wanglab/gogpt-training-data huggingface dataset:
Protein: GrpE protein homolog, mitochondrial (Q18421)
Organism: Caenorhabditis elegans
Function: Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. Seems to control the nucleotide-dependent binding of mitochondrial HSP70 to substrate proteins (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000250}.
Interaction partners:
- 10 kDa heat shock protein, mitochondrial
- Heat shock protein hsp-6
- Probable mitochondrial import inner membrane translocase subunit tin-44
- Mitochondrial Ribosomal Protein, Large
- COX5B-domain-containing protein
- Chaperonin homolog Hsp-60, mitochondrial
- Histidine kinase/HSP90-like ATPase domain-containing protein
- Mitochondrial import inner membrane translocase subunit tim-16
- Mitochondrial import inner membrane translocase subunit TIM14
- Elongation factor Ts, mitochondrial
Sequence:
MLRKGVSFVGQAVQQTLKTQKNLRIQRFSATASQSSEEVNYEIRKDGKRLRGADYEEIVLTSIAGEDKTQIPKGAFDVLLKEYDDLQAESLDFKDKYQRSLAETENVRRRGIKQTDDAKVFAIQSFCKDLLEVSDILDIAVKSVKPEDLESGGKALKDLFEGVSMTRTVMAKTFAKHGLVTVDPTNEKFDPNLHEAVFQIPSANAKQPVGHIEVCTKIGYSLKERPIRPAQVGVVSK
Protein: Leukotriene A-4 hydrolase (LTA-4 hydrolase) (EC 3.3.2.6) (Leukotriene A(4) hydrolase) (Tripeptide aminopeptidase LTA4H) (EC 3.4.11.4) (P09960)
Organism: Homo sapiens (Human)
Function: Bifunctional zinc metalloenzyme that comprises both epoxide hydrolase (EH) and aminopeptidase activities. Acts as an epoxide hydrolase to catalyze the conversion of LTA4 to the pro-inflammatory mediator leukotriene B4 (LTB4). Has also aminopeptidase activity, with high affinity for N-terminal arginines of various synthetic tripeptides. In addition to its pro-inflammatory EH activity, may also counteract inflammation by its aminopeptidase activity, which inactivates by cleavage another neutrophil attractant, the tripeptide Pro-Gly-Pro (PGP), a bioactive fragment of collagen generated by the action of matrix metalloproteinase-9 (MMP9) and prolylendopeptidase (PREPL). Involved also in the biosynthesis of resolvin E1 and 18S-resolvin E1 from eicosapentaenoic acid, two lipid mediators that show potent anti-inflammatory and pro-resolving actions.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:6490615}.
Interaction partners:
- Polyunsaturated fatty acid 5-lipoxygenase
- Leukotriene C4 synthase
- Arachidonate 5-lipoxygenase-activating protein
- Cytochrome P450 4F3
- Cytochrome P450 4F2
- Leukotriene B4 receptor 2
- tRNA dimethylallyltransferase
- Leukotriene B4 receptor 1
- Phospholipase A2, membrane associated
Sequence:
MPEIVDTCSLASPASVCRTKHLHLRCSVDFTRRTLTGTAALTVQSQEDNLRSLVLDTKDLTIEKVVINGQEVKYALGERQSYKGSPMEISLPIALSKNQEIVIEISFETSPKSSALQWLTPEQTSGKEHPYLFSQCQAIHCRAILPCQDTPSVKLTYTAEVSVPKELVALMSAIRDGETPDPEDPSRKIYKFIQKVPIPCYLIALVVGALESRQIGPRTLVWSEKEQVEKSAYEFSETESMLKIAEDLGGPYVWGQYDLLVLPPSFPYGGMENPCLTFVTPTLLAGDKSLSNVIAHEISHSWTGNLVTNKTWDHFWLNEGHTVYLERHICGRLFGEKFRHFNALGGWGELQNSVKTFGETHPFTKLVVDLTDIDPDVAYSSVPYEKGFALLFYLEQLLGGPEIFLGFLKAYVEKFSYKSITTDDWKDFLYSYFKDKVDVLNQVDWNAWLYSPGLPPIKPNYDMTLTNACIALSQRWITAKEDDLNSFNATDLKDLSSHQLNEFLAQTLQRAPLPLGHIKRMQEVYNFNAINNSEIRFRWLRLCIQSKWEDAIPLALKMATEQGRMKFTRPLFKDLAAFDKSHDQAVRTYQEHKASMHPVTAMLVGKDLKVD
Protein: Alpha-ketoglutarate-dependent L-arginine hydroxylase (EC 1.14.11.41) (Viomycin biosynthesis protein C) (Q6WZB0)
Organism: Streptomyces vinaceus
Function: Involved in the biosynthesis of capreomycidine, an unusual amino acid used by non-ribosomal peptide synthases (NRPS) to make the tuberactinomycin class of peptide antibiotics such as viomycin and capreomycin. Catalyzes the stereospecific hydroxylation of the C3 of (2S)-arginine to generate (3S)-hydroxy-(2S)-arginine. Usually clavaminic acid synthase-like oxygenases catalyze the formation of threo diastereomers, however VioC produces the erythro diastereomer of beta-carbon-hydroxylated L-arginine. It exerts a broad substrate specificity by accepting the analogs L-homoarginine and L-canavanine for the beta-carbon hydroxylation.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MTESPTTHHGAAPPDSVATPVRPWSEFRLTPAEAAAAAALAARCAQRYDETDGPEFLLDAPVIAHELPRRLRTFMARARLDAWPHALVVRGNPVDDAALGSTPVHWRTARTPGSRPLSFLLMLYAGLLGDVFGWATQQDGRVVTDVLPIKGGEHTLVSSSSRQELGWHTEDAFSPYRADYVGLLSLRNPDGVATTLAGVPLDDLDERTLDVLFQERFLIRPDDSHLQVNNSTAQQGRVEFEGIAQAADRPEPVAILTGHRAAPHLRVDGDFSAPAEGDEEAAAALGTLRKLIDASLYELVLDQGDVAFIDNRRAVHGRRAFQPRYDGRDRWLKRINITRDLHRSRKAWAGDSRVLGQR
Protein: Sperm acrosome membrane-associated protein 6 (BACHELOR-like protein) (W5XKT8)
Organism: Homo sapiens (Human)
Function: Sperm protein required for fusion of sperm with the egg membrane during fertilization.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, acrosome membrane {ECO:0000269|PubMed:32210282}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Sperm-egg fusion protein TMEM95
- Izumo sperm-egg fusion protein 1
- Small nuclear ribonucleoprotein Sm D2
- DC-STAMP domain-containing protein 2
- Small nuclear ribonucleoprotein Sm D3
- Small nuclear ribonucleoprotein F
- Small nuclear ribonucleoprotein E
- Small nuclear ribonucleoprotein G
- U6 snRNA-associated Sm-like protein LSm4
Sequence:
MALLALASAVPSALLALAVFRVPAWACLLCFTTYSERLRICQMFVGMRSPKLEECEEAFTAAFQGLSDTEINYDERSHLHDTFTQMTHALQELAAAQGSFEVAFPDAAEKMKKVITQLKEAQACIPPCGLQEFARRFLCSGCYSRVCDLPLDCPVQDVTVTRGDQAMFSCIVNFQLPKEEITYSWKFAGGGLRTQDLSYFRDMPRAEGYLARIRPAQLTHRGTFSCVIKQDQRPLARLYFFLNVTGPPPRAETELQASFREVLRWAPRDAELIEPWRPSLGELLARPEALTPSNLFLLAVLGALASASATVLAWMFFRWYCSGN
Protein: Antizyme inhibitor 2 (AzI2) (Arginine decarboxylase-like protein) (ADC) (ARGDC) (Ornithine decarboxylase-like protein) (ODC-like protein) (ornithine decarboxylase paralog) (ODC-p) (Q8BVM4)
Organism: Mus musculus (Mouse)
Function: Antizyme inhibitor (AZI) protein that positively regulates ornithine decarboxylase (ODC) activity and polyamine uptake. AZI is an enzymatically inactive ODC homolog that counteracts the negative effect of ODC antizymes (AZs) OAZ1, OAZ2 and OAZ3 on ODC activity by competing with ODC for antizyme-binding. Inhibits antizyme-dependent ODC degradation and releases ODC monomers from their inactive complex with antizymes, leading to formation of the catalytically active ODC homodimer and restoring polyamine production. Participates in the morphological integrity of the trans-Golgi network (TGN) and functions as a regulator of intracellular secretory vesicle trafficking (By similarity).
Subcellular location: Nucleus. Cytoplasm. Cytoplasm, perinuclear region {ECO:0000250}. Membrane. Cytoplasmic vesicle {ECO:0000250}. Endoplasmic reticulum-Golgi intermediate compartment. Golgi apparatus, cis-Golgi network. Golgi apparatus, trans-Golgi network {ECO:0000250}. Cytoplasmic granule. Cell projection, axon {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Perikaryon {ECO:0000250}. Note=Detected as vesicle-like pattern in neurite outgrowths. Localizes to the vesicular compartments of the secretory pathway, predominantly in the trans-Golgi network (TGN). Localizes with vesicle-associated membrane protein VAMP8 in the vicinity of the plasma membrane within serotonin-containing secretory granules (By similarity). Colocalizes with KDEL receptors in ER-Golgi intermediate compartment (ERGIC). Translocates from the ERGIC structure to the cytoplasm in a antizyme-dependent manner. Localizes with vesicle-associated membrane protein VAMP8 in the vicinity of the plasma membrane within serotonin-containing secretory granules. {ECO:0000250}.
Interaction partners:
- Guanidino acid hydrolase, mitochondrial
- Arginase-2, mitochondrial
- Glycine amidinotransferase, mitochondrial
- Arginase-1
- Ornithine decarboxylase antizyme 3
- Argininosuccinate lyase
- Nitric oxide synthase 1
- Nitric oxide synthase 3
- Nitric oxide synthase, inducible
- Ornithine decarboxylase antizyme 1
Sequence:
MAGYLSESDFVMVEEGFSTRDLLEELTLGASQATSGKVAAFFVADLGAVVRKHFCFLKHLPRVRPFYAVGCNSSLGVLKVLAELGLGFSCANKAEMELVQHIGVPASKIICANPCKQVAQIKYAAKHGVRLLSFDNEVELAKVVKSHPSAKMVLCIATQDSHSLNHLSLRFGASLKSCRHLLENAKKSHVEVVGVSFHIGSGCPDPQAYAQSIADARLVFQMGEELGHTMNILDLGGGFPGLEGAKVRFEEMASVINSALDLYFPEGCGVDILAELGRYYVTSAFTVAVSIVAKREVLDQASREEQTGAAPKSIVYYLDEGVYGVFNSVLFDNTCPTPALQKKPSADQPLYSSSLWGPAVEGCDCVAEGLWLPQLQVGDWLVFDNMGAYTVDTKSLLGGTQARRVTYAMSRLAWEALRGQLLPAEEDQDAEGVCKPLSCGWEITDTLCVGPVFTPASIM
Protein: Nicotinamidase/pyrazinamidase (Nicotinamidase) (EC 3.5.1.19) (Nicotinamide deamidase) (NAMase) (Pyrazinamidase) (PZAase) (EC 3.5.1.-) (I6XD65)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the deamidation of nicotinamide (NAM) into nicotinate. Likely functions in the cyclical salvage pathway for production of NAD from nicotinamide (By similarity).
Interaction partners:
- Nicotinate phosphoribosyltransferase pncB1
- Nicotinate phosphoribosyltransferase pncB2
- Small ribosomal subunit protein uS12
- Enoyl-[acyl-carrier-protein] reductase
- DNA-directed RNA polymerase subunit beta
- Probable arabinosyltransferase B
- Catalase-peroxidase
- DNA gyrase subunit A
- DNA gyrase subunit B
- Conserved protein
Sequence:
MRALIIVDVQNDFCEGGSLAVTGGAALARAISDYLAEAADYHHVVATKDFHIDPGDHFSGTPDYSSSWPPHCVSGTPGADFHPSLDTSAIEAVFYKGAYTGAYSGFEGVDENGTPLLNWLRQRGVDEVDVVGIATDHCVRQTAEDAVRNGLATRVLVDLTAGVSADTTVAALEEMRTASVELVCSS
Protein: Apidaecin + (C0HKX5)
Organism: Dolichovespula maculata (Bald-faced hornet) (Vespula maculata)
Function: Antimicrobial peptide active against many Gram-negative enterobacterial and plant-associated bacterial species. Not active against other bacterial species like H.pylori, P.mirabilis, B.pertussis or N.gonorrhoeae.
Subcellular location: Secreted {ECO:0000269|PubMed:7929322}.
Interaction partners:
Sequence:
GKPRPQQVPPRPPHPRL
Protein: Putative plasmid segregation protein (A0A0A0PJ25)
Organism: Bacillus phage Bp8p-T
Interaction partners:
Sequence:
MCPGSYEVVDTLMMNLPIKYDTEERRKALTKLAQGTHLIDISHDGKNFINKMITVEHVDIKKQPFGSICDLVLDESGNLSNREVAKGFNVVVDVGARTLNILTVDGLVEQPELSIQTNDGMFTAYKQVGSHLETSLGATIPDGKYPQIIAAREFKGRNIDPLIDAAYATQANNIMNVLDKVLINSWAFVQCIVFTGGGSELLKPYLLPRVPNNVEAVVLDRYANARGLRKYGMRQAKKNIKRADHYGG
Protein: Ras-related protein rac-2 (Q94124)
Organism: Caenorhabditis elegans
Function: During gonad morphogenesis, plays a role in distal tip cell (DTC)-mediated guidance of gonad elongation.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Serine/threonine-protein kinase pak-1
- NCK adaptor protein family
- Serine/threonine-protein kinase max-2
- Probable rho GDP-dissociation inhibitor
- Stress-activated protein kinase jnk-1
- Stress-activated protein kinase JNK
- GLH-binding kinase 1
- Rac-like GTPase
- CRAL-TRIO domain-containing protein
- DH domain-containing protein
Sequence:
MQAIKCVVVGDGAVGKTCLLLSYTTNAFPGEYILTVFDTYSTNVMVDGRPINLSLWDTAGQDDYDQFRHLSFPQTDVFLVCFALNNPASFENVRAKWYPEVSHHCPNTPIILVGTKADLREDRDTIERLRERRLQPVSHTQGYVMAKEIKAVKYLECSALTQIGLKQVFDEAIRTGLTPPQTPQTRAKKSNCTVL
Protein: Striatin-interacting protein 1 (Protein FAM40A) (Q5VSL9)
Organism: Homo sapiens (Human)
Function: Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the cortical actin filament dynamics and cell shape.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21834987}. Note=Enriched on the plasma membrane.
Interaction partners:
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
- CTTNBP2 N-terminal-like protein
- Serine/threonine-protein kinase 25
- Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
- Striatin-3
- Programmed cell death protein 10
- Striatin-4
- Serine/threonine-protein kinase 26
- MOB-like protein phocein
- Striatin
Sequence:
MEPAVGGPGPLIVNNKQPQPPPPPPPAAAQPPPGAPRAAAGLLPGGKAREFNRNQRKDSEGYSESPDLEFEYADTDKWAAELSELYSYTEGPEFLMNRKCFEEDFRIHVTDKKWTELDTNQHRTHAMRLLDGLEVTAREKRLKVARAILYVAQGTFGECSSEAEVQSWMRYNIFLLLEVGTFNALVELLNMEIDNSAACSSAVRKPAISLADSTDLRVLLNIMYLIVETVHQECEGDKAEWRTMRQTFRAELGSPLYNNEPFAIMLFGMVTKFCSGHAPHFPMKKVLLLLWKTVLCTLGGFEELQSMKAEKRSILGLPPLPEDSIKVIRNMRAASPPASASDLIEQQQKRGRREHKALIKQDNLDAFNERDPYKADDSREEEEENDDDNSLEGETFPLERDEVMPPPLQHPQTDRLTCPKGLPWAPKVREKDIEMFLESSRSKFIGYTLGSDTNTVVGLPRPIHESIKTLKQHKYTSIAEVQAQMEEEYLRSPLSGGEEEVEQVPAETLYQGLLPSLPQYMIALLKILLAAAPTSKAKTDSINILADVLPEEMPTTVLQSMKLGVDVNRHKEVIVKAISAVLLLLLKHFKLNHVYQFEYMAQHLVFANCIPLILKFFNQNIMSYITAKNSISVLDYPHCVVHELPELTAESLEAGDSNQFCWRNLFSCINLLRILNKLTKWKHSRTMMLVVFKSAPILKRALKVKQAMMQLYVLKLLKVQTKYLGRQWRKSNMKTMSAIYQKVRHRLNDDWAYGNDLDARPWDFQAEECALRANIERFNARRYDRAHSNPDFLPVDNCLQSVLGQRVDLPEDFQMNYDLWLEREVFSKPISWEELLQ
Protein: Protein sprouty homolog 1 (Spry-1) (O43609)
Organism: Homo sapiens (Human)
Function: Inhibits fibroblast growth factor (FGF)-induced retinal lens fiber differentiation, probably by inhibiting FGF-mediated phosphorylation of ERK1/2 (By similarity). Inhibits TGFB-induced epithelial-to-mesenchymal transition in lens epithelial cells (By similarity).
Subcellular location: Cytoplasm. Membrane; Peripheral membrane protein. Note=Found in the cytoplasm in unstimulated cells but is translocated to the membrane ruffles in cells stimulated with EGF (epidermal growth factor).
Interaction partners:
- Growth factor receptor-bound protein 2
- E3 ubiquitin-protein ligase CBL
- Son of sevenless homolog 1
- RAF proto-oncogene serine/threonine-protein kinase
- Protein sprouty homolog 2
- Fibroblast growth factor receptor substrate 2
- Epidermal growth factor receptor
- Fibroblast growth factor 8
Sequence:
MDPQNQHGSGSSLVVIQQPSLDSRQRLDYEREIQPTAILSLDQIKAIRGSNEYTEGPSVVKRPAPRTAPRQEKHERTHEIIPINVNNNYEHRHTSHLGHAVLPSNARGPILSRSTSTGSAASSGSNSSASSEQGLLGRSPPTRPVPGHRSERAIRTQPKQLIVDDLKGSLKEDLTQHKFICEQCGKCKCGECTAPRTLPSCLACNRQCLCSAESMVEYGTCMCLVKGIFYHCSNDDEGDSYSDNPCSCSQSHCCSRYLCMGAMSLFLPCLLCYPPAKGCLKLCRRCYDWIHRPGCRCKNSNTVYCKLESCPSRGQGKPS
Protein: Inosine-5'-monophosphate dehydrogenase 1 (IMP dehydrogenase 1) (IMPD 1) (IMPDH 1) (EC 1.1.1.205) (P47996)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03156}.
Interaction partners:
- GMP synthase
- Adenylosuccinate synthetase, chloroplastic
- AMP deaminase
- AICARFT/IMPCHase bienzyme family protein
- Hypoxanthine phosphoribosyltransferase
- At1g72880
- Inosine triphosphate pyrophosphatase
- Adenylosuccinate lyase
- Adenylosuccinate lyase
- Haloacid dehalogenase-like hydrolase
Sequence:
MSTLEDGFPADKLFAQGYSYTYDDVIFLPHFIDFSTDAVSLSTRLSRRVPLSIPCVSSPMDTVSESHMAAAMASLGGIGIVHYNCGIAAQASIIRQAKSLKHPIASDAGVKFPEYEITSLDAFGPSSFVFVEQTGTMTTPKLLGYVTKSQWKRMNYEQREMKIYDYMKSCDSSDYCVPWEIDFEKLEFVLEDKQKGFVVLERDGETVNVVTKDDIQRVKGYPKSGPGTVGPDGEWMVGAAIGTRESDKERLEHLVNVGVNAVVLDSSQGNSIYQLEMIKYVKKTYPELDVIGGNVVTMYQAQNLIQAGVDGLRVGMGSGSICTTQEVCAVGRGQATAVYKVCSIAAQSGIPVIADGGISNSGHIVKALVLGASTVMMGSFLAGSTEAPGGYEYTNGKRIKKYRGMGSLEAMTKGSDQRYLGDQTKLKIAQGVVGAVADKGSVLKLIPYTMHAVKQGFQDLGASSLQSAHGLLRSNILRLEARTGAAQVEGGVHGLVSYEKKSF
Protein: Lipophosphoglycan biosynthetic protein (Q9BIR6)
Organism: Leishmania major
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- LPG5B protein
- Beta galactofuranosyl transferase
- Endoplasmin homolog
Sequence:
MNHTRAVMEAILAVITYSFCSVSMILVNKLIMNTYDMNFPFGILVLQTGGALVIVALAKAARFVEYPAFSFDVAKKWLPLTLLFVAMLFTSMKSLATMSVAAQTILKNLAVILIALGDKFLYGKAQTPMVYFSFALMILGSFLGAKGDKWVTAWGLIWTLLNIVSTVSYTLYMKAVLGSVSNSIGRYGPVFYNNLLSLPFFLIMGVGEIMPFSAAIGETTTLGKLVLTFSVLVSSVMTFSVFWCMSITSPTTMSVVGSLNKIPLTFLGMLAFHQFPTATGYLGIMVALSAGFLYTHLNIRANRAKASSDLEHQMQQTGKTTTESIVLVRTDENSSDNFKSE
Protein: Double homeobox protein A (A6NLW8)
Organism: Homo sapiens (Human)
Function: Transcription factor that acts as repressor.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
Interaction partners:
- Paired-like homeodomain transcription factor LEUTX
- Tetra-peptide repeat homeobox protein 1
- Arginine-fifty homeobox
Sequence:
MAEDTYSHKMVKTNHRRCRTKFTEEQLKILINTFNQKPYPGYATKQKLALEINTEESRIQIWFQNRRARHGFQKRPEAETLESSQSQGQDQPGVEFQSREARRCRTTYSASQLHTLIKAFMKNPYPGIDSREELAKEIGVPESRVQIWFQNRRSRLLLQRKREPVASLEQEEQGKIPEGLQGAEDTQNGTNFTSDSHFSGARTW
Protein: Glutaminase liver isoform, mitochondrial (GLS) (EC 3.5.1.2) (L-glutaminase) (L-glutamine amidohydrolase) (LGA) (Q571F8)
Organism: Mus musculus (Mouse)
Function: Plays an important role in the regulation of glutamine catabolism. Promotes mitochondrial respiration and increases ATP generation in cells by catalyzing the synthesis of glutamate and alpha-ketoglutarate. Increases cellular anti-oxidant function via NADH and glutathione production. May play a role in preventing tumor proliferation.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q9UI32}.
Interaction partners:
- Glutamine synthetase
- Glutamate dehydrogenase 1, mitochondrial
- Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial
- Glutamate decarboxylase 1
- Glutamate decarboxylase 2
- Amidophosphoribosyltransferase
- Glutamine--fructose-6-phosphate aminotransferase 1
- Carbamoyl-phosphate synthase, mitochondrial
- Glutamine--fructose-6-phosphate aminotransferase 2
- Multifunctional protein CAD
Sequence:
MRSMRALQNALSRAGSHGRRGGWGHPSRGPLLGRGVRYYLGEAAAQGRGTPHSHQPQHSDHDASHSGMLPRLGDLLFYTIAEGQERIPIHKFTTALKATGLQTSDPRLQDCMSKMQRMVQESSSGGLLDRELFQKCVSSNIVLLTQAFRKKFVIPDFEEFTGHVDRIFEDAKEPTGGKVAAYIPHLAKSNPDLWGVSLCTVDGQRHSVGHTKIPFCLQSCVKPLTYAISVSTLGTDYVHKFVGKEPSGLRYNKLSLNEEGIPHNPMVNAGAIVVSSLIKMDCNKAEKFDFVLQYLNKMAGNEFMGFSNATFQSEKETGDRNYAIGYYLKEKKCFPKGVDMMAALDLYFQLCSVEVTCESGSVMAATLANGGICPITGESVLSAEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSAVSGAILLVVPNVMGMMCLSPPLDKLGNSQRGINFCQKLVSLFNFHNYDNLRHCARKLDPRREGGEVRNKTVVNLLFAAYSGDVSALRRFALSAMDMEQKDYDSRTALHVAAAEGHIEVVKFLIEACKVNPFVKDRWGNIPLDDAVQFNHLEVVKLLQDYHDSYLLSETQAEAAAETLSKENLESMV
Protein: F2K11.11 (Q9SH37)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MRVDFSEPEYRNCYHCRDSGILNTQESEPNNVIGSSITSVPVSSGPFQALGHASAAIGSTSTSSPVQSSSSFSFGSAPAATTSVGVSSTSTPTPISFLPFGYVPPPPPSSSLSGPAQNVPWSISAYSTAGRGVEWAWARPDVAVYPASSSSSSTSTVVFGTTPVSVSSLFGPSQDFPKTTFACCSSTPAPTRCECSFAKPFFGSSPASSSSNLFGPNPSTTTASVFGTSATSGSSLFGPAQHPLSYDSIGGSAFAGVKTSSPQPLGFNGATTLLPSSHEGQNISSFKPYVDKSHDELRWEYYKKEAKGGSFPAAHASPIGSKPNAVFSPSTVSTSLFASPSVPDHHQRTNFSTTLGNFTGPAFGFFPAAAGGATTFSSTGFGQPNAPFPGFDSQFPSAFSSFSTTYPAVSSSVQRPHETGAVSSPAFGCTACGATSSSSASDHFTFNGATTPPGLFFPTTSSGPMMFGTTLAAQGTTPALQTYPVQGFILLPFAAMSLQ
Protein: Serine/threonine-protein kinase SBK1 (EC 2.7.11.1) (SH3 domain-binding kinase 1) (Q9Z335)
Organism: Rattus norvegicus (Rat)
Function: May be involved in signal-transduction pathways related to the control of brain development.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11322885}.
Interaction partners:
Sequence:
MSVGCPEPEPLHSLPCCGPGAAPVPGAGVPLLTEDMQALTLRTLAASDVTKHYELVRELGKGTYGKVDLVAYKGTGTKMALKFVNKSKTKLKNFLREVSITNSLSSSPFIIKVFDVVFETEECYVFAQEYAPAGDLFDIIPPQVGLPEDTVKRCVQQLGLALDFMHSRQLVHRDIKPENVLLFDRECRRVKLADFGMTRRVGCRVKRVSGTIPYTAPEVCQAGRADGFAVDTGVDVWAFGVLIFCVLTGNFPWEAASGADAFFEEFVRWQRGRLPGLPSQWRRFTEPALRMFQRLLALEPERRGPAKEVFRFLKHELTSELRRRPSHRARKPPGDRLPGPLRLEAPGPLKRTVLTESGSGSRPSPPSVGPVVPVPVPVPVPVPEAGLAPPAPPGRTDGRADKSKGQVVLATAIEICV
Protein: Ammonium transporter Rh type B (Rhesus blood group family type B glycoprotein) (Rh family type B glycoprotein) (Rh type B glycoprotein) (Q4VUI0)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: Functions as a specific ammonium transporter.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9H310}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9H310}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q9H310}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Gamma-crystallin B
- Transcobalamin 1.
Sequence:
MARSPRRAGAPRLQLPLLCLLLQGATAILFAVFVRYNHETDAALWHWGNHSNLDNEFYFRYPSFQDVHVMVFVGFGFLMAFLQRYGFSSVGFTFLLAAFALQWSTLIQGFFHSLHGGYIHVSVNSMINADFCAGAVLISFGAILGKTGPAQLLLMTVLEVALFGINEFVLLNLLQVKDAGGSMTIHTFGAYFGLVLSRVLYRPQLEKSKHRQCSVYHSDLFAMIGTIFLWIFWPSFNSAPTTLGDGQHRTALNTYYSLSASTLGTFAMSALVGERGRLDMVHIQNAALAGGVVVGTAGEMMLTPFGALAAGFLAGTVSTLGYKFFTPILEAKFKVQDTCGVHNLHGIPGVLGALLGVLVVGLATHEAYGEGLGSVFPLIAKGQRTAMSQAMYQLFGLFVTLMFASVGGALGGLLLKLPCLGSPADCQCYEDQVYWEVPGEHEDAAQGPLKAEEPDTQA
Protein: M-myrmeciitoxin-Mp1 (M-MIITX-Mp1) (Allergen Myr p I) (Major allergen Myr p 1) (Pilosulin-1) (allergen Myr p 1) [Cleaved into: M-myrmeciitoxin-Mp1a (M-MIITX-Mp1a) (M-myrmeciitoxin-Mp1b) (M-MIITX-Mp1b) (Pilosulin-1 57->112) (Myr p 1 57->112) (Myr p 1 57->112 (Ile5)) ([Ile-5]pilosulin-1); M-myrmeciitoxin-Mp1c (M-MIITX-Mp1c) (Pilosulin-1 65->112) (Myr p 1 65->112); M-myrmeciitoxin-Mp1d (M-MIITX-Mp1d) (Pilosulin-1 68->112) (Myr p 1 68->112); M-myrmeciitoxin-Mp1e (M-MIITX-Mp1e) (Pilosulin-1 71->112) (Myr p 1 71->112); U1-myrmeciitoxin-Mp1f (U1-MIITX-Mp1f) (Pilosulin-1 86->112) (Myr p 1 86->112)] (Q07932)
Organism: Myrmecia pilosula (Jack jumper ant) (Australian jumper ant)
Function: Has strong cytotoxic and hemolytic activities. Is more potent against mononuclear leukocytes than against granulocytes. The synthesized peptide 57-76 shows a potent and broad spectrum antimicrobial activity against both Gram-positive and Gram-negative bacteria, and also against the fungus C.albicans. Adopts an alpha-helical structure.
Subcellular location: Secreted {ECO:0000269|PubMed:8866004}.
Interaction partners:
Sequence:
MKLSCLLLTLTIIFVLTIVHAPNVEAKDLADPESEAVGFADAFGEADAVGEADPNAGLGSVFGRLARILGRVIPKVAKKLGPKVAKVLPKVMKEAIPMAVEMAKSQEEQQPQ
Protein: NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial (Complex I-9kD) (CI-9kD) (NADH-ubiquinone oxidoreductase 9 kDa subunit) (Q6PCU8)
Organism: Rattus norvegicus (Rat)
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. May be the terminally assembled subunit of Complex I.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P56181}; Peripheral membrane protein {ECO:0000250|UniProtKB:P56181}; Matrix side {ECO:0000250|UniProtKB:P56181}.
Interaction partners:
- NADH dehydrogenase 1 alpha subcomplex subunit 12
- NADH dehydrogenase 1 beta subcomplex subunit 10
- NADH dehydrogenase iron-sulfur protein 4, mitochondrial
- NADH dehydrogenase iron-sulfur protein 6, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 6
- NADH dehydrogenase flavoprotein 2, mitochondrial
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 5
- NADH dehydrogenase 1 beta subcomplex subunit 5, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 7
Sequence:
MAVSLLLRGGRIRALKAALLEAKVFRGELASTVPLSTESENNKKAAGPTSKTESVFKEPTLVPESSDTTTYKNLQHHEYNAFTFLDLNLDLSKFRLPQPSSGRESPRH
Protein: Glucose-1-phosphate adenylyltransferase large subunit 2, chloroplastic (EC 2.7.7.27) (ADP-glucose pyrophosphorylase) (ADP-glucose synthase) (AGPase S) (Alpha-D-glucose-1-phosphate adenyl transferase) (P55230)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: This protein plays a role in synthesis of starch. It catalyzes the synthesis of the activated glycosyl donor, ADP-glucose from Glc-1-P and ATP.
Subcellular location: Plastid, chloroplast.
Interaction partners:
- Granule-bound starch synthase 1, chloroplastic/amyloplastic
- Phosphoglucomutase, chloroplastic
- Probable phosphoglucomutase, cytoplasmic 1
- Probable phosphoglucomutase, cytoplasmic 2
- Probable starch synthase 4, chloroplastic/amyloplastic
- Sucrose synthase 3
- Sucrose synthase 4
- Sucrose synthase 5
- Sucrose synthase 2
- Sucrose synthase 6
Sequence:
MESCFPAMKLNQCTFGLNNEIVSERVSAFWGTQVVKPNHLRTTKLRSAPQKKIQTNLIRSVLTPFVDQESHEPLLRTQNADPKNVASIILGGGAGTRLFPLTSKRAKPAVPIGGCYRLIDIPMSNCINSGIRKIFILTQFNSFSLNRHLSRTYNFGNGVNFGDGFVEVLAATQTSGDAGKKWFQGTADAVRQFIWVFEDAKTKNVEHVLILSGDHLYRMDYMNFVQKHIESNADITVSCLPMDESRASDFGLLKIDQSGKIIQFSEKPKGDDLKAMQVDTSILGLPPKEAAESPYIASMGVYVFRKEVLLKLLRSSYPTSNDFGSEIIPLAVGEHNVQAFLFNDYWEDIGTIGSFFDANLALTEQPPKFQFYDQKTPFFTSPRFLPPTKVDKCRILDSIVSHGCFLRECSVQHSIVGIRSRLESGVELQDTMMMGADFYQTEAEIASLLAEGKVPVGVGQNTKIKNCIIDKNAKIGKNVVIANADGVEEGDRPEEGFHIRSGITVVLKNATIRDGLHI