wanglab/gogpt-training-data huggingface dataset:
Protein: LD06925p (Pico, isoform A) (Q9VWB7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- GIGYF family protein Gyf
- Ras-related protein Rap1
- Abelson interacting protein, isoform D
- Rhea, isoform B
- Adapter molecule Crk
- Tyrosine-protein kinase
- Protein enabled
- Growth factor receptor-bound protein 2
- DShc protein
Sequence:
MDCGGIAAHQQQQLQQQQLHLLQQQLQQQHHQQQRQQQQHSLEEAATITNINLRGILVGGAASSAGVAGAAAGGATTTTTTTTAAGFVAGGDCPVIGAGAGAGVKLRRHSDRPLTPEAKQLSHTYRISMANLEDSQESELDQILGELSLLEAQISYTEASMLPAMCAPSAGAQIAPPPGVTQLPGSAPTMVSMSASSSRSHSRTNSTISADVSSCSSSGISENGHGLGLVLGGPGSAGMMVQPPPPGGMTMGITLGVVTPREPRTESPDNDSAFSDTVSLLSSESSASSNTSLQQQQQQQQQQHHQHQQHHQHQQQQQKPQLAGAEKLHHHGVHGQHGGQQSGANSITKADKIQLALHKLESAPIRRLFVKAFTSDGASKSLLVDERMGCGHVTRLLADKNHVQMQSNWALVEHLGDLQMERLFEDHELLVDNLMTWHSDAGNRVLFQQRPDKVTLFLRPELYLPGPQMAPGCQHDEQTRQMLLDEFFDSHNQLQMDGPLYMKADPKKGWKRYHFVLRSSGLYYFPKEKTKNTRDLACLNLFHGHNVYTGLGWRKKWKSPTDYTFGFKAVGDSSLGKSCRSLKMLCAEDLPTLDRWLTAIRVCKYGKQLWDSHKSLLEDLCLSRDDAVSQSSFAASMRSESISSISSAVPSQCGSVSSAISSMSNSTSGRTSRASSSSSSGCLSDDNNAFDSEFTTGTIKRKPSMKPNLPLTTMTRQLKEVGEITICESAGGDASSPERSGTLTRRHSRRKSQESNGSGTLKRRPIAVPVATVVKQTEPMGSASSTSSSSNSTPTPTPSICAKPPPGDSASLMCSSTLSLDSLPPPPPPPALDGSEDQDVYGSQLSLASLPPPPPPEDVLAMNYAEPSSPSTPTPMSTPMIMPNSNGSLPPAVPAKPMKPAVKQAAGGLKAAPPYKAPPDYVGPALLPGPPLPPPPPAQKKVSFADSPVLLRRKMCSPEPVLPQRSPSTTLSCHSSSSAGSAYQTYAPGPMLPPRADVARLSSLSNGSSSEVTSPKRLQESASNPPRDFLKDLQRVMRKKWQVAQKCKAEPATTPHEVLGFRDFSNEDLLAAHNLNSGANSSHYYRETANVSHWVRKHYEYAHNALYENVHAQSAAAAGVPGSGEATTPPLPPPPGNSVAAKKRPPPPPPKRSDKTHLTNRV
Protein: Protein FATTY ACID EXPORT 3, chloroplastic (At-FAX3) (Q9ZVH7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in free fatty acids export from the plastids.
Subcellular location: Plastid, chloroplast membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Protein FATTY ACID EXPORT 4, chloroplastic
- Protein FATTY ACID EXPORT 2, chloroplastic
- Uncharacterized protein At5g03900
- 6,7-dimethyl-8-ribityllumazine synthase
- Alpha/beta-Hydrolases superfamily protein
- Inner membrane localized protein
- Low-density receptor-like protein
- Zinc finger/BTB domain protein
- Protein PAM71-homolog, chloroplastic
- Mitochondrial substrate carrier family protein
Sequence:
MMSIPMELMSIRNPNSTLLYRAHSRPPVKLCAPPRSLLPSRRHFSAPRAVVSYPGIRFGFTSPEVLLNRSVVAFAASHEDSGESGVEVGKEKSDIDVEDDTSKEAWKQTLESFKEQVSKMQSVSSEAYSVNSQKAMTVLKETSEQLRIQAEKAKEELGTKAKVVSEEGREYILKAAEESPSDVKEIVEAFASTEDLKNVSRANDFHVGIPYGLLLLVGGFINFMVSGSIPAIRFGVILGGALFALSLASLKSHRKGESSTKFLKGQMAIVAIIFLRELRLLLSQKSTFLGFFTTLTSGGVLGFYLYKMVVKREKGPTLEDGGEDESSDGFVRSEG
Protein: Probable rhodanese domain-containing dual specificity protein phosphatase (EC 3.1.3.16) (EC 3.1.3.48) (Q556Y8)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Has a dual specificity toward Ser/Thr and Tyr-containing proteins.
Interaction partners:
Sequence:
MVLINRVNIQPEELPLLYHVNSMDVYNLLQDIGSSKIIIDLRTKEQYEKNHIRTSVNIPPPPSTTPLYENGEIKEFNLSKYIGSNVTAKHWNLIFQKLIVYSDKPFLYNIDELEKTISTTTITTTATTTTTTTTTSNSIGSDQDIIKSLKVSDWDKVVLRHFLLKKKKTKVIIYQGGFDQFQKDYSFMCNPSSSPSSSSGGGGGSQLYPSEIIKDFLYLGGAENAGNRQQLINLKITHLVNMAGELDDVYPHLYKYYRANLDDRPKANIYEHFEPVIQFINDCKKQGGRVLIHCAMGISRSTTVVLAYLMKEDHMTYSDAFTFCKQKRSCINPNFGFVKQLKDYQQHLTLEWEKQEKLKKQQQQTLNINNNNTGIPLSKKLQLDVSDPLSNSSPSSPLISSTLPIPETPPAIILKNEVASPCPIKTTTSSTTINNKGQQQDKAQEEKDSIFSYADKQEKMTHPTLHSPIELPQSSL
Protein: Probable transcriptional regulator (Q9HXW2)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- HTH gntR-type domain-containing protein
- Probable Resistance-Nodulation-Cell Division
Sequence:
MSESTSSVGPGRPKDPAKREAILEAAKRLFLCNGYDGSSMEAIASEAGVSKLTVYSHFTDKETLFSEAVKAKCAEQLPALYFQLAEGAPLEKVLLNIARGFHRLINSHEAIALTRLMAAQAGQNPKLSELFFEAGPKQVIDEMERLLEQARRSGKLAFPDARHAAEHFFMLVKGCANYRLLIGCAEPLDEAEGERHVEEVVALFLRAFAAGG
Protein: FT-interacting protein 4 (Multiple C2 domain and transmembrane region protein 4) (Q9C8H3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for proliferation and differentiation of shoot stem cells in the shoot apical meristem (SAM), thus determining the appropriate balance between the maintenance of shoot stem cells and their differentiation into other aboveground plant parts via the control of subcellular localization and intercellular trafficking of STM in the shoot apex. Prevents intracellular trafficking of STM to the plasma membrane in cells in the peripheral shoot meristem region thus facilitating STM recycling to the nucleus to maintain stem cells.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9FL59}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:29259105, ECO:0000269|PubMed:29742441}. Vesicle {ECO:0000269|PubMed:29742441}. Cell membrane {ECO:0000269|PubMed:29259105, ECO:0000269|PubMed:29742441}; Multi-pass membrane protein {ECO:0000255}. Endosome membrane {ECO:0000269|PubMed:29259105, ECO:0000269|PubMed:29742441}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:29742441}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Plasmodesmata-located protein 6
- Plasmodesmata-located protein 2
- Plasmodesmata-located protein 7
- Protein FLOWERING LOCUS T
Sequence:
MQRPPPEDFSLKETKPHLGGGKVTGDKLTTTYDLVEQMQYLYVRVVKAKELPGKDLTGSCDPYVEVKLGNYRGTTRHFEKKSNPEWNQVFAFSKDRVQASYLEATVKDKDLVKDDLIGRVVFDLNEIPKRVPPDSPLAPQWYRLEDGKGQKVKGELMLAVWFGTQADEAFPEAWHSDAATVSGTDALANIRSKVYLSPKLWYLRVNVIEAQDLIPSDKGRYPEVFVKVIMGNQALRTRVSQSRSINPMWNEDLMFVVAEPFEEPLILSVEDRVAPNKDEVLGRCAVPLQYLDKRFDYRPVNSRWFNLEKHVIMEGGEKKEIKFASKIHMRICLEGGYHVLDESTHYSSDLRPTAKQLWKPNIGVLELGVLNATGLMPMKAKEGGRGTTDAYCVAKYGQKWIRTRTIIDSFTPRWNEQYTWEVFDPCTVVTVGVFDNCHLHGGDKNNGGGKDSRIGKVRIRLSTLEADRVYTHSYPLLVLHPSGVKKMGEIHLAVRFTCSSLLNMMYMYSMPLLPKMHYLHPLTVSQLDNLRHQATQIVSTRLTRAEPPLRKEVVEYMLDVGSHMWSMRRSKANFFRIMGVLSGIIAVGKWFEQICVWKNPITTVLIHILFIILVIYPELILPTIFLYLFLIGVWYYRWRPRHPPHMDTRLSHADSAHPDELDEEFDTFPTSRPSDIVRMRYDRLRSIAGRIQTVVGDLATQGERFQSLLSWRDPRATALFVLFCLIAAVILYITPFQVVAFAIGLYVLRHPRLRYKLPSVPLNFFRRLPARTDCML
Protein: NET1-associated nuclear protein 1 (U three protein 17) (t-17) (U3 protein 17 required for transcription) (U3 small nucleolar RNA-associated protein 17) (U3 snoRNA-associated protein 17) (Q02931)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in nucleolar processing of pre-18S ribosomal RNA. Required for optimal pre-ribosomal RNA transcription by RNA polymerase I together with a subset of U3 proteins required for transcription (t-UTPs).
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:12068309, ECO:0000269|PubMed:15489292}. Note=Associated with ribosomal chromatin, even in the absence of transcription.
Interaction partners:
- 13 kDa ribonucleoprotein-associated protein
- Ribosomal RNA-processing protein 7
- Periodic tryptophan protein 2
- Protein SOF1
- Ribosome biogenesis protein ENP2
- rRNA-processing protein FCF1
- U3 small nucleolar RNA-associated protein 16
- U3 small nucleolar RNA-associated protein 13
- U3 small nucleolar RNA-associated protein 18
- U3 small nucleolar RNA-associated protein MPP10
Sequence:
MTQSLGIEQYKLSVVSGGKPALNNLSSVTGNKNIARLSQDQRNYIIPFNNQIKVYSVETRQCVKTLKFANNSLLSGIFLQEEENNESIVKILLGDITVPQQEDAHLITVFTNNGHVIVLNYKGKLVESPKHFKISLADEKLANVFHSEGNYRILTTFKDPSQKAHNSLQSYRLYALTFDDAKKQFEVAHQAEWHNVILSNISSNGKLLAHMCKDVSTKDHEHKSISVVSLFDDSVNLSFPLGSILSSQTQSLSYNTRYVSSMAIDNMGQQLAVGFASGVISIVSLADLQIRLLKWHIDSVLSLSFSHDGSYLLSGGWEKVMSLWQLETNSQQFLPRLNGIIIDCQVLGPQGNYYSLILQMTENNSNSDYQFLLLNASDLTSKLSINGPLPVFNSTIKHIQQPISAMNTKNSNSITSLNHSKKKQSRKLIKSRRQDFTTNVEINPINKNLYFPHISAVQIFDFYKNEQVNYQYLTSGVNNSMGKVRFELNLQDPIITDLKFTKDGQWMITYEIEYPPNDLLSSKDLTHILKFWTKNDNETNWNLKTKVINPHGISVPITKILPSPRSVNNSQGCLTADNNGGLKFWSFDSHESNWCLKKISLPNFNHFSNSVSLAWSQDGSLIFHGFDDKLQILDFDTFKKFESLENTKTVSEFTLDSEIQTVKLINDTNLIVATRTTLNAINLLRGQVINSFDLYPFVNGVYKNGHMDRLITCDERTGNIALVINQQLTDLDGVPTINYKSRIIIFDSDLSTKLGNFTHHEYISWIGWNYDTDFIFLDIESTLGVVGTTVNTQLSDEVNNEGILDGLVSNTITTSASNSDIFAEQLHKLSSRGKKSDTRDKNTNDNDEDEEDIALEFINGEKKDKLVNMNSFTSMFDNIQNVQMDTFFDRVMKVLT
Protein: Diphosphoinositol polyphosphate phosphohydrolase DDP1 (EC 3.6.1.52) (Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase) (Ap6A hydrolase) (Diadenosine and diphosphoinositol polyphosphate phosphohydrolase 1) (Diadenosine hexaphosphate hydrolase (AMP-forming)) (EC 3.6.1.60) (Endopolyphosphatase) (EC 3.6.1.10) (Q99321)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May eliminate potentially toxic dinucleoside polyphosphates during sporulation. Most active against diadenosine 5',5'''-P1,P6-hexaphosphate (Ap6A). Can also hydrolyze diadenosine 5',5'''-P1,P5-pentaphosphate (Ap5A), adenosine 5'-pentaphosphate (p5A), and adenosine 5'-tetraphosphate (p4A) are also substrates, but not diadenosine 5',5'''-P1,P4-tetraphosphate (Ap4A) or other dinucleotides, mononucleotides, nucleotide sugars, or nucleotide alcohols. Also cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate) and [PP]2-InsP4 (bisdiphosphoinositol tetrakisphosphate). Also has endopolyphosphatase activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Polyphosphatase
- Inositol hexakisphosphate kinase 1
- Endopolyphosphatase
- mRNA-decapping enzyme subunit 1
Sequence:
MGKTADNHGPVRSETAREGRENQVYSPVTGARLVAGCICLTPDKKQVLMITSSAHKKRWIVPKGGVEKDEPNYETTAQRETWEEAGCIGKIVANLGTVEDMRPPKDWNKDIKQFENSRKDSEVAKHPPRTEFHFYELEIENLLDKFPECHKRHRKLYSYTEAKQNLIDAKRPELLEALNRSAIIKDDK
Protein: glucose-6-phosphate 1-epimerase (EC 5.1.3.15) (Q8IP67)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MATTAAAMAATSVVVLDRGNNTTCTINLHGATVVSWRVNNQEQLFVSKLASFDGKKAIRGGIPFVFPQFGAWSFGPQHGFARITRWHLERPPDRLHNGDVEAIFSLMDNDFTRSIWNYQFRITYRLILREKELHFHIGVYNPSKELSFTFNMLLHTYLKVPDVRRCQITGLQGCHFIDKTRENALYQEGREVVTVNEWTDRIYQHTPQEHVITNVVSGRKMRLHKYNFPDTVIWNPWIDRSREMSDFGDDEFPNMLCVEAGNVTSPVILLPGTAFEASQILQVEQPVLE
Protein: Vacuolar-sorting receptor 3 (AtVSR3) (BP80-like protein a') (AtBP80a') (Epidermal growth factor receptor-like protein 2a) (AtELP2a) (O80977)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Vacuolar-sorting receptor (VSR) involved in clathrin-coated vesicles sorting from Golgi apparatus to vacuoles.
Subcellular location: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Prevacuolar compartment membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Receptor homology region, transmembrane domain- and RING domain-containing protein 1
- Probable methyltransferase PMT12
- Probable methyltransferase PMT26
- Conserved oligomeric Golgi complex subunit 6
- Vesicle transport v-SNARE 11
- Protein RER1A
- Protein transport protein Sec61 subunit gamma-3
- Vacuolar protein sorting-associated protein 45 homolog
- RING-type E3 ubiquitin transferase
- Protein CANDIDATE G-PROTEIN COUPLED RECEPTOR 7
Sequence:
MKQLLCYLPWLLLLTLLVSPLNDARFVVEKNSLSVTSPESIKGTHDSAIGNFGIPQYGGSMAGTVVYPKENQKSCKEFSDFSISFKSQPGALPTFLLVDRGDCFFALKVWNAQKAGASAVLVADNVDEPLITMDTPEEDVSSAKYIENITIPSALVTKGFGEKLKKAISGGDMVNLNLDWREAVPHPDDRVEYELWTNSNDECGVKCDMLMEFVKDFKGAAQILEKGGFTQFRPHYITWYCPHAFTLSRQCKSQCINKGRYCAPDPEQDFSSGYDGKDVVVENLRQLCVYKVANETGKPWVWWDYVTDFQIRCPMKEKKYNKECADSVIKSLGIDSKKLDKCMGDPDADLDNPVLKEEQDAQVGKGSRGDVTILPTLVVNNRQYRGKLEKSAVLKALCSGFEETTEPAICLSTDVESNECLDNNGGCWQDKSANITACKDTFRGRVCECPTVDGVQFKGDGYSHCEPSGPGRCTINNGGCWHEERDGHAFSACVDKDSVKCECPPGFKGDGTKKCEDINECKEKKACQCPECSCKNTWGSYECSCSGDLLYIRDHDTCISKTGAQVRSAWAAVWLIMLSLGLAAAGAYLVYKYRLRQYMDSEIRAIMAQYMPLDSQPEIPNHVNDERA
Protein: C2H2-type domain-containing protein (Q57UR3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000256|ARBA:ARBA00004120}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000256|ARBA:ARBA00004114}.
Interaction partners:
Sequence:
MTALDFQFVQGSERLDWGVLVSIDIQRLIKDTNVDTLQRVVENIAFARLTRDEAAMFTPDHFIHLYTLCQLVIQYLVCSQECLAKINVKLNERMQESQQGVDSLKQECDRLNQENSVLRKEVKAQRRTLLAYEYNRAGRNATAGSTYICPQCGEMYGKCESLQSHIRKRHMMKPAVESPLVQVQPQQQPQTALEPPRQPEQWKTDYDLKMHQLQDKLSSIEQLLEKERDRNDRLQREGMMMMMQAALIGQKPASPVPPSAEGGKANVQAGQPISPQQQKLEQTKSEPTLPGLPTVQAAGVAALPHRNSQQSLFAVPVVPDVAALQQYNNTRQQEASNSALVKQVEELQKVVKSLKEGKQSESALPATSVSGNAAGPSASPSWLTVNEMQQGNAEKPAISALLSRAANVGSANTAKVGPDTNTSVPPLQTQPLRAVQELNPQCVAMTQQPLIQQQHPLDLQRETRTLPTATQQLPLQQPVALHPTASATIPLAPQQVPPATAQMVQQHPSDPHYQTHAFPTATQRTSLDQQQPITGLTTITAPPIESPKIQTAQQTSTHLATQQAPNPQHVPSTQQPLAPASIQQQHPLVEPNQIYAPSAVPQQLPFPGARPAVPQPLQPQPQPQPQLLPSAPQAATAPPVQQQQEVTKGEPQTVPAPHTSVAPPSLSQQPQPHTVTEVVHNTSHLTAGVVAPVDVMPITSAARPSKCIVSNCASSMASMGSLPQLFSTLKPPGQVQNSGKSSLLDDSLSVRPKPSTAAPGVDCQVVQHLVSSSKPSTAASSCTPEWLRNDSITDSGRNGATGRGYAPSGGTNFAIPKESNVVPTAPMESPPGLASTTGVAVSPPGTHPNAGLETSNSVIRAIPVPVQQHQPGPKVMVPPFAASLPVPVPTTSPPLSLGSGVAPMHVETGVAQVSADVKVANISVTDLSSGGSSV
Protein: Sodium/mannose cotransporter SLC5A10 (Sodium/glucose cotransporter 5) (Na(+)/glucose cotransporter 5) (Solute carrier family 5 member 10) (A0PJK1)
Organism: Homo sapiens (Human)
Function: Electrogenic Na+-coupled sugar symporter that actively transports D-mannose or D-fructose at the plasma membrane, with a Na+ to sugar coupling ratio of 1:1. Transporter activity is driven by a transmembrane Na+ electrochemical gradient set by the Na+/K+ pump. Exclusively recognizes sugar substrates having a pyranose ring with an axial hydroxyl group on carbon 2. Has likely evolved to enable renal reabsorption of D-mannose, an important constituent of oligosaccharide chains of glycoproteins. Contributes to dietary D-fructose reabsorption from glomerular filtrate across the brush border of the kidney.
Subcellular location: Apical cell membrane {ECO:0000250|UniProtKB:Q5SWY8}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MAANSTSDLHTPGTQLSVADIIVITVYFALNVAVGIWSSCRASRNTVNGYFLAGRDMTWWPIGASLFASSEGSGLFIGLAGSGAAGGLAVAGFEWNATYVLLALAWVFVPIYISSEIVTLPEYIQKRYGGQRIRMYLSVLSLLLSVFTKISLDLYAGALFVHICLGWNFYLSTILTLGITALYTIAGGLAAVIYTDALQTLIMVVGAVILTIKAFDQIGGYGQLEAAYAQAIPSRTIANTTCHLPRTDAMHMFRDPHTGDLPWTGMTFGLTIMATWYWCTDQVIVQRSLSARDLNHAKAGSILASYLKMLPMGLIIMPGMISRALFPDDVGCVVPSECLRACGAEVGCSNIAYPKLVMELMPIGLRGLMIAVMLAALMSSLTSIFNSSSTLFTMDIWRRLRPRSGERELLLVGRLVIVALIGVSVAWIPVLQDSNSGQLFIYMQSVTSSLAPPVTAVFVLGVFWRRANEQGAFWGLIAGLVVGATRLVLEFLNPAPPCGEPDTRPAVLGSIHYLHFAVALFALSGAVVVAGSLLTPPPQSVQIENLTWWTLAQDVPLGTKAGDGQTPQKHAFWARVCGFNAILLMCVNIFFYAYFA
Protein: Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (Immunoglobulin heavy chain-binding protein homolog) (BiP) (P36604)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Is required for secretory polypeptide translocation. May physically associate with SEC63 protein in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:P16474, ECO:0000255|PROSITE-ProRule:PRU10138}.
Interaction partners:
- Heat shock protein 70 homolog lhs1
- Hsp70 nucleotide exchange factor fes1
- Putative protein disulfide-isomerase C1F5.02
- Uncharacterized derlin-like protein C365.08c
- Ribosome-associated molecular chaperone sks2
- Calnexin homolog
- Sensor for unfolded proteins in the ER ire1
- DnaJ-related protein spj1
- Heat shock protein 60, mitochondrial
- UBA domain-containing protein 7
Sequence:
MKKFQLFSILSYFVALFLLPMAFASGDDNSTESYGTVIGIDLGTTYSCVAVMKNGRVEIIANDQGNRITPSYVAFTEDERLVGEAAKNQAPSNPENTIFDIKRLIGRKFDEKTMAKDIKSFPFHIVNDKNRPLVEVNVGGKKKKFTPEEISAMILSKMKQTAEAYLGKPVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVIRIVNEPTAAAIAYGLDKTDTEKHIVVYDLGGGTFDVSLLSIDNGVFEVLATSGDTHLGGEDFDNRVINYLARTYNRKNNVDVTKDLKAMGKLKREVEKAKRTLSSQKSVRIEIESFFNGQDFSETLSRAKFEEINMDLFKKTLKPVEQVLKDSNLKKSEIDDIVLVGGSTRIPKVQELLESFFGKKASKGINPDEAVAYGAAVQAGVLSGEEGSDNIVLLDVIPLTLGIETTGGVMTKLIGRNTPIPTRKSQIFSTAVDNQNTVLIQVYEGERTLTKDNNLLGKFDLRGIPPAPRGVPQIEVTFEVDANGVLTVSAVDKSGKGKPEKLVIKNDKGRLSEEDIERMVKEAEEFAEEDKILKERIEARNTLENYAYSLKGQFDDDEQLGGKVDPEDKQAVLDAVEDVAEWLEIHGEDASKEEFEDQRQKLDAVVHPITQKLYSEGAGDADEEDDDYFDDEADEL
Protein: 1-Acylglycerol-3-phosphate O-acyltransferase 3, isoform A (1-Acylglycerol-3-phosphate O-acyltransferase 3, isoform B (EC 2.3.-.-, EC 2.3.1.51)) (1-Acylglycerol-3-phosphate O-acyltransferase 3, isoform C) (RE10780p) (Q9VV51)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGSLEKLKQLRLIHLCIALTFFTSGLCINFIQLLMHVFIKPIDKRLFRKLMYYACYSLYSQLIFVSDWYAGSKMTVYMDKEDFEKHAGKEHVLLIMNHKYEIDWLNGWMICEKLGVLGNCKAYAKKAIRYVPIIGWGWWLAEFVFLNRNFDQDKTIITEQLKVVFSYPDPTWLLLNAEGTRFTPAKHEASVKFAQERGMTVLKHHLIPRTKGFTASLAPIRGLCPVIYDINLAYRPTDKTPATMLSLLHGKSVEPHLLMRRIPLEQVPEDEKEAAAWLQNLFVEKDKIIDSFLETGSFFKTSGIKEVPAYVNKRRLCSLVNFVCWAVFSLSCIFYYVITSLLAANWTAFITALSVLGLFYWLMGQAINKTQISKASNYGSSKSVAK
Protein: MAGUK p55 subfamily member 2 (Discs large homolog 2) (Protein MPP2) (Q9WV34)
Organism: Mus musculus (Mouse)
Function: Postsynaptic MAGUK scaffold protein that links CADM1 cell adhesion molecules to core components of the postsynaptic density (By similarity). In CA1 pyramidal neurons, required for synaptic KCNN2-containing channel function and long-term potentiation expression. Seems to negatively regulate SRC function in epithelial cells (By similarity).
Subcellular location: Cell projection, dendrite {ECO:0000269|PubMed:26880549}. Postsynaptic density {ECO:0000269|PubMed:26880549}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q14168}. Membrane {ECO:0000250|UniProtKB:Q14168}. Note=Prominently expressed in the postsynaptic densities of dendritic spines, is also detected in dendritic shafts. {ECO:0000269|PubMed:26880549}.
Interaction partners:
- Calcium/calmodulin-dependent protein kinase type II subunit alpha
- Glutamate receptor ionotropic, NMDA 2B
- Calcium/calmodulin-dependent protein kinase type II subunit beta
- Disks large homolog 4
- Protein lin-7 homolog C
- Calcium/calmodulin-dependent protein kinase type II subunit delta
- Disks large-associated protein 1
- Calcium/calmodulin-dependent protein kinase type II subunit gamma
Sequence:
MPVAATNSESAMQQVLDNLGSLPNATGAAELDLIFLRGIMESPIVRSLAKAHERLEETKLEAVRDNNLELVQEILRDLAELAEQSSTAAELARILQEPHFQSLLETHDSVASKTYETPPPSPGLDPTFSNQPVPPDAVRMVGIRKTAGEHLGVTFRVEGGELVIARILHGGMVAQQGLLHVGDIIKEVNGQPVGSDPRALQELLRSASGSVILKILPSYQEPHLPRQVFVKCHFDYDPARDSLSPCKEAGLRFNAGDLLQIVNQDDANWWQACHVEGGSAGLIPSQLLEEKRKAFVKRDLELTPTSGTLCGSLSGKKKKRMMYLTTKNAEFDRHELLIYEEVARMPPFRRKTLVLIGAQGVGRRSLKNKLILWDPDRYGTTVPYTSRRPKDSEREGQGYSFVSRGEMEADIRAGRYLEHGEYEGNLYGTRIDSIRGVVASGKVCVLDVNPQAVKVLRTAEFVPYVVFIEAPDYETLRAMNRAALESGVSTKQLTEADLRRTVEESSRIQRGYGHYFDLSLVNSNLERTFRELQTAMEKLRTEPQWVPVSWVY
Protein: Cystathionine gamma-synthase (CGS) (EC 2.5.1.48) (O-succinylhomoserine (thiol)-lyase) (P00935)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the formation of L-cystathionine from O-succinyl-L-homoserine (OSHS) and L-cysteine, via a gamma-replacement reaction. In the absence of thiol, catalyzes gamma-elimination to form 2-oxobutanoate, succinate and ammonia.
Subcellular location: Cytoplasm.
Interaction partners:
- Bifunctional aspartokinase/homoserine dehydrogenase 2
- 5,10-methylenetetrahydrofolate reductase
- Homoserine O-succinyltransferase
- HTH-type transcriptional regulator MetR
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
- Cysteine synthase A
- Methionine synthase
- Cystathionine beta-lyase MetC
- Met repressor
- Methionine aminotransferase
Sequence:
MTRKQATIAVRSGLNDDEQYGCVVPPIHLSSTYNFTGFNEPRAHDYSRRGNPTRDVVQRALAELEGGAGAVLTNTGMSAIHLVTTVFLKPGDLLVAPHDCYGGSYRLFDSLAKRGCYRVLFVDQGDEQALRAALAEKPKLVLVESPSNPLLRVVDIAKICHLAREVGAVSVVDNTFLSPALQNPLALGADLVLHSCTKYLNGHSDVVAGVVIAKDPDVVTELAWWANNIGVTGGAFDSYLLLRGLRTLVPRMELAQRNAQAIVKYLQTQPLVKKLYHPSLPENQGHEIAARQQKGFGAMLSFELDGDEQTLRRFLGGLSLFTLAESLGGVESLISHAATMTHAGMAPEARAAAGISETLLRISTGIEDGEDLIADLENGFRAANKG
Protein: Thioredoxin, mitochondrial (MTRX) (Mt-Trx) (Thioredoxin-2) (P97615)
Organism: Rattus norvegicus (Rat)
Function: Important for the control of mitochondrial reactive oxygen species homeostasis, apoptosis regulation and cell viability. Possesses a dithiol-reducing activity.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:9006939}.
Interaction partners:
- Thioredoxin-interacting protein
- Thioredoxin reductase 2, mitochondrial
- Thioredoxin-dependent peroxide reductase, mitochondrial
- Thioredoxin
- Peroxiredoxin-5, mitochondrial
- 3-mercaptopyruvate sulfurtransferase
- mitogen-activated protein kinase kinase kinase
- Mitochondrial peptide methionine sulfoxide reductase
- Thioredoxin reductase 1, cytoplasmic
- Glutathione reductase
Sequence:
MAQRLLLRRFLTSVISRKPPQGVWASLTSTSLQTPPYNAGGLTGTPSPARTFHTTRVCSTTFNVQDGPDFQDRVVNSETPVVVDFHAQWCGPCKILGPRLEKMVAKQHGKVVMAKVDIDDHTDLAIEYEVSAVPTVLAIKNGDVVDKFVGIKDEDQLEAFLKKLIG
Protein: Cyclin-L2 (Paneth cell-enhanced expression protein) (Q96S94)
Organism: Homo sapiens (Human)
Function: Involved in pre-mRNA splicing. May induce cell death, possibly by acting on the transcription and RNA processing of apoptosis-related factors.
Subcellular location: Nucleus speckle {ECO:0000269|PubMed:14684736, ECO:0000269|PubMed:18216018}. Nucleus, nucleoplasm {ECO:0000269|PubMed:18216018}.
Interaction partners:
- Cyclin-dependent kinase 4
- Cyclin-dependent kinase 6
- Cyclin-dependent kinase 2
- Cyclin-dependent kinase 1
- Cyclin-dependent kinase inhibitor 1
- Cyclin-dependent kinase inhibitor 1B
- Cyclin-dependent kinase 9
- Cyclin-dependent kinase inhibitor 2A
- Cyclin-A2
- Cyclin-A1
Sequence:
MAAAAAAAGAAGSAAPAAAAGAPGSGGAPSGSQGVLIGDRLYSGVLITLENCLLPDDKLRFTPSMSSGLDTDTETDLRVVGCELIQAAGILLRLPQVAMATGQVLFQRFFYTKSFVKHSMEHVSMACVHLASKIEEAPRRIRDVINVFHRLRQLRDKKKPVPLLLDQDYVNLKNQIIKAERRVLKELGFCVHVKHPHKIIVMYLQVLECERNQHLVQTSWNYMNDSLRTDVFVRFQPESIACACIYLAARTLEIPLPNRPHWFLLFGATEEEIQEICLKILQLYARKKVDLTHLEGEVEKRKHAIEEAKAQARGLLPGGTQVLDGTSGFSPAPKLVESPKEGKGSKPSPLSVKNTKRRLEGAKKAKADSPVNGLPKGRESRSRSRSREQSYSRSPSRSASPKRRKSDSGSTSGGSKSQSRSRSRSDSPPRQAPRSAPYKGSEIRGSRKSKDCKYPQKPHKSRSRSSSRSRSRSRERADNPGKYKKKSHYYRDQRRERSRSYERTGRRYERDHPGHSRHRR
Protein: Alpha/beta-Hydrolases superfamily protein (At4g25770) (Q147P6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MIASFSRFQISIPDLIPSSPRFLPPSQNQFRFRLYLQFPAQPKNLCQMEWMNRLGIGCFAANRSKRELTTEIDNGGEDFFDADVMESAEKPDHLVVMVNGIVGSAADWKYAAEQFVKKFPDKVLVHRSESNSATLTFDGVDKMGERLANEVLGVVKHRSGLKKISFVAHSLGGLVARYAIGKLYEQPGEVDSLDSPSKEKSARGGEIAGLEPMNFITFATPHLGSRGHRQFPILCGLPFLERTASQTAHLAAGRTGKHLFLVDNDDGNAPLLIRMATDSDDLKFISALNAFKRRVAYANVNFDSMVGWRTSSIRRPNELPKPNLLATDPNYPHIVYVERGNVDNGSCQSTSTVVTEQDTDLEEEMIHGLSQLSWERVDVSFHNSKQRYVAHSTIQVKTYWLHSDGKDVVFHMMDHFGL
Protein: Transcription termination factor 3, mitochondrial (Mitochondrial transcription termination factor 3) (mTerf3) (Q9VPD5)
Organism: Drosophila melanogaster (Fruit fly)
Function: Binds promoter DNA and regulates initiation of transcription (By similarity). Regulator of mitochondrial ribosome biogenesis and translation that is essential for development. Required for normal mitochondrial transcription and translation. Required for assembly of mitochondrial respiratory complexes and normal mitochondrial function. Maintains 16S rRNA levels and functions in mitochondrial ribosome assembly by regulating the biogenesis of the 39S ribosomal subunit.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:23300484}.
Interaction partners:
- DNA-directed RNA polymerase
- RE18748p
- RuvB-like helicase 1
- Transcription termination factor 5, mitochondrial
- Mitochondrial transcription factor A, isoform B
- FI01658p
- Transcription termination factor, mitochondrial
- Transmembrane GTPase Marf
- Protein ref
- Dimethyladenosine transferase 1, mitochondrial dimethyltransferase 1)
Sequence:
MFCSALRNILRNSQNAAKNATITSQIRNLRGQQSVHHEVEVLTSPGITTKQNDKKTEPAECEGSKEVALDFRNREAHVPSFNLAAYVNNSSTLQQFLSLGVDLHSIERRKGLGDFVLKLDFEKNVKPYITFLVDQGVSPDDFGRMFTKNPLLFKEDLDDLQTRVNYLKSKRFSDEARQRILTQNPYWLMFSTRRVDRRLGYFQKEFKLSGHDLRLLATREPNAITYNMEHLRKSVFTLKEEMGFNAKELSDLVVRKPRLLMIPPDDLVERFSYIHQDMGLPHAQIVQCPELLASREFRLRERHEFLKLLGRAQYDPQKDLYISPKTIVEGNNFYFVRNVAKSDLETFDLFLKTR