wanglab/gogpt-training-data huggingface dataset:
Protein: ET module (Q94246)
Organism: Caenorhabditis elegans
Interaction partners:
- Galectin
- Zinc finger protein GFI1 homolog pag-3
- C-type LECtin
- C-type LECtin
- CUB_2 domain-containing protein
Sequence:
MRLGIFLLALAGCCSFASAKQNCLVGNLIVSENVITSKSVELRECEGLCRKQTVKSPSGGLVLLTCEENKLMAFINKGQDCSSSELETSCFCEDELCNKVDLEENIPKPIEVINAPNNILCYVGFYANNTTPGFGSGDTVTCSAGNVCTSVSGVYNGYDAAAYACMPQGLCDGIFPNIDPNNPIACTNLAGTNIQGCCCYKQDCTSLAPMNNPPTPSPWNKNNQTCYQGISVNGALLYGGSFSQCLGECGSARIRTTYNGANVWGEIFVCDPVNVFTALNLDSGCMNLDTQNINGVPTALITGCACNSMDKCIDPTVVPPVYPVKQLRCAVGLYNGTTWLGAEMNCQGRCGRVRFNANGQQVSYFTCMPYDVCAGFGLASTEGQTYNPPQDEELEVYCCSASNNCNVNNPYILGRVNNSAVSTAKYPVLCYGGIWVNGVSITNSAYGLCQGECASASFTTTFANQVHNATIYTCDPVTMCQQAGISNSCGSVLGGVNACCCDNDLCIDPNRGSQRPQLRCYSGVSIPQDKYNTGGDQFCDGWCGSLNSVVNGKNATVYYCAPVGMCRYFGLGFGGSYGNCGQIPGADPQVTGCCCSETDNCLAPAGVNVTAIPARRDPRIVCYEGIHLNGQNISQPYYRMCDGECVSVSLGGTVNNNSHYATLYTCDPSSACAAMGLRNNCSTIDNSLTACCCDSNECIDPTYNRVPGKALKCYVGISTQHKGNIAGAEVLCDGYCATVSAVVGSDYVTAFHCAPRSMCRSLGLDNSNNTFYLDRFVNAYCCDVFDNCNVATSGFNVTIPPLAPNEMPRACYSGIFIGGSQISDGGWTACKGDCVAVNLNTTYNGVATTASLYTCDPSYICRMMNSTNRCHQQEQGFETCCCDSDACLDPTSTPPRKPYGDGNLCYVGAYSYDLKGNTIFNAGGEQYCEGNCASVTSTLANANVTVYACVPTYVCNSLYVYDSCRTLWYDRDITGCCCTNGPNCNLNQVVPRPPINNPGRRRPRVEYPITCPAGLIVDGFNQTPMEFSVCFGECASVSINATINGTLHTASFYTCDPSSVCYQLKVHNNCTSPEAGVTACCCDSDACLDPNRGKTVPTPPLKCYVGLYSTSVPSLQTGAEQLCDGKCASVNARIANDNVTLFACVPHSLCRSLELYDSCARMEPYYPEFRACCCDNADNCNVRQTHLANVINTTIPLTPLNDAPISCYSGLFINGTAYSSAGWQTCQGECVSVSITSQFNGQAGTAALYTCDPSRVCRNLKILNKCSTLENGITGCCCNTNACIDPTVYPARNPGNQLMCYAGISSNYIVNGSAVNVGAQIPCNGQCSSLSGVVGGFQVNTYHCMPNSICNSLELYDNCKPVWNDNQVTGCCCNNANNCNIANTTITPPPPPTSVDYAIACYTGLYVNGVPSTPVILGACQGQCASISLNTTLNGVATTATLYGCDPSTVCQSLNMNNWCASPIPGVSGCCCNTDLCLDPPKNKTVPSGFRKCFAGIYAQGKATGSEIFCPGKCASIQATLNQDPVAIFGCVPTQFCRQLEMYDECKPLPYDTTVTGCCCDNYNNCNVDLAGYGGKINTSMPVTNFRDYPIACFSGLYVNNMPISIAGWQACKGECASATLSTMYNGALTNATIYTCDPVSTCYQLGMNNNCTTIENGLSGCCCSTDACLDPTVSPPRTPNPLKCYVGLQSTYNSLSLGAETYCSGQCASLTGIVGGFNVTTYHCVADTICKSLEIKDTCRPLWSDREVTACCCNNADNCNLKDPNVKPGPAVLPDFPTACYQGLLVNNQTYGAPLTLQGCYGDCASITISTTIQNQNHTATLLTCDPTTVCQQLNMSNSCQTVEPGVSGCCCDTDGCLNPLTNTYPGPAKCYVGVYTSDGNVNVGGTVSCDGYCGSLETTVNNVLYKSYHCVPKTICKSLGLNNERKTISTDKDITGYCCTTGTNCNVKEAAVNTTNTIPVPTGIPMILCRSSIYLNNIALTADAYSVCAGSCASISYTGPYNGGSQTLTLYTCDPVTVCTSLNLANSCASIDGGLSGCCCSTNNCVGPNVLPSAGTTQPSTVSTLSPIVSTLSPIVSTLSPIVSTLSPIVSTLSPTVSTLSSNATSLTPSNPVLVSTATTQSPATTTKGSSSITFSILALFAAVYIALTRH
Protein: Myelin-associated glycoprotein (Siglec-4a) (P20916)
Organism: Homo sapiens (Human)
Function: Adhesion molecule that mediates interactions between myelinating cells and neurons by binding to neuronal sialic acid-containing gangliosides and to the glycoproteins RTN4R and RTN4RL2 (By similarity). Not required for initial myelination, but seems to play a role in the maintenance of normal axon myelination. Protects motoneurons against apoptosis, also after injury; protection against apoptosis is probably mediated via interaction with neuronal RTN4R and RTN4RL2. Required to prevent degeneration of myelinated axons in adults; this probably depends on binding to gangliosides on the axon cell membrane (By similarity). Negative regulator of neurite outgrowth; in dorsal root ganglion neurons the inhibition is mediated primarily via binding to neuronal RTN4R or RTN4RL2 and to a lesser degree via binding to neuronal gangliosides. In cerebellar granule cells the inhibition is mediated primarily via binding to neuronal gangliosides. In sensory neurons, inhibition of neurite extension depends only partially on RTN4R, RTN4RL2 and gangliosides. Inhibits axon longitudinal growth (By similarity). Inhibits axon outgrowth by binding to RTN4R (By similarity). Preferentially binds to alpha-2,3-linked sialic acid. Binds ganglioside Gt1b (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:26179919}; Single-pass type I membrane protein {ECO:0000269|PubMed:26179919}. Membrane raft {ECO:0000250|UniProtKB:P07722}.
Interaction partners:
- Reticulon-4 receptor
- Oligodendrocyte-myelin glycoprotein
- Myelin basic protein
- Reticulon-4
- Dynein light chain 1, cytoplasmic
- Leucine-rich repeat and immunoglobulin-like domain-containing nogo receptor-interacting protein 1
- Myelin-oligodendrocyte glycoprotein
- Reticulon-4 receptor-like 2
- E3 SUMO-protein ligase EGR2
- Transcription factor SOX-10
Sequence:
MIFLTALPLFWIMISASRGGHWGAWMPSSISAFEGTCVSIPCRFDFPDELRPAVVHGVWYFNSPYPKNYPPVVFKSRTQVVHESFQGRSRLLGDLGLRNCTLLLSNVSPELGGKYYFRGDLGGYNQYTFSEHSVLDIVNTPNIVVPPEVVAGTEVEVSCMVPDNCPELRPELSWLGHEGLGEPAVLGRLREDEGTWVQVSLLHFVPTREANGHRLGCQASFPNTTLQFEGYASMDVKYPPVIVEMNSSVEAIEGSHVSLLCGADSNPPPLLTWMRDGTVLREAVAESLLLELEEVTPAEDGVYACLAENAYGQDNRTVGLSVMYAPWKPTVNGTMVAVEGETVSILCSTQSNPDPILTIFKEKQILSTVIYESELQLELPAVSPEDDGEYWCVAENQYGQRATAFNLSVEFAPVLLLESHCAAARDTVQCLCVVKSNPEPSVAFELPSRNVTVNESEREFVYSERSGLVLTSILTLRGQAQAPPRVICTARNLYGAKSLELPFQGAHRLMWAKIGPVGAVVAFAILIAIVCYITQTRRKKNVTESPSFSAGDNPPVLFSSDFRISGAPEKYESERRLGSERRLLGLRGEPPELDLSYSHSDLGKRPTKDSYTLTEELAEYAEIRVK
Protein: Alpha-(1,3)-fucosyltransferase fut-1 (EC 2.4.1.214) (Fucosyltransferase fut-1) (G5EDR5)
Organism: Caenorhabditis elegans
Function: Preferentially catalyzes the addition of fucose in alpha 1-3 linkage to the first GlcNAc residue (with or without alpha 1,6-linked fucose), next to the peptide chains in N-glycans. Unlike in mammals, does not require the prior action of N-acetylglucosaminyltransferase I to generate complex N-glycans.
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000255|RuleBase:RU003832}; Single-pass type II membrane protein {ECO:0000255|RuleBase:RU003832}.
Interaction partners:
- beta-N-acetylhexosaminidase
- beta-N-acetylhexosaminidase
- beta-N-acetylhexosaminidase
- beta-N-acetylhexosaminidase
- Alpha-
- Beta-1,4-galactosyltransferase galt-1
- GDP-mannose 4,6 dehydratase 1
- Exostosin-like-3 homolog
- GDP-L-fucose synthase
- Alpha-galactosidase
Sequence:
MTARSIKLFFARWKYLMFACCITYLLVIYAPISKSEQKDWKEGEIELSNDHELDVPILQKEELKPQQRPSFEENVPKKKTFNFNPVGKEPFDVEEVLTSSDIKLEERMTATVIPGQKRLILSWNAGHSQDNLQGCPDWNCEFTQVRARAPDADAVLIAHMDNDFVPKPNQYVVYFSQESPANSGIQIPRPDYINMTLGFRHDTPAGSPYGYTVKLGAKSRKTGQVVDANLVNGKAKGAAWFVSHCQTNSKREDFVKKLQKHLQIDIYGGCGPMKCARGDSKCDTMLDTDYHFYVTFENSICEDYVTEKLWKSGYQNTIIPLVLKRKLVEPFVPPNSFIAIDDFKSVKEMGDYLNYLMNNKTAYMEYFEWRHDYKVVFLDGSHHDVLERPWGFCQVCRMAWTEPRQKVLIPNWDAYWRQTCEKDGTLVDSIPLD
Protein: AIDA-associated heptosyltransferase (Autotransporter strand-loop-strand O-heptosyltransferase) (Glycosyltransferase (EC 2.4.-.-)) (F8SKF2)
Organism: Escherichia coli
Interaction partners:
Sequence:
MTFLSPPEVPTIKAENGTYYDFNNGARILFPKGEWHVNIIDEDSGNILFSCDTQAGWVTSTKKYYVKFRIQAFKKGEKKPFLDTVMELKDNPVLISFPTGTLGDIIAWFHYAEKFRIKHQCKLECSVSEEFITLLSDNYPDIKFTSAQDKYEGKPYATYRIGLFFNGDTDNQPVDFRLVGFHRNAGYILGVSPQEDPPRLNLSAERKIQEPYVCIAVQSTAQAKHWNNGLGWAEVVRYLKELGYRVLCIDRNAHAGNGFVWNHIPWGAEDFTGALPLQERVDLLRHASFFVGLASGLSWLAWACRIPVVLISGFSRPDSEFYTPWRVFNSHGCNGCWDNTNYNFDHTDFLWCPVHKGTDRQFECTRLITGKQVCGVIRTLHSYLTNHDRII
Protein: Ribosome maturation protein SBDS (Protein 22A3) (Shwachman-Bodian-Diamond syndrome protein homolog) (P70122)
Organism: Mus musculus (Mouse)
Function: Required for the assembly of mature ribosomes and ribosome biogenesis. Together with EFL1, triggers the GTP-dependent release of EIF6 from 60S pre-ribosomes in the cytoplasm, thereby activating ribosomes for translation competence by allowing 80S ribosome assembly and facilitating EIF6 recycling to the nucleus, where it is required for 60S rRNA processing and nuclear export. Required for normal levels of protein synthesis. May play a role in cellular stress resistance. May play a role in cellular response to DNA damage. May play a role in cell proliferation (By similarity).
Subcellular location: Cytoplasm. Nucleus, nucleolus {ECO:0000250}. Nucleus, nucleoplasm. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Detected in the cytoplasm, but not in the nucleus (PubMed:21536732). Primarily detected in the cytoplasm, and at low levels in nucleus (PubMed:19602484). Detected in the nucleolus during G1 and G2 phase of the cell cycle, and diffusely distributed in the nucleus during S phase. Detected at the mitotic spindle. Colocalizes with the microtubule organizing center during interphase (By similarity). {ECO:0000250, ECO:0000269|PubMed:19602484, ECO:0000269|PubMed:21536732}.
Interaction partners:
- Elongation factor-like GTPase 1
- Large ribosomal subunit protein eL43
- Large ribosomal subunit protein uL5
- Eukaryotic translation initiation factor 6
- Small ribosomal subunit protein eS19
- Large ribosomal subunit protein uL18
- mRNA turnover protein 4 homolog
- Elongation factor 2
- 60S ribosome subunit biogenesis protein NIP7 homolog
- Small ribosomal subunit protein eS24
Sequence:
MSIFTPTNQIRLTNVAVVRMKRGGKRFEIACYKNKVVGWRSGVEKDLDEVLQTHSVFVNVSKGQVAKKEDLISAFGTDDQTEICKQILTKGEVQVSDKERHTQLEQMFRDIATIVADKCVNPETKRPYTVILIERAMKDIHYSVKPNKSTKQQALEVIKQLKEKMKIERAHMRLRFILPVNEGKKLKEKLKPLMKVVESEDYSQQLEIVCLIDPGCFREIDELIKKETKGRGSLEVLSLKDVEEGDEKFE
Protein: Proteasome component Pre6, putative (AFU_orthologue AFUA_5G02150) (C8V668)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Proteasome subunit beta
- Proteasome subunit alpha type
- 26S proteasome regulatory subunit S5A
- proteasome endopeptidase complex
- Proteasome subunit alpha type
- Proteasome subunit alpha type
- Proteasome component Pup3, putative
- proteasome endopeptidase complex
- Proteasome subunit alpha type
- Proteasome subunit beta
Sequence:
MEAVKRGTCAVGVKGKDVVVLGCEKRSALKLQDTRITPSKIAVLDNHAILAFAGLNADARILIDKARLEAQSHRLTVEDPVSIEYITKYIATVQQRYTQSGGVRPFGISTLVVGFDPNDKTPRLYQTEPSGIYSAWKANAIGRSSKTVREFLERNHQDDMDREQTIQLTIKSLLEVVQTGAKNIEVAIMSPGKTIEMLPDDQIESYVKSIETEKQEEAAKKKTRAGTTTAAILTRSGGGESSEARE
Protein: Cytochrome b561 / ferric reductase transmembrane domain-containing protein (Q54WU1)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Large ribosomal subunit protein uL23m
- Large ribosomal subunit protein mL46
- Large ribosomal subunit protein uL3m
Sequence:
MIKSIVFLSTILFLTFLIGVNGQFQNSVILDQNSNYNLQWIIFNETITIQVSINKKAWIGLGWHCQGCQKDGPMENADYSIATFDENGQGYVWDCYQENDPTSQPQNDTVFKGAEDNIISFSGYQTDQYSIMMFTKKLSTGDTVGDHILVNGPVDFVWAHGQDNSFGFHGVGNAGRTTVNLATGSTNSGPDYVNWHASLMLVAFGLLMPFSIFSARFLKVFHWWWPLHYVFNGLASVCALIGFIIAIVMLDGLDFSTLHSIFGIITLCLVLVSILFGALSHFLWKPTRVGTPIFPDMFHWFVGRCTFALSIAAIITGMVLHQVPTAVIIVFSGVIALYFGVIIFIEIYKKVYPNHVDFSHGGATGYTQGINHN
Protein: Opacity protein opA50 (V0) (opA30) (P11296)
Organism: Neisseria gonorrhoeae
Function: Implicated in a number of adherence functions. OPA proteins are implicated in pathogenesis and are subject to phase variation.
Subcellular location: Cell outer membrane.
Interaction partners:
Sequence:
ASEDGGRGPYVQADLAYAYEHITHDYPKPTDPSKGKISTVSDYFRNIRTHSIHPRVSVGYDFGGWRIAADYARYRKWSDNKYSVSIKNMRVHKHNSNRKNLKTENQENGSFHAVSSLGLSAIYDFQINDKFKPYIGARVAYGHVRHSIDSTKKITGLLTTSTPGIMSGVYKVLRTPGAHRESDSIRRVGLGVIAGVGFDITPKLTLDAGYRYHNWGRLENTRFKTHEASLGVRYRF
Protein: Mitogen-activated protein kinase kinase kinase 1a (PpMEKK1a) (EC 2.7.11.25) (MAP kinase kinase kinase 1a) (A9SY39)
Organism: Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens)
Function: The CERK1, MEKK1a/b, MKK1a/b/c and MPK4a/b proteins are involved in pathogen defense. The pathway induces rapid growth inhibition, cell wall depositions and accumulation of defense-related transcripts. This protein is required for responses to chitin and acts redundantly with MEKK1b.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q39008}.
Interaction partners:
Sequence:
MIEERGSSRGSREDRGSSRGSSRGSFEDKGSSHDWKGMGGSTPRPRLTRLVAKKDRNYDAKVDSDFDDDSSVHSTSSPRLSPASSDNLSKITIGQQSFRVGGDVDNLKALYEALGATSPAALGIEASDWESRRKSAVYSRPTSPPRVSHDTGQSSYSHDFQFPASRVDSSLESPPLSPRGLAPMSPVRPIEVEWRKHRNNYAKPTISNRPGRENNPLKPSQPPPTMFPQSSGLRTPDPLPPIDTSTSRLGRESLELQNRHTTLGAYSPPGLRKVHSELTGLVSARSDGAGWASDIESAKRNEDLAVASPVFRDNLPSAAVAMPNGSLVRASFTPRDSNRMNSVRSNSHGLRWNSCHAQEAEAIAKTALEETSNGLRIEDPERIRDLEKPSPLIIEKVDEPLSEVSSSVSTESSPSVIPKRPPWDTWAKGEFLGSGTFGSVYEGVARNGTFFAVKEVNLADEGKLGRQAVKQLEREIALLSDIQHPNIVQYLGTERTEDKLYIFLELLNKGSLANLYRKYGLFYEQIKAYTEQILTGLKYLHDRKIIHRDIKCANILVDTNGVVKLADFGMAKQVEKFGFAKSFVGSAHWMAPEVVDPKQQYNFAADIWSLGCTVLEMATEGPPFGELEFIAVFWKIGRGEAPLIPDDLEDELKDFIAQCLQVDASKRPTCDMLLAHPFITGEEMTGPVTQMGTPGLSTISEERSVDMSVTSSIAVSSNSGTSPRVIENLVNHLSIERRPKSMRTLRSELSMSSAESIAS
Protein: LIM/homeobox protein lim-4 (G5EEA1)
Organism: Caenorhabditis elegans
Function: Transcription factor that binds to the promoter of target genes. Regulates genes involved in serotonin synthesis and release in serotonergic ADF neurons. Involved in specification of neuron cell fate, olfactory receptor expression, locomotion, and foraging behavior. Required in AWB olfactory neurons to repress AWC cell fate and promote the AWB cell fate during early development. Cooperates with additional factors to direct the differentiation of the olfactory neurons, functioning with the transcription factor sox-2 to suppress AWC terminal differentiation and promote AWB neuron differentiation. Involved in regulating terminal specification and maintenance of the SMB sensory/inter/motor neurons. Plays a role in regulation of RID motor neuron differentiation, but is dispensable for motor axon outgrowth in the dorsal nerve cord. May regulate its own expression.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|RuleBase:RU000682}.
Interaction partners:
- Nuclear hormone receptor family member odr-7
- Homeobox protein ceh-36
- TBC1 domain family member 13
- LIM interaction domain-containing protein
Sequence:
MDAHLVQAKKTSTASELSDSSLTFPFIGDYLSSPSLTTSDYVSDCSNLTVEGPVPANQEFSSSDESSVYISSALRLADYAFTPDDNIRIKPDAVIVICTQCQHQIQDKFFLSIDGRNYHENCLQCSTCENPLSNKCFYKDKTFYCKGCYFRTHVTSTASSCRELGPKCASCDRTIQATDWVRRARNYVYHLACFSCNQCKRQLSTGEEYALQEGNLLCKQHFLELVEGDSGVSSQKAKTKRVRTTFAEDQLSVLQTYFNRDSNPDGADLEKIASMTGLSKRVTQVWFQNSRARQKKWHQKSEGDNGDSQRSSVGPSSPSQKSDSSSEMMYPTSVTTSVEDAIPDSIVILGSLQFD
Protein: Uncharacterized protein C29B12.12 (O14033)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MQTPTARSSTNVYGKLVDNETRCFHYHSKADVVALRCGQCEKFYACFQCHDELNTHPFLPWRKAKFHIPCVICGACKNSLTVEEYRSTVHCKYCNHPFNPKCKNHAGYYFEDA
Protein: Uncharacterized protein (Q57XL2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Ribosomal protein S9
- Uncharacterized protein
- Pentacotripeptide-repeat region of PRORP domain-containing protein
- Uncharacterized protein
- Opioid growth factor receptor
- LysM domain-containing protein
- Uncharacterized protein
- Uncharacterized protein
- Small ribosomal subunit protein mS41
- Enoyl-CoA hydratase/isomerase domain-containing protein
Sequence:
MEVYRRITERVRGALWAHHGRLMSERQFHRILAFVYNNKYEYQIRFDRMEVVGREWGGRVEVVTTPAGYLKRVRVNPCVEDLTLYQQQQLILSAYASACADGRKLMEQAEMNIYKQFLKDLKPIVMGIRDNPEFYTVPENSIETIGGVLQTGDSNNLCHTHRTIPAAKARQPTDEVRARQEWEQKWINSPRGQSWALTLRGKTYFTLHGPQYRPRGAPGAKKETLPLDIPAPYTAMDEKRLLKKNWMAYLDNKHVAEVMWTRVKIADREKRQRLLQETGRAWHRPINEEAINRW
Protein: Stearoyl-[acyl-carrier-protein] 9-desaturase, chloroplastic (Stearoyl-ACP desaturase) (EC 1.14.19.2) (Acyl-[acyl-carrier-protein] desaturase) (Delta(9) stearoyl-acyl carrier protein desaturase) (P22337)
Organism: Ricinus communis (Castor bean)
Function: Converts stearoyl-ACP to oleoyl-ACP by introduction of a cis double bond between carbons 9 and 10 of the acyl chain.
Subcellular location: Plastid, chloroplast. Plastid. Note=In green tissue, found in chloroplasts. In non-photosynthetic tissue, found in plastids.
Interaction partners:
Sequence:
MALKLNPFLSQTQKLPSFALPPMASTRSPKFYMASTLKSGSKEVENLKKPFMPPREVHVQVTHSMPPQKIEIFKSLDNWAEENILVHLKPVEKCWQPQDFLPDPASDGFDEQVRELRERAKEIPDDYFVVLVGDMITEEALPTYQTMLNTLDGVRDETGASPTSWAIWTRAWTAEENRHGDLLNKYLYLSGRVDMRQIEKTIQYLIGSGMDPRTENSPYLGFIYTSFQERATFISHGNTARQAKEHGDIKLAQICGTIAADEKRHETAYTKIVEKLFEIDPDGTVLAFADMMRKKISMPAHLMYDGRDDNLFDHFSAVAQRLGVYTAKDYADILEFLVGRWKVDKLTGLSAEGQKAQDYVCRLPPRIRRLEERAQGRAKEAPTMPFSWIFDRQVKL
Protein: Cell death protein hid (Protein head involution defective) (Protein wrinkled) (Q24106)
Organism: Drosophila melanogaster (Fruit fly)
Function: Activator of apoptosis, with grim and rpr, that acts on the effector Dredd. Seems to act genetically upstream of baculoviral anti-apoptotic p35. Blocks Diap2 from binding and inactivating the effector caspase Drice. Might regulate apoptosis downstream of Clbn/NEMF.
Interaction partners:
- Death-associated inhibitor of apoptosis 1
- Mitogen-activated protein kinase ERK-A
- Caspase Dronc
- Caspase drICE
Sequence:
MAVPFYLPEGGADDVASSSSGASGNSSPHNHPLPSSASSSVSSSGVSSASASSASSSSSASSDGASSAASQSPNTTTSSATQTPMQSPLPTDQVLYALYEWVRMYQSQQSAPQIFQYPPPSPSCNFTGGDVFFPHGHPNPNSNPHPRTPRTSVSFSSGEEYNFFRQQQPQPHPSYPAPSTPQPMPPQSAPPMHCSHSYPQQSAHMMPHHSAPFGMGGTYYAGYTPPPTPNTASAGTSSSSAAFGWHGHPHSPFTSTSTPLSAPVAPKMRLQRSQSDAARRKRLTSTGEDEREYQSDHEATWDEFGDRYDNFTAGRERLQEFNGRIPPRKKKSSNSHSSSSNNPVCHTDSQPGGTSQAESGAIHGHISQQRQVERERQKAKAEKKKPQSFTWPTVVTVFVLAMGCGFFAAR
Protein: Type 3 secretion system chaperone PscG (Pseudomonas secretion protein G) (Type III export protein PscG) (P95435)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Chaperone of the type III secretion (T3S) injectisome that translocates effector toxins into host cells, facilitating the establishment and dissemination of infection. Prevents premature polymerization of PscF, along with PscE, within the cytoplasm. Required for type III secretion needle assembly. Also required for cytotoxicity by influencing PscF levels.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16115870}.
Interaction partners:
- Type 3 secretion system needle filament protein
- Type 3 secretion system chaperone PscE
- Lipoprotein
- Type 3 secretion system stator protein
- Type 3 secretion system secretin
- Type III export protein PscH
- Type III inner-rod protein PscI
- Type III export apparatus protein
- Regulatory protein PcrH
- Type III export protein PscK
Sequence:
MDTSLIRELAELALAGSGQHCHEEALCIAEWLERLGQDEAARLIRISSLANQGRYQEALAFAHGNPWPALEPWFALCEWHLGLGAALDRRLAGLGGSSDPALADFAAGMRAQVRT
Protein: RE34149p (Zydeco, isoform E) (Q8SXS9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MEDYWGLSSTTDINCTQPAIDDFPRDLFSEAQRQSGAVVLHVIASLYLFVALAVVCDEYFVPAVEKICAALNMSNDVAGATFMAAATSAPELFVNVIGTFITEGDIGVGTIVGSAVFNILAVAACCGIGAGMTIPLDWWPLTRDSIAYGVTVAILICVMHDERVEWYEALILVSLYAVYLAVMYFDKTFQKCAKGGVKQARSRSRSSNCSIHTKNSNEKEPELVENRICQNMANIQLNGGLNKEQAKATSTSGAGTTAISITTSTMTTTLSTTHSAGGGGGAVGLCSGPGAIVQMAPLDDAEAESHVAVAAADEGRKEEGYSLLSYPKDKSCFAQFTWLIIWPIHLLFRIAIPDCKKAKNNKIFPLTFIMCIVWIGSLSYVVAWMITIIGDTLKIPDSVMGITFLAAGTSVPEAVSSVIVAKRGHGSMGICNSIGSNTFDILLCLGVPWLIKAVFFPIQPGQNYVAINSAGLEYSAITLLSTLFLLYLTFSTNKFKLDKKVGTACLVMYLVFMVFASLIELNVFFRVNLPTCGRS
Protein: Phosphatidic acid phospholipase A1, isoform D (EC 3.1.1.-, EC 3.1.1.32) (X2JDJ3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSERSKGDVSARVNNNANQTRVVKNPLLSASVTGLSFDDFPNKPQLLPAAPPVVHATPPAAPVLIAGILNREPKSLVTVGQPSSIDDSEALDEINLNTSSEDSVGAGGSSPYLGAGDQNANPLLEPPTEAGNDSLLSQAASSFTALPAVASNVFSTFSKRIYAGSRETSEEPKLDIQPSYIQQASYVQPVAPVPAPFYAAPPAAANEVVAPEPPKFYAPTEVPPPNVGVPAPPPTSGNPNTYRFTARKKLYAPIPGLSEQSGQPAQQPQVPQAPQAAPSFQTPPYPPQLTYAANPAPFDISAQPAAIPAEERKSGGGLFSLTSLVPTGVLQNITGIVQSATGRSSEPEHTNVQQAGGYLDITTASAPAPSTNLFGGPNSTFPPGGNYFVPGAPPSLPSTGVVGPPSVGNFFAPAAPLPVAQTAAPPAVGAFFTSAAPSVTPSVFTPGTVPPLAPQPFQSATVNQSALPPNNPPTASAVGELFVPAPTTIAQGTSPAVPFVDTQAVPTIPLTVPPGNPPPTSTLGGFFTTGEVAPVVAPFGTQASPATQSAGFFNPGEVRPNVPLAEPVPTIPITSSGVPPIGLFPPAPAQPGVQTASNPNPLPGAAAPPPAAGQASYRLQKGTRLYKSPLTPQETATSSGFAAPLPPTSVTPAIFNPFGAPAPGSFNSVGHLEGQSSQGVPFFTPPVQNPPGQVAAPTVAVPQSAPIAPPPGTSSTSVAPPLTASIANPPPTSGFASVPLFAAPTISSTPIPFFNPQPTGAEVTTGLSQQENEATASTTLEGLVQGPAPTLSASQFFDTPLPTGTQPENQVASVSSERENLVQEPISNQGIPFFAPPQTNIFTPQLQQEFIAPAEDSKRSEIQEEFLSAPPQESNLSTELREDTHTGPPVIEPVLEETPASSSESSVPPASKVDQEDIVYPEPSAPVEQEIPLFVPVPGLPGLSQDIPLYPPPPTGSTTASSIFAAPPVASSAPLFVPVPGPPSVSSLFSPSQVDSTSSLFAPPPTSANTTILTPAPDTTSTLFANNIPTTTPSIPDIVPTTSAELVDAPPGFQGSSDDTATNLFQGNTETQTVFSPFAQTKATPLVQETKPELVPPPIGFFAPKSESEVLSQPPLAPSPLQSFFSTAPETATTTDFNFFGSPAPGSVFPDLPVQQGIAPPPLALESPPQNSVSNIATSAIGFDLLNQTQQASSLVENSNQNSSVNSFDGYFGGPSASAAQTFANETTNALVAPAINCDPVNFFDQVPQTQSQIQQANEDQRIQNFFNNPPLQDQPAVPGELKYDIVHSGVAVKQLQERSQTPVSNLVEPPSSACSEFSTLAPAPTQTDRQSGDDLLQQHLGELPEDILRELRMASASSEKGQVATPPVAIPYSPVVAHWFYKRSVDTKFIWTPFSHYDSALLETSLNLDDSTLIIPVEGGRYDVNIKERTKTPVYWEGKAIEVRRCSWFYKGVDSKYVPYTEDTAALLEAEYKRSAETGEWHQKIMLANGEQVVFHGPTVIVHFLPQQNADTWGASTQGSMRPRVVKRDLDDFTIEQGESQRVDHLLFMVHGIGSACDLKMRSVEEVVDDFRVIAQQLVQSHYKNSTDMGLVGRVEVLPISWHGHLHSEELGIDEKLKSITLESIPRLRNFTNDTLLDVLFYTSPKYCQKIMNTVADALNDVYLKYRMRHPEFNGGVSLAGHSLGSLILFDLLCHQEPLKESEEENKNPDQLPQKQSSQKVQLPTSDPLPKQVSYAMGPEGTGQPVITYTQLIFHPKKFFALGSPIGMFVTIRGIDKLGLDFHLPTCPGFYNIFHPFDPVAYRIEALVNPDMNGIRPVLIPHHKGRKRMHLELKETMTRVGADIKQRFMDTFKTTLDSVNFLTTVTKVKKEAEESLEKETSQTSSQAFQKQTEDQDESSVASSSCKLRNRTDSNSTTASDPEFIELDFPLGKLNDSKRVDYVLQEAPLEFINEYIFALSSHVCYWGSEDTILFVMKEIYASLGISTDSQVPQSSMTIERPVSHESSVSHSLLPM
Protein: Glucocorticoid modulatory element binding protein 2 (Q5JTV1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
METENAAAAAAAAFTASSQLKEAVLVKMAEEGENLEAEIVYPITCGDSRANLIWRKFVCPGINVKCVQYDEHVISPKEFVHLAGKSTLKDWKRAIRMNGIMLRKIMDSGELDFYQHDKVCSNTCRSTKIDLSGARVSLSSPTSAEYIPLTPAAADVNGSPATITIETCEDPGDWTAAIGDDTFTFWRGLKDAGLLDEVIQEFHQELVETMRGLQQRVQDPPLQLRDAVLLNNIVQNFGMLDLVKKVLASHKCQMDRSREQYARDLAALEQQCDEHRRRAKELKHKSQHLSNVLMTLTPVSLPPPVKRPRLARATSGPAAMASQVLTQSAQLALGPGVPVPQLTSVPLGKVVSTLPSTVLGKGSLQAPPASSPASPLLGGYTVLASSGSTYPSTVEIHPDASSLTVLSTAAVQDGSTVFKVVSPLQLLTLPGLGPTLQNVAQASPGSSTIVTVPAGAAPGPEEHTATIEVAAMAEDHERK
Protein: Phenylacetaldehyde synthase (AtPAAS) (EC 4.1.1.109) (3,4-dihydroxyphenylacetaldehyde synthase) (DHPAA synthase) (EC 4.1.1.107) (Aromatic L-amino acid decarboxylase) (Aromatic aldehyde synthase) (AtAAS) (Q8RY79)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Bifunctional enzyme that catalyzes the decarboxylation of L-phenylalanine to 2-phenylethylamine, which is then oxidized to form 2-phenylacetaldehyde, a constituent of floral scent. 2-phenylacetaldehyde is a precursor of 2-phenylethanol, another constituent of floral scent. Catalyzes both the decarboxylation and deamination of L-dopa to 3,4-dihydroxylphenylacetaldehyde (DHPAA).
Interaction partners:
- GCN5-related N-acetyltransferase 1, chloroplastic
- GCN5-related N-acetyltransferase 2, chloroplastic
- Aspartate aminotransferase, mitochondrial
- Histidinol-phosphate aminotransferase 1, chloroplastic
- Tryptophan aminotransferase-related protein 1
- Tyrosine aminotransferase
- Probable aminotransferase TAT1
- Tyrosine transaminase family protein
- Probable aminotransferase TAT4
- Probable aminotransferase TAT2
Sequence:
MENGSGKVLKPMDSEQLREYGHLMVDFIADYYKTIEDFPVLSQVQPGYLHKLLPDSAPDHPETLDQVLDDVRAKILPGVTHWQSPSFFAYYPSNSSVAGFLGEMLSAGLGIVGFSWVTSPAATELEMIVLDWVAKLLNLPEQFMSKGNGGGVIQGSASEAVLVVLIAARDKVLRSVGKNALEKLVVYSSDQTHSALQKACQIAGIHPENCRVLTTDSSTNYALRPESLQEAVSRDLEAGLIPFFLCANVGTTSSTAVDPLAALGKIANSNGIWFHVDAAYAGSACICPEYRQYIDGVETADSFNMNAHKWFLTNFDCSLLWVKDQDSLTLALSTNPEFLKNKASQANLVVDYKDWQIPLGRRFRSLKLWMVLRLYGSETLKSYIRNHIKLAKEFEQLVSQDPNFEIVTPRIFALVCFRLVPVKDEEKKCNNRNRELLDAVNSSGKLFMSHTALSGKIVLRCAIGAPLTEEKHVKEAWKIIQEEASYLLHK
Protein: tRNA(Phe) 7-[(3-amino-3-carboxypropyl)-4-demethylwyosine(37)-N(4)]-methyltransferase (EC 2.1.1.282) (tRNA(Phe) 7-((3-amino-3-carboxypropyl)-4-demethylwyosine(37)-N(4))-methyltransferase) (Q381E4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Radical SAM domain protein, putative
- tRNA 4-demethylwyosine synthase
- Multifunctional methyltransferase subunit TRM112
Sequence:
MVMRAHLPLLSRASTLAFNQPAPNSTFFGQRRQKILEDLQENKNDKSLAGRVDPQVAPLVQFINEHFSCYVTSSSCSGRVSLFHKGQLSAGCPINPLAEAKVLKADANADMHNRKRGAFGQGALFQSHDPIPNVEEMVTQRLVPVLGSFEEWRSRQLQLEGGLKLMQEKKYFDSLLHETELLELKFEPMIVHVQCETLDDAARLLQCANESGQMESGILSCSRGANEQRKITCCITSSLRVALPLFAQGCWLLGHPKFDSAEWRSLLTNALVHMNVLFGVNEQRRGRFLEKLQKRLL