomal protein eS31 fusion protein
- Large ribosomal subunit protein uL15
Sequence:
MSNTVLVSGASGFIALHILSQLLKQDYKVIGTVRSHEKEAKLLRQFQHNPNLTLEIVPDISHPNAFDKVLQKRGREIRYVLHTASPFHYDTTEYEKDLLIPALEGTKNILNSIKKYAADTVERVVVTSSCTAIITLAKMDDPSVVFTEESWNEATWESCQIDGINAYFASKKFAEKAAWEFTKENEDHIKFKLTTVNPSLLFGPQLFDEDVHGHLNTSCEMINGLIHTPVNASVPDFHSIFIDVRDVALAHLYAFQKENTAGKRLVVTNGKFGNQDILDILNEDFPQLRGLIPLGKPGTGDQVIDRGSTTDNSATRKILGFEFRSLHESVHDTAAQILKKQNRL
Protein: Large ribosomal subunit protein uL4 (60S ribosomal protein L1) (60S ribosomal protein L4) (P36578)
Organism: Homo sapiens (Human)
Function: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23636399}.
Interaction partners:
- Small ribosomal subunit protein uS17
- Large ribosomal subunit protein eL28
- Small ribosomal subunit protein eS27
- Large ribosomal subunit protein uL3
- Large ribosomal subunit protein eL31
- Large ribosomal subunit protein eL37
- Large ribosomal subunit protein eL33
- Small ribosomal subunit protein eS26
- Large ribosomal subunit protein eL20
- Elongation factor 2
Sequence:
MACARPLISVYSEKGESSGKNVTLPAVFKAPIRPDIVNFVHTNLRKNNRQPYAVSELAGHQTSAESWGTGRAVARIPRVRGGGTHRSGQGAFGNMCRGGRMFAPTKTWRRWHRRVNTTQKRYAICSALAASALPALVMSKGHRIEEVPELPLVVEDKVEGYKKTKEAVLLLKKLKAWNDIKKVYASQRMRAGKGKMRNRRRIQRRGPCIIYNEDNGIIKAFRNIPGITLLNVSKLNILKLAPGGHVGRFCIWTESAFRKLDELYGTWRKAASLKSNYNLPMHKMINTDLSRILKSPEIQRALRAPRKKIHRRVLKKNPLKNLRIMLKLNPYAKTMRRNTILRQARNHKLRVDKAAAAAAALQAKSDEKAAVAGKKPVVGKKGKKAAVGVKKQKKPLVGKKAAATKKPAPEKKPAEKKPTTEEKKPAA
Protein: Leucine rich repeats and calponin homology domain containing 3 (E9PD99)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAAAGLVAVAAAAEYSGTVASGGNLPGVHCGPSSGAGPGFGPGSWSRSLDRALEEAAVTGVLSLSGRKLREFPRGAANHDLTDTTRAELAELPLIRLDFSCNKITTIPVCYRNLRHLQTITLDNNPLQSPPAQICIKGKVHIFKYLNIQACKIAPDLPDYDRRPLGFGSCHEELYSSRPYGALDSGFNSVDSGDKRWSGNEPTDEFSDLPLRVAEITKEQRLRRESQYQENRGSLVVTNGGVEHDLDQIDYIDSCTAEEEEAEGSPVKPVAIREFQKTEDMRRYLHQNRVPAEPSSLLSLSASHNQLSHTDLELHQRREQLVERTRREAQLAALQYEEEKIRTKQIQRDAVLDFVKQKASQSPQKQHPLLDGVDGECPFPSRRSQHTDDSALCMSLSGLNQVGCAATLPHSSAFTPLKSDDRPNALLSSPATETVHHSPAYSFPAAIQRNQPQRPESFLFRAGVRAETNKGHASPLPPSAAPTTDSTDSITGQNSRQREEELELIDQLRKHIEYRLKVSLPCDLGAALTDGVVLCHLANHVRPRSVPSIHVPSPAVPKLTMAKCRRNVENFLEACRKIGVPQEQLCLPLHILEEKGLSQVAVTVQALLELAPPKQQQHQLSAV
Protein: Insulin-like growth factor 2 mRNA-binding protein 3 (IGF2 mRNA-binding protein 3) (IMP-3) (Decapentaplegic and Vg-related 1 RNA-binding protein) (IGF-II mRNA-binding protein 3) (VICKZ family member 3) (Vg1 RNA-binding protein) (Vg1-RBP) (Q9PW80)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: RNA-binding factor that may recruit target transcripts to cytoplasmic protein-RNA complexes (mRNPs). This transcript 'caging' into mRNPs allows mRNA transport and transient storage. It also modulates the rate and location at which target transcripts encounter the translational apparatus and shields them from endonuclease attacks or microRNA-mediated degradation (By similarity). Preferentially binds to N6-methyladenosine (m6A)-containing mRNAs and increases their stability (By similarity). Involved in neuronal crest migration.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10525193}. Nucleus {ECO:0000250}. Cytoplasm, P-body {ECO:0000250|UniProtKB:O00425}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:O00425}. Note=Accumulates along the vegetal cortex as oogenesis progresses. Colocalizes to extended processes in migrating neuronal crest cells.
Interaction partners:
- RNA demethylase ALKBH5
- YTH domain-containing family protein
- YTH domain-containing family protein 2
- YTH domain containing 2.
- YTH domain-containing 1.
Sequence:
MNKLYIGNVSEQASALDLESIFEQWKIPFSAPFLVKSGYAFVDCPDEKVAMRAIDTLSGKVELHGKVLEVEHSVPKRQRSCKLQIRNIPPHMQWEVLDGLLAQYGTVESCEQVNTDTETAVVNVRYGAKDQAREAMDKLNGFLMENYALKVSYIPDETAAADAPAVGGRRGFNPRGPPRQGSPSLGARPKLQSDVPLRLLVPTQFVGAIIGKEGATIRNITKQTHSKIDIHRKENAGAAEKPITVHSTPEGCSSACRNIMEIMQKEAIDTKITEEIPLKILAHNNFVGRLIGKEGRNLKKIEQDTDTKITISPLQDLTLYNPERTITVKGTLDACAKAEEEIMKKVRESYENDVAAMHLQSNLIPGLNLNALGLFPGAASGGISPSVVSGPPPGAQAGYQSFGAQMESETVHLFIPALAVGAIIGKQGQHIKQLSRFAGASIKIAPADGIDAKQRMVIISGPPEAQFKAQGRIFGKLKEENFFGPKEEVKLEAHIKVPSFAAGRVIGKGGKTVNELQNLTSAEVVVPRDQTPDENDQVVVKITGHFYASQLAQRKIQEIISQVRRQQQPKPSAAGPPVARRK
Protein: ABC transporter ATP-binding/permease protein Rv1747 (EC 7.-.-.-) (O65934)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in the translocation of an unknown substrate across the membrane. Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation. Required for virulence.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Multifunctional 2-oxoglutarate metabolism enzyme
- Serine/threonine-protein kinase PknF
- Serine/threonine-protein kinase PknB
- Serine/threonine-protein kinase PknD
- DUF4129 domain-containing protein
- Probable fatty acid synthase Fas
- Phenolphthiocerol/phthiocerol polyketide synthase subunit C
- Probable multifunctional mycocerosic acid synthase membrane-associated Mas
- Mycoketide-CoA synthase
- Mycocerosic acid synthase-like polyketide synthase
Sequence:
MPMSQPAAPPVLTVRYEGSERTFAAGHDVVVGRDLRADVRVAHPLISRAHLLLRFDQGRWVAIDNGSLNGLYLNNRRVPVVDIYDAQRVHIGNPDGPALDFEVGRHRGSAGRPPQTTSIRLPNLSAGAWPTDGPPQTGTLGSGQLQQLPPATTRIPAAPPSGPQPRYPTGGQQLWPPSGPQRAPQIYRPPTAAPPPAGARGGTEAGNLATSMMKILRPGRLTGELPPGAVRIGRANDNDIVIPEVLASRHHATLVPTPGGTEIRDNRSINGTFVNGARVDAALLHDGDVVTIGNIDLVFADGTLARREENLLETRVGGLDVRGVTWTIDGDKTLLDGISLTARPGMLTAVIGPSGAGKSTLARLVAGYTHPTDGTVTFEGHNVHAEYASLRSRIGMVPQDDVVHGQLTVKHALMYAAELRLPPDTTKDDRTQVVARVLEELEMSKHIDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDPALDRQVMTMLRQLADAGRVVLVVTHSLTYLDVCDQVLLLAPGGKTAFCGPPTQIGPVMGTTNWADIFSTVADDPDAAKARYLARTGPTPPPPPVEQPAELGDPAHTSLFRQFSTIARRQLRLIVSDRGYFVFLALLPFIMGALSMSVPGDVGFGFPNPMGDAPNEPGQILVLLNVGAVFMGTALTIRDLIGERAIFRREQAVGLSTTAYLIAKVCVYTVLAVVQSAIVTVIVLVGKGGPTQGAVALSKPDLELFVDVAVTCVASAMLGLALSAIAKSNEQIMPLLVVAVMSQLVFSGGMIPVTGRVPLDQMSWVTPARWGFAASAATVDLIKLVPGPLTPKDSHWHHTASAWWFDMAMLVALSVIYVGFVRWKIRLKAC
Protein: Rifin (Q9NFB3)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKIHYTNILLFPLKLNILVNTHKKPSITSRHIQTTRLLCECELYTPNYDNDPEMKSVMQQFHDRTTQRFHEYDENLKEKRQKCKDKCDKEIQKIILKDKIEKELTEKFSSLQTDIHSDAIPTCICEKSLADKVEKNCLKCTQNLGKIVAPSSGVLAGISEAALSVWKTTEIAAAMELAKQAGAAAGLKAGHLAGTNAVIEQLRTLGIYFVGDKLLETIIDVTNYMNVSFIYDKVYSHYTTSCTPSLVNDQLVGTFNTSDPFCNLVHSNLQGSFYRSSAQTIIYEKVEEAVAGAEQAATTKTAVMTPIYTTEFTAKNIAEVEAATTSYYTPIIASIVAIVIIVLIMVIIYLILRYRRKMKLKKKLQYIKLLEE
Protein: AMP deaminase 3 (EC 3.5.4.6) (AMP deaminase isoform E) (Erythrocyte AMP deaminase) (Q01432)
Organism: Homo sapiens (Human)
Function: AMP deaminase plays a critical role in energy metabolism.
Interaction partners:
- Adenylosuccinate synthetase isozyme 2
- Adenine phosphoribosyltransferase
- Adenosine kinase
- Adenylosuccinate lyase
- Inosine-5'-monophosphate dehydrogenase 2
- Inosine-5'-monophosphate dehydrogenase 1
- Hypoxanthine-guanine phosphoribosyltransferase
- GMP reductase 1
- Adenylosuccinate synthetase isozyme 1
- Bifunctional purine biosynthesis protein ATIC
Sequence:
MPRQFPKLNISEVDEQVRLLAEKVFAKVLREEDSKDALSLFTVPEDCPIGQKEAKERELQKELAEQKSVETAKRKKSFKMIRSQSLSLQMPPQQDWKGPPAASPAMSPTTPVVTGATSLPTPAPYAMPEFQRVTISGDYCAGITLEDYEQAAKSLAKALMIREKYARLAYHRFPRITSQYLGHPRADTAPPEEGLPDFHPPPLPQEDPYCLDDAPPNLDYLVHMQGGILFVYDNKKMLEHQEPHSLPYPDLETYTVDMSHILALITDGPTKTYCHRRLNFLESKFSLHEMLNEMSEFKELKSNPHRDFYNVRKVDTHIHAAACMNQKHLLRFIKHTYQTEPDRTVAEKRGRKITLRQVFDGLHMDPYDLTVDSLDVHAGRQTFHRFDKFNSKYNPVGASELRDLYLKTENYLGGEYFARMVKEVARELEESKYQYSEPRLSIYGRSPEEWPNLAYWFIQHKVYSPNMRWIIQVPRIYDIFRSKKLLPNFGKMLENIFLPLFKATINPQDHRELHLFLKYVTGFDSVDDESKHSDHMFSDKSPNPDVWTSEQNPPYSYYLYYMYANIMVLNNLRRERGLSTFLFRPHCGEAGSITHLVSAFLTADNISHGLLLKKSPVLQYLYYLAQIPIAMSPLSNNSLFLEYSKNPLREFLHKGLHVSLSTDDPMQFHYTKEALMEEYAIAAQVWKLSTCDLCEIARNSVLQSGLSHQEKQKFLGQNYYKEGPEGNDIRKTNVAQIRMAFRYETLCNELSFLSDAMKSEEITALTN
Protein: Adenylate kinase isoenzyme 6 homolog (AK6) (DAK6) (EC 2.7.4.3) (Dual activity adenylate kinase/ATPase) (AK/ATPase) (Q7JYV7)
Organism: Drosophila melanogaster (Fruit fly)
Function: Broad-specificity nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. AMP is the best phosphate acceptor, and CMP is also a good substrate. All nucleoside triphosphates ATP, TTP, CTP, GTP, and UTP are accepted as phosphate donors. ATP is the best phosphate donor. May have a role in nuclear energy homeostasis.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03173}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03173}.
Interaction partners:
- Adenylate kinase 1
- Adenylate kinase 2
- RNA-binding protein NOB1
- Adenosine kinase
- Adenosine kinase
- Adenosine kinase
- Ribonucleoside-diphosphate reductase large subunit
- Adenine phosphoribosyltransferase
- Nucleoside diphosphate kinase
- Nucleoside diphosphate kinase
Sequence:
MSEPEPDVKPNILITGTPGAGKSYLCERIASELKFEWLDCSKIAKEKNFVEEYDEEYDCPILDEEKLMDHLEPLMAKGGNVVEYHGCDFFPERWFQAVFVVTCPNTTLYDRLKERNYNEKKLASNIQCEIFGTILEEARDSYKSDIVFELKGETKADAHISIKTVKNWYRMWKRK