wanglab/gogpt-training-data huggingface dataset:
Protein: Group IIC secretory phospholipase A2 (GIIC sPLA2) (sPLA2-IIC) (EC 3.1.1.4) (14 kDa phospholipase A2) (PLA2-8) (Phosphatidylcholine 2-acylhydrolase 2C) (P39878)
Organism: Rattus norvegicus (Rat)
Function: PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Group XIIB secretory phospholipase A2-like protein
- Group XIIA secretory phospholipase A2
- Phospholipase A2, group III
- Cytochrome P450 2E1
- Phospholipase A2
- Group 10 secretory phospholipase A2
- Phospholipase A2, membrane associated
- Acyl-CoA 6-desaturase
- Phospholipase A2 group V
- Phospholipase A2
Sequence:
MKGIAVFLVFIFCWTTSTLSSFWQFQRMVKHITGRSAFFSYYGYGCYCGLGGRGIPVDATDRCCWAHDCCYHKLKEYGCQPILNAYQFAIVNGTVTCGCTMGGGCLCGQKACECDKLSVYCFKENLATYEKTFKQLFPTRPQCGRDKLHC
Protein: ADP-ribosylation factor-like protein 13B (ADP-ribosylation factor-like protein 2-like 1) (ARL2-like protein 1) (Protein scorpion) (Q8JHI3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Cilium-specific protein required to control the microtubule-based, ciliary axoneme structure. May act by maintaining the association between IFT subcomplexes A and B. Binds GTP but is not able to hydrolyze it; the GTPase activity remains unclear. Required to pattern the neural tube. Involved in cerebral cortex development: required for the initial formation of a polarized radial glial scaffold, the first step in the construction of the cerebral cortex, by regulating ciliary signaling. Regulates the migration and placement of postmitotic interneurons in the developing cerebral cortex Required during embryogenesis for cilia formation in multiple organs such as the pronephric duct.
Subcellular location: Cell projection, cilium membrane {ECO:0000269|PubMed:19906870}; Lipid-anchor {ECO:0000269|PubMed:19906870}. Note=Associates to the cilium membrane via palmitoylation. Localizes to proximal ciliary membranes, to an inversin-like subciliary membrane compartment, excluding the transition zone.
Interaction partners:
- Intraflagellar transport 88 homolog.
- Inositol polyphosphate-5-phosphatase E.
- Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta
- Abelson helper integration site 1.
- Coiled-coil and C2 domain-containing 2A.
- Meckelin isoform X1
- Centrosomal protein of 290 kDa
- Kinesin-like protein
- Protein fantom
- Transmembrane protein 216
Sequence:
MFNLMANCCNWLKRWREPARKVTLVMVGLDNAGKTATVRGIQGESPLDVAPTVGFSKVDLKQGKFEVTIFDLGGGKRIRGIWKNYYSESYGVVFVVDSSDVQRIQETRDTMAEVLRHPRIAGKPVLVLANKQDQDGAMAEADIIETLSLEKLVNENKCLCQIEPCSAVLGYGKKVDKSIKNGLNWLLNNIAKDYEAISERVQKDTAEQKAQEEQDKKERAERVRRIREERDRQEREEAEREGRTLKEEELDDVNMFNPFQPINNVLTENQDRLNREKEMQRQRENGQQGSVQEQIALQDEEEEEEDEESERQTPESTESGAVDQTKKKTRKLRLKRKHRVDPLRMEEAAPKSPTPPPLPVGWATPKVSRLPKLEPLGDTRHSDFYGKPLPPVAIRQRPNSDTHDVIS
Protein: Protein scylla (Protein regulated in development and DNA damage response 2) (REDD-2) (Q9VTH4)
Organism: Drosophila melanogaster (Fruit fly)
Function: Inhibits cell growth by regulating the Tor pathway upstream of the Tsc1-Tsc2 complex and downstream of Akt1. Acts as cell death activator during head development.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
Sequence:
MKMDVIAREQIIYGSLQGSNKNKDWTSRLPPPSAYTLDLMSKKAKTTTGGSSNGSNATATSTTTSTSSSIKHKQPAGSSNNNVGQSQSKKTKPSGSYNSNSNYYYYAADEEEGGSADYALSNYDKKAVEELSLRLLDELRAAKSRHLTCTEVSLPCDLTPSVAREIIRVSEKEPRGIRGCTIYIEFEDEPKNSRRIASIKVDSDTVSTFEVYLTLRQDHRGWTSLLPQFMKSLARTITISPEYTITKNKLYSADGLGARRSYSFGSHAHRPSAAIATPTN
Protein: UPF0613 protein PB24D3.06c (Q9C0Y8)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Zinc-type alcohol dehydrogenase-like protein PB24D3.08c
- WW domain-containing protein C2F3.14c
- Putative agmatinase 3
- Uncharacterized transcriptional regulatory protein PB24D3.01
- 3,4-dihydroxy-2-butanone 4-phosphate synthase
- Diaminohydroxyphosphoribosylamino-pyrimidine deaminase
- ATP-binding cassette transporter pdr1
Sequence:
MSASHPGILHEYTERLVAFELVGKSNVTLTSNVTRSLLLFVGGLGDGLLTVPYVQELVNPLDEIGWSIVQVQTQSSYIGWGTGSLKRDDEDLHKAVDYFLHIGGADFSTRKIVLMGHSTGSQNVLYYLTQSILPNYLIAGIAQAPVSDREAAYQFNGKEKTKELVDWVKAEYLDKGLGNDVLPRSKVENFFGEVPTSANRCIDLTDVRGNDDFFSSDLSADDFAKTFGNLKEISGSTAHSQLILLMSERDEFVSPSTDKAQLLNRFRESIRPTTSNSSLSGIIPGATHNVGPKSSPEALKWLINQLITALRSFIDQ
Protein: RNA editing complex protein MP67 (Q86MW2)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MRNSLIHHTRNLSATKQITGIVCDHVDVFTWGHSPPEQHGNKFSSGKATAPFYNAGQRRCTLCDDRLETSFSAHCGYVGHVARVGILERAMEILQKGEKRAANGKSGGLGGKITDLDESIKALVGTWWSRLNDTKREPALDYKRIPSLSASTTKKRLWRMRFLLQYLRDRGITRYSLTPAKVAGAGDNAFVRSARFERSEMIGDNIVKVVVPDRLVRLFPADEGGVTYKLASIQQLLDSNEGLLEIYDYLGLNNIIGVRLPNNKTKSDVVEALFGELQTFLWASELSCGSCQYPAFPTAEHRYVRALVDHLLNELTHMVIMWRVGSTLENSKEYLAKYLLQGARQNGSFSTSASGATIVKEVDCDRSRYAVLPLLLTFPYSTSSANKSAGGKQPPLQSSSLAAAKSVQERGTPRMLFTSPVAMPAALHSHYNPPLRIVRTIKDYQREILTVLEEEEVVSALIPCTDSSWGMKEGYMNSRETGRRKPPHGQIRAPWHELALEKYPRWRCDTEEAVVRQALELRLMQRKVYTKGTNWRALTTAMAQRLLPNSPLEVDPVGVRPVRQTGRLLLTFEGTTERRAALATSMCFPSLAQSAG
Protein: Acetyl-CoA decarbonylase/synthase complex subunit epsilon 2 (ACDS complex subunit epsilon 2) (ACDS complex carbon monoxide dehydrogenase subunit epsilon 2) (ACDS CODH subunit epsilon 2) (Q9C4Z3)
Organism: Methanosarcina thermophila
Function: Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase. The precise role of the epsilon subunit is unclear; it may have a stabilizing role within the alpha(2)epsilon(2) component and/or be involved in electron transfer to FAD during a potential FAD-mediated CO oxidation.
Interaction partners:
Sequence:
MVDTTKNTKLFTSYGVKTSKAITTEVAAKLISKAKRPLFVVGTGVLDPELLDRAVKIAKAKNIPIAATGSSMPGFVDKDVNAKYINLHQLGFYLTDPDWPGLDGNGNYDTIILLGHKKYYINQVLSAVKNFSDVKSISIDRNYIQNATMSFGNLSKADHIAALDEVIDLL
Protein: RpfF protein (Q7CLS3)
Organism: Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
Interaction partners:
- Sensory/regulatory protein RpfC
- Long-chain-fatty-acid--CoA ligase
- RpfH protein
- Response regulator
- 3-sulfinopropanoyl-CoA desulfinase
- Acyl-CoA dehydrogenase
- Isovaleryl-CoA dehydrogenase, mitochondrial
- Aconitate hydratase
- p-hydroxycinnamoyl CoA hydratase/lyase
- 3-methylmercaptopropionyl-CoA dehydrogenase
Sequence:
MSAVQPFIRTNIGSTLRIIEEPQRDVYWIHMHADLAINPGRACFSTRLVDDITGYQTNLGQRLNTAGVLAPHVVLASDSDVFNLGGDLALFCQLIREGDRARLLDYAQRCVRGVHAFHVGLGARAHSIALVQGNALGGGFEAALSCHTIIAEEGVMMGLPEVLFDLFPGMGAYSFMCQRISAHLAQKIMLEGNLYSAEQLLGMGLVDRVVPRGQGVAAVEQVIRESKRTPHAWAAMQQVREMTTAVPLEEMMRITEIWVDTAMQLGEKSLRTMDRLVRAQSRRSGLDAG
Protein: Lipoprotein lipase (LPL) (EC 3.1.1.34) (Q6P2U2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|RuleBase:RU362020}; Peripheral membrane protein {ECO:0000256|RuleBase:RU362020}; Extracellular side {ECO:0000256|RuleBase:RU362020}. Secreted {ECO:0000256|RuleBase:RU362020}. Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498, ECO:0000256|RuleBase:RU362020}. Note=Newly synthesized LPL binds to cell surface heparan proteoglycans and is then released by heparanase. Subsequently, it becomes attached to heparan proteoglycan on endothelial cells. Locates to the plasma membrane of microvilli of hepatocytes with triglyceride-rich lipoproteins (TRL). Some of the bound LPL is then internalized and located inside non-coated endocytic vesicles. {ECO:0000256|RuleBase:RU362020}.
Interaction partners:
Sequence:
MMFNKGRVSSAFLISWMYFVYISSGLETTIDPTAESITLSDIIGNATEWMMDFTDIESKFSFRTLEEPEDDLCYIVPGQPQSIKDCNFNTETKTFIVIHGWTVTGMFESWVPKLVTALYEREPSANVIVVDWLSRAQQHYPTSASYTKLVGKDVAKFVNWLQAEIDYPWEKLHLLGYSLGAHVAGIAGLLTKHKVNRITGMDPAGPTFEYADSLSTLSPDDANFVDVLHTNTRGSPDRSIGIQRPVGHIDIYPNGGTFQPGCDLQNTMLMVATTGLRNMDQIVKCSHERSIHLFIDSLVNQDHESMAFRCSSRDSFNKGMCLSCRKNRCNKVGYAVNKIRTRRSSKMYMKTREMMPYKVFHYQVKVHFFGKTQLSYTDQPMKISLYGIHGEKENIPYIMPTLNTNSTVSFLLTTDADIGELLMVKLLWEKDTLISWPWWNSDTFHIRKLRIKSGETQSKIIFSAKESEFSYLSRGGEAAVFVKDKEAQSSRKNQRLHKMKMHGSSFKQNNE
Protein: Protein pleiotropic regulatory locus 1 (Protein PRL1) (MOS4-associated complex protein 2) (MAC protein 2) (Q42384)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Pleiotropic regulator of glucose, stress and hormone responses. Also regulates cytochrome P450 CYP90A1/CPD. Coordinates the expression of hormone- and stress-related genes and genes related to cell wall modification and growth, leading to altered sugar-dependent growth and developmental responses. Component of the MAC complex that probably regulates defense responses through transcriptional control and thereby is essential for plant innate immunity. By suppressing the expression of several (1)O(2)-responsive genes, PRL1 seems to play a major role in modulating responses of plants to environmental changes by interconnecting (1)O(2)-mediated retrograde signaling with other signaling pathways. Acts as negative regulator of SNF1-related protein kinases AKIN10 and AKIN11 via the inhibition of their interaction with SKP1/ASK1. Component of the CUL4-RBX1-DDB1-PRL1 E3 ubiquitin-protein ligase complex, PRL1 may function as the substrate recognition module within this complex, leading to the AKIN10 degradation.
Subcellular location: Nucleus {ECO:0000269|PubMed:9765207}.
Interaction partners:
- Cell division cycle 5-like protein
- Pre-mRNA-splicing factor SPF27 homolog
- Pre-mRNA-processing-splicing factor 8A
- DExH-box ATP-dependent RNA helicase DExH12
- Pre-mRNA-processing factor 19 homolog 2
- Cwf15 / Cwc15 cell cycle control family protein
- Pre-mRNA-processing factor 19 homolog 1
- ARM repeat superfamily protein
- Zinc finger CCCH domain-containing protein 4
- Tetratricopeptide repeat
Sequence:
MPAPTTEIEPIEAQSLKKLSLKSLKRSLELFSPVHGQFPPPDPEAKQIRLSHKMKVAFGGVEPVVSQPPRQPDRINEQPGPSNALSLAAPEGSKSTQKGATESAIVVGPTLLRPILPKGLNYTGSSGKSTTIIPANVSSYQRNLSTAALMERIPSRWPRPEWHAPWKNYRVIQGHLGWVRSVAFDPSNEWFCTGSADRTIKIWDVATGVLKLTLTGHIEQVRGLAVSNRHTYMFSAGDDKQVKCWDLEQNKVIRSYHGHLSGVYCLALHPTLDVLLTGGRDSVCRVWDIRTKMQIFALSGHDNTVCSVFTRPTDPQVVTGSHDTTIKFWDLRYGKTMSTLTHHKKSVRAMTLHPKENAFASASADNTKKFSLPKGEFCHNMLSQQKTIINAMAVNEDGVMVTGGDNGSIWFWDWKSGHSFQQSETIVQPGSLESEAGIYAACYDNTGSRLVTCEADKTIKMWKEDENATPETHPINFKPPKEIRRF
Protein: Autophagy-related protein 3 (Autophagy-related E2-like conjugation enzyme ATG3) (AtAPG3) (Protein autophagy 3) (Q0WWQ1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: E2 conjugating enzyme responsible for the E2-like covalent binding of phosphatidylethanolamine to the C-terminal Gly of ATG8. This step is required for the membrane association of ATG8. The formation of the ATG8-phosphatidylethanolamine conjugate is essential for autophagy and for the cytoplasm to vacuole transport (Cvt).
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Autophagy-related protein 8a
- Autophagy-related protein 16
- Ubiquitin-like protein ATG12B
- Autophagy protein 5
- Ubiquitin-like modifier-activating enzyme atg7
- Ubiquitin-like protein ATG12A
- Beclin-1-like protein
- Autophagy-related protein 8f
- Autophagy-related protein 8e
- Autophagy-related protein 8i
Sequence:
MVLSQKLHEAFKGTVERITGPRTISAFKEKGVLSVSEFVLAGDNLVSKCPTWSWESGDASKRKPYLPSDKQFLITRNVPCLRRAASVAEDYEAAGGEVLVDDEDNDGWLATHGKPKDKGKEEDNLPSMDALDINEKNTIQSIPTYFGGEEDDDIPDMEEFDEADNVVENDPATLQSTYLVAHEPDDDNILRTRTYDLSITYDKYYQTPRVWLTGYDESRMLLQPELVMEDVSQDHARKTVTIEDHPHLPGKHASVHPCRHGAVMKKIIDVLMSRGVEPEVDKYLFLFLKFMASVIPTIEYDYTMDFDLGSSST
Protein: C-X-C chemokine receptor type 6 (CXC-R6) (CXCR-6) (CD antigen CD186) (Q9EQ16)
Organism: Mus musculus (Mouse)
Function: Receptor for the C-X-C chemokine CXCL16.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- C-X-C motif chemokine 16
- C-X-C motif chemokine 9
- C-C motif chemokine 20
- C-X-C motif chemokine 10
- C-C motif chemokine 5
- Stromal cell-derived factor 1
- Fractalkine
- C-X-C chemokine receptor type 3
- Guanine nucleotide-binding protein G
- C-C motif chemokine 3
Sequence:
MDDGHQESALYDGHYEGDFWLFNNSSDNSQENKRFLKFKEVFLPCVYLVVFVFGLLGNSLVLIIYIFYQKLRTLTDVFLLNLPLADLVFVCTLPFWAYAGTYEWVFGTVMCKTLRGMYTMNFYVSMLTLTCITVDRFIVVVQATKAFNRQAKWKIWGQVICLLIWVVSLLVSLPQIIYGHVQDIDKLICQYHSEEISTMVLVIQMTLGFFLPLLTMILCYSGIIKTLLHARNFQKHKSLKIIFLVVAVFLLTQTPFNLAMLIQSTSWEYYTITSFKYAIVVTEAIAYFRACLNPVLYAFVGLKFRKNVWKLMKDIGCLSHLGVSSQWKSSEDSSKTCSASHNVETTSMFQL
Protein: Annexin A2 (Annexin II) (Annexin-2) (Calpactin I heavy chain) (Calpactin-1 heavy chain) (Chromobindin-8) (Lipocortin II) (Placental anticoagulant protein IV) (PAP-IV) (Protein I) (p36) (Q07936)
Organism: Rattus norvegicus (Rat)
Function: Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity. May be involved in heat-stress response. Inhibits PCSK9-enhanced LDLR degradation, probably reduces PCSK9 protein levels via a translational mechanism but also competes with LDLR for binding with PCSK9.
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000269|PubMed:1618851}. Melanosome {ECO:0000250}. Note=In the lamina beneath the plasma membrane.
Interaction partners:
- Protein S100-A10
- Tissue-type plasminogen activator
- Plasminogen
- Protein S100-A4
- Uncharacterized protein.
- AHNAK nucleoprotein
- Annexin A1
- CD63 antigen
- Protein S100-A11
- Beta-2-glycoprotein 1
Sequence:
MSTVHEILCKLSLEGDHSTPPSAYGSVKPYTNFDAERDALNIETAIKTKGVDEVTIVNILTNRSNAQRQDIAFAYQRRTKKELPSAMKSALSGHLETVMLGLLKTPAQYDASELKASMKGLGTDEDSLIEIICSRTNQELQEINRVYKEMYKTDLEKDIISDTSGEFRKLLVALAKGKRAEDGSVIDYELIDQDARELYDAGVKRKGTDVPKWISIMTERSVCHLQKVFERYKSYSPYDMLESIRKEVKGDLENAFLNLVQCIQNKPLYFADRLYDSMKGKGTRDKVLIRIMVSRSEVDMLKIRSEFKRKYGKSLYYFIQQDTKGDYQKALLYLCGGDD
Protein: Filamin B (E7EN95)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MQEHSTRRRSLSLCPDWESWDPQKPVDNAREAMQQADDWLGVPQVITPEEIIHPDVDEHSVMTYLSQFPKAKLKPGAPLKPKLNPKKARAYGRGIEPTGNMVKQPAKFTVDTISAGQGDVMVFVEDPEGNKEEAQVTPDSDKNKTYSVEYLPKVTGLHKVTVLFAGQHISKSPFEVSVDKAQGDASKVTAKGPGLEAVGNIANKPTYFDIYTAGAGVGDIGVEVEDPQGKNTVELLVEDKGNQVYRCVYKPMQPGPHVVKIFFAGDTIPKSPFVVQVGEACNPNACRASGRGLQPKGVRIRETTDFKVDTKAAGSGELGVTMKGPKGLEELVKQKDFLDGVYAFEYYPSTPGRYSIAITWGGHHIPKSPFEVQVGPEAGMQKVRAWGPGLHGGIVGRSADFVVESIGSEVGSLGFAIEGPSQAKIEYNDQNDGSCDVKYWPKEPGEYAVHIMCDDEDIKDSPYMAFIHPATGGYNPDLVRAYGPGLEKSGCIVNNLAEFTVDPKDAGKAPLKIFAQDGEGQRIDIQMKNRMDGTYACSYTPVKAIKHTIAVVWGGVNIPHSPYRVNIGQGSHPQKVKVFGPGVERSGLKANEPTHFTVDCTEAGEGDVSVGIKCDARVLSEDEEDVDFDIIHNANDTFTVKYVPPAAGRYTIKVLFASQEIPASPFRVKVDPSHDASKVKAEGPGLSKAGVENGKPTHFTVYTKGAGKAPLNVQFNSPLPGDAVKDLDIIDNYDYSHTVKYTPTQQGNMQVLVTYGGDPIPKSPFTVGVAAPLDLSKIKLNGLENRVEVGKDQEFTVDTRGAGGQGKLDVTILSPSRKVVPCLVTPVTGRENSTAKFIPREEGLYAVDVTYDGHPVPGSPYTVEASLPPDPSKVKAHGPGLEGGLVGKPAEFTIDTKGAGTGGLGLTVEGPCEAKIECSDNGDGTCSVSYLPTKPGEYFVNILFEEVHIPGSPFKADIEMPFDPSKVVASGPGLEHGKVGEAGLLSVDCSEAGPGALGLEAVSDSGTKAEVSIQNNKDGTYAVTYVPLTAGMYTLTMKYGGELVPHFPARVKVEPAVDTSRIKVFGPGIEGKDVFREATTDFTVDSRPLTQVGGDHIKAHIANPSGASTECFVTDNADGTYQVEYTPFEKGLHVVEVTYDDVPIPNSPFKVAVTEGCQPSRVQAQGPGLKEAFTNKPNVFTVVTRGAGIGGLGITVEGPSESKINCRDNKDGSCSAEYIPFAPGDYDVNITYGGAHIPGSPFRVPVKDVVDPSKVKIAGPGLGSGVRARVLQSFTVDSSKAGLAPLEVRVLGPRGLVEPVNVVDNGDGTHTVTYTPSQEGPYMVSVKYADEEIPRSPFKVKVLPTYDASKVTASGPGLSSYGVPASLPVDFAIDARDAGEGLLAVQITDQEGKPKRAIVHDNKDGTYAVTYIPDKTGRYMIGVTYGGDDIPLSPYRIRATQTGDASKCLATGPGIASTVKTGEEVGFVVDAKTAGKGKVTCTVLTPDGTEAEADVIENEDGTYDIFYTAAKPGTYVIYVRFGGVDIPNSPFTVMVTEEAYVPVSDMNGLGFKPFDLVIPFAVRKGEITGEVHMPSGKTATPEIVDNKDGTVTVRYAPTEVGLHEMHIKYMGSHIPESPLQFYVNYPNSGSVSAYGPGLVYGVANKTATFTIVTEDAGEGGLDLAIEGPSKAEISCIDNKDGTCTVTYLPTLPGDYSILVKYNDKHIPGSPFTAKITDDSRRCSQVKLGSAADFLLDISETDLSSLTASIKAPSGRDEPCLLKRLPNNHIGISFIPREVGEHLVSIKKNGNHVANSPVSIMVVQSEIGDARRAKVYGRGLSEGRTFEMSDFIVDTRDAGYGGISLAVEGPSKVDIQTEDLEDGTCKVSYFPTVPGVYIVSTKFADEHVPGSPFTVKISGEGRVKESITRTSRAPSVATVGSICDLNLKIPEINSSDMSAHVTSPSGRVTEAEIVPMGKNSHCVRFVPQEMGVHTVSVKYRGQHVTGSPFQFTVGPLGEGGAHKVRAGGPGLERGEAGVPAEFSIWTREAGAGGLSIAVEGPSKAEITFDDHKNGSCGVSYIAQEPGNYEVSIKFNDEHIPESPYLVPVIAPSDDARRLTVMSLQESGLKVNQPASFAIRLNGAKGKIDAKVHSPSGAVEECHVSELEPDKYAVRFIPHENGVHTIDVKFNGSHVVGSPFKVRVGEPGQAGNPALVSAYGTGLEGGTTGIQSEFFINTTRAGPGTLSVTIEGPSKVKMDCQETPEGYKVMYTPMAPGNYLISVKYGGPNHIVGSPFKAKVTGQRLVSPGSANETSSILVESVTRSSTETCYSAIPKASSDASKVTSKGAGLSKAFVGQKSSFLVDCSKAGSNMLLIGVHGPTTPCEEVSMKHVGNQQYNVTYVVKERGDYVLAVKWGEEHIPGSPFHVTVP
Protein: Dihydroxyacetone phosphate acyltransferase (DAP-AT) (DHAP-AT) (EC 2.3.1.42) (Acyl-CoA:dihydroxyacetonephosphateacyltransferase) (Glycerone-phosphate O-acyltransferase) (P98192)
Organism: Mus musculus (Mouse)
Function: Dihydroxyacetonephosphate acyltransferase involved in plasmalogen biosynthesis.
Subcellular location: Peroxisome membrane {ECO:0000269|PubMed:10456321}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9ES71}; Matrix side {ECO:0000250|UniProtKB:Q9ES71}. Note=Exclusively localized to the lumenal side of the peroxisomal membrane. {ECO:0000250|UniProtKB:Q9ES71}.
Interaction partners:
- Alkyldihydroxyacetonephosphate synthase, peroxisomal
- Fatty acyl-CoA reductase 2
- Glycerol-3-phosphate dehydrogenase [NAD
- Glycerol-3-phosphate dehydrogenase, mitochondrial
- Glycerol-3-phosphate dehydrogenase 1-like protein
- Fatty acyl-CoA reductase 1
- 1-acyl-sn-glycerol-3-phosphate acyltransferase gamma
- 1-acyl-sn-glycerol-3-phosphate acyltransferase beta
- 1-acyl-sn-glycerol-3-phosphate acyltransferase alpha
- 1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon
Sequence:
MDVPSSSSSRFSVGSASPSSVLLYAKDLKKWDEFEDLLEERRHISDFKFAMKCYTPPLYRGITPCKPGDIKSIVLSSEEINYVIKQLSRESLTGVDVLREEASEILEEMSHKLRIGAIRFFAFVLSKIFKQIFSKVCVNEEGIQKLQRAVQEHPVVLLPSHRSYIDFLMLSFILYSYDLPVPVIAAGMDFLGMRVVSELLRMSGAFFMRRTFGGNKLYWAVFSEYVKTMLRCGYAPVEFFLEGTRSRAAKTLTPKFGLLNIVMEPFFKREVFDTYFVPISISYDKILEESLYAYEILGVPKPKESTTGLLKARRILSENFGSIHVYFGDPVSLRSLAAGRLNRNTYNLVPRCIPQKQPEDVQAFVTEVAYKMQLLQIENLALSPWLLVVTILLQNQLSMDFDALVEKTLWLKGVTQVFGGFLLWPDNKLPEEVVQSSILLHSNLASLVKDQVVLKMNSGSSQVVNGLVPEHIALLMCSAYRNQLLNIFARPSLVALALHMTPGLRKEDVFSCFSFLRNVFSDEFIFLPGNTLRDFEEGCYLLCKAEAMQMAGKDIILTDKGTAVLQFLTSLFKPFVESYQLLCRYLLHEEDYFGEKEYLVAARKFTRQLLDQGSSQCYDALSSELQKNALAAFVRLGVVEKKKVDSKYVYYVNGPATSKLEEMLGCKKPIGKPATAKL
Protein: Protein mab-21-like (Q9Y106)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- RH13166p
- Alpha-
Sequence:
MLVPPDMMAAQTRMVYQMNRFCTERVQARMYKTATAIREICKIVQDILKEVELQEPRFISSLVECNGRFEGVEVISPNEFEIVLYLNQMGVFNFVDDGTLPGCAVLKLSDGRKRSMSLWVEFITASGYLSSRKIRARFQTLVAQACDKSVYRDMVKMVGDTSEVKLRIRERFVVQITPAFKCSGIWPRSAAHWPVPHLPWPHPNIVAEVKTEGFDLLSKESVIMQNKNNNAASMEGDAWVLSFFEAENRLLQGGCRRRCLSMLKTLRDRHLDLPGNPISAYHLKNLLLYECEKHPRDFEWDEGCIADRINGIFLQLISCLQYRRCPHYFLPALDMFKGKSPSALEQAAKQVWRLTRELLTNANAFEKL
Protein: Elongation factor 1-alpha (Q3LUM1)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
- Elongation factor 1-gamma-like
- Elongation factor 1-gamma-like
- Elongation factor 1-gamma-like
- Elongation factor 1-beta 2-like isoform X1
- Elongation factor 1-delta-like
- Elongation factor 1-delta-like
- Elongation factor 1-beta 2-like
- Elongation factor 1-beta 2-like
- Ubiquitin extension protein
- 60S ribosomal protein L11
Sequence:
MGKEKVHINLVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKFETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVRQMICCCNKMDATTPKYSKARFDEIVKEVSSYLKKVGYNPEKIPFVPISGFEGDNMIERSTNLDWYKGPTLLEALDQITEPKRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFGPTGLTTEVKSVEMHHESLPEAFPGDNVGFNVKNVAVKDLKRGFVASNSKDDPAKEAANFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFSELLTKIDRRSGKELEKEPKFLKNGDAGMVKMIPTKPMVVETFSEYPPLGRFAVRDMRQTVAVGVIKSVEKKDPTGAKVTKSAAKKK
Protein: Oxidation resistance protein 1 (Q8MSQ5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
MQNVILTSQYYWSRRASQDVSSLSRSVDNLAIPVRRSKSRSVDHGLAAPFDLDSLRSKVEQRFESVDKLSRQKSSLPTIPTISYTVGNRDTLTSVAARFDTTPSELTHLNRLNSSFIYPGQQLLVPDKSAKDDASSSSTHDADGASLSGKSSPVERKLSGDESREKDILEGLRPGSPKPGHIERVGGSSQQQQAEEEANKSDDPVITQRFLKINVRHITDGQGVVGGVLLVTPNAVMFDPNVSDPLVIEHGPESYGVIAPMELVVNAAIFHDIAHMRVAGGAGQGLNSASGDAEKPEIYYPKPVLVEEDSKELPEQQSLLGEDGNKRLDAEIGSLEIADDQESLCSSTGRDGDAFPKAFDRERVEDSSMEAKDSAKTDALDDEDKKAGLGLSSTRSTLEERRKSLLDHHWAIPSKDRYCLSNSRRSSEDEGDNESNVTVDSGARVQDPHSANSSVSGVPLSQPPVAAAAAAAAVAPASAVVPLPPSGIDLEHLEQLSKQSCYDSGIDIREPVPNVQPIPKKTVYSDADIVLSSDWVPPKTIVPTHFSESPPRSTILGQSLDAGTGGAGGVRKKTSSVSFSVDDEAAQQAQAQSAALAVTDKQADKKNKMLKRLSYPLTWVEGLTGEGGAVPPGGVGSGSLNKSGDTDSAPNTGDSNQSVFSKVFSRRSSIGTFIRPHSSEGTSSSTKLKEAKQAPKLDYRSMVSMDDKPELFISVDKLIPRPARACLDPPLYLRLRMGKPIGKAIPLPTSVMSYGKNKLRAEYWFSVPKNRVDELYRFINTWVKHLYGELDEEQIKARGFELIQEDTEWTKSGTTKAGMGGGSQDGEEISDLTRESWEVLSMSTDEYRKTSLFATGSFDLDFPIPDLIGKTEILTEEHREKLCSHLPARAEGYSWSLIFSTSQHGFALNSLYRKMARLESPVLIVIEDTEHNVFGALTSCSLHVSDHFYGTGESLLYKFNPSFKVFHWTGENMYFIKGNMESLSIGAGDGRFGLWLDGDLNQGRSQQCSTYGNEPLAPQEDFVIKTLECWAFV
Protein: WRKY transcription factor WRKY24 (OsWRKY24) (Q6IEQ7)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Transcription activator. Interacts specifically with the W box (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis-acting element. Negative regulator of both gibberellic acid (GA) and abscisic acid (ABA) signaling in aleurone cells, probably by interfering with GAM1, via the specific repression of GA- and ABA-induced promoters.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00223, ECO:0000269|PubMed:19199048}.
Interaction partners:
- WRKY transcription factor WRKY24
- Os02g0539500 protein
- Os08g0102900 protein
- Os04g0417600 protein
- Os03g0267400 protein
- Os07g0162000 protein.
- Os07g0161700 protein
- Os07g0161900 protein
- WRKY transcription factor WRKY24
- Os11g0108932 protein
Sequence:
MTTSSSGSVETSANSRLGTFSFASASFTDLLGGNAGAGGGGVSRYKAMTPPSLPLSPPPVSPSSFFNSPIGMNQADFLGSPVLLTSSIFPSPTTGAFASQHFDWRPEVAAAQSADQGGKDEQRNSYSDFSFQTAPASEEAVRTTTFQPPVPPAPLGDEAYRSQQQQQPWGYQQQPAGMDAGANAASFGAAPFQATSSEMAPQVQGGGGYSQPQSQRRSSDDGYNWRKYGQKQVKGSENPRSYYKCTFPNCPTKKKVERSLDGQITEIVYKGTHNHAKPQNTRRNSGSSAAQVLQSGGDMSEHSFGGMSGTAATPENSSASFGDDEIRVGSPRAGNGGGDEFDDDEPDSKRWRKDGDGEGISMAGNRTVREPRVVVQTMSDIDILDDGYRWRKYGQKVVKGNPNPRSYYKCTTAGCPVRKHVERASHDLRAVITTYEGKHNHDVPAARGSAALYRPAPPAAAATSSHPYLPNQPPPMSYQPTGPQPYALRPDGFGGQGPFGGVVGGSSFGGFSGFDDARGSYMSQHQQQQRQNDAMHASRAKEEPGDDMFFQNSLY
Protein: GNBP-like 3 (A1ZBU5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Bomanin Bicipital 1
- Bomanin Short 1
- Bomanin Short 2
- Bomanin bicipital 2, isoform A
- Daisho1
- Bomanin Short 3
- Bomanin bicipital 3, isoform A
- Bomanin Tailed 2
- Bomanin Short 5
- Bomanin tailed 3, isoform A
Sequence:
MAQNSKLTIYLFLVAISVGSSLSYDVPKATVKVNSPKGFEVSIPDEPGISLFAFHGKVNEEMDDLSDQTWAADVVSSRNGRWTYRNRNHQLRPGDVLYYWTTARYHGVDYHNYNQRYVVGQGDSQRIDVNGSNGGRQPIVANGHNTFNIYVQ
Protein: NADH dehydrogenase (ubiquinone) complex I, assembly factor 6 (Putative phytoene synthase) (Q330K2)
Organism: Homo sapiens (Human)
Function: Involved in the assembly of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I) at early stages. May play a role in the biogenesis of complex I subunit MT-ND1.
Subcellular location: [Isoform 1]: Mitochondrion inner membrane. Note=Peripherally localized on the matrix face of the mitochondrial inner membrane.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. Nucleus.
Interaction partners:
- Arginine-hydroxylase NDUFAF5, mitochondrial
- Complex I intermediate-associated protein 30, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex assembly factor 4
- NADH dehydrogenase 1 alpha subcomplex assembly factor 2
- NADH dehydrogenase 1 alpha subcomplex assembly factor 3
- NADH dehydrogenase iron-sulfur protein 3, mitochondrial
- NADH-ubiquinone oxidoreductase chain 1
- FAD-dependent oxidoreductase domain-containing protein 1
- NADH dehydrogenase iron-sulfur protein 7, mitochondrial
- NADH dehydrogenase iron-sulfur protein 4, mitochondrial
Sequence:
MAASAHGSVWGPLRLGIPGLCCRRPPLGLYARMRRLPGPEVSGRSVAAASGPGAWGTDHYCLELLRKRDYEGYLCSLLLPAESRSSVFALRAFNVELAQVKDSVSEKTIGLMRMQFWKKTVEDIYCDNPPHQPVAIELWKAVKRHNLTKRWLMKIVDEREKNLDDKAYRNIKELENYAENTQSSLLYLTLEILGIKDLHADHAASHIGKAQGIVTCLRATPYHGSRRKVFLPMDICMLHGVSQEDFLRRNQDKNVRDVIYDIASQAHLHLKHARSFHKTVPVKAFPAFLQTVSLEDFLKKIQRVDFDIFHPSLQQKNTLLPLYLYIQSWRKTY