wanglab/gogpt-training-data huggingface dataset:
Protein: C4-type zinc ribbon domain-containing protein (Q0PAH3)
Organism: Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Interaction partners:
- GTP cyclohydrolase 1 type 2 homolog
- 3-deoxy-D-manno-octulosonic acid transferase
- RNA pseudouridylate synthase
- DUF3972 domain-containing protein
- Glycine--tRNA ligase alpha subunit
- N5-carboxyaminoimidazole ribonucleotide mutase
- Protease
- Chemotaxis protein
- 3,4-dihydroxy-2-butanone 4-phosphate synthase
- histidine kinase
Sequence:
MNKYLEQLVLLSKIDQEIDSYEPKIDSINKTLKDAELKIEKINADLEKIDEEIKDIENQKIQNNAHISEFSAKIKDLSKKSGVVKTEKEANALKIEEDIAKEQLDAANDEIVRLDKILENKETYKKELEEEKIKQEQNINEIRVSIKSEMEVLEKDRMSVYDKKTKLVSEMNQKVLSFYEKIRKWAKNTAVVPVKKQACYGCFMKIYDKTYLSVVKGEEIVTCPHCGRILYKEQEEQN
Protein: Protein NRT1/ PTR FAMILY 2.3 (AtNPF2.3) (Probable nitrate excretion transporter 3) (Protein NAXT1-like 2) (Q9M175)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transporter involved in a passive nitrate efflux.
Subcellular location: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- High affinity nitrate transporter 2.5
- Peptide transporter family protein
- Uncharacterized protein At5g19190
- High affinity nitrate transporter 2.4
- At5g43870)
- Tagatose-6-phosphate ketose/aldose isomerase, putative
- High affinity nitrate transporter 2.7
Sequence:
MASLVSGDKEAQISGDPGSKRGGWITFPFMLATLLGLSVTSFGWVMNLIVFLIEEFNIKSIAAAQISNVANGCLSMLPVVAAILADSFFGNIPVIAASSFISLLGIVLLTLIASLDYLRPRPCEAGSVLCTPPSKLHLGILYTALALVTTGAGGTRFTMASAGANQYEKPKEQGSFFNWYFLTLYAGAITGATAIVYIQDNASWKLGFGLCAAANLISFIVFVSGKRYYKHDKPMGSPFTSLIRVVVSATVKRKAVISCNEEDYHHYGLEKEVKTSAAMPSKSFRFLNRAALMTKDDLNQKEGSVNNIWRLCSVQEVEDFKAILRVFPLWLSIIFVSTPMVMQTSLIVLQALVTDRGLGPNFKVPAGSLQVIIIITACIVIIMNNWLVFPMYKKLTHKLLTPLQKVGIGQVLTILSMALSAVVEAKRLKTVENGHPMSVLWLFPPLVIVGIGEAFQFPANIELFYGEFPESLRNTATSLTSVVIGISFYLSTALIDLIQRTTAWLPNDINHGRVDNVYWLLVIGGILNFGYFLVCSWVYKYRNLKDNDQEQDPKDGTM
Protein: ATP synthase F(1) complex subunit epsilon, mitochondrial (ATPase subunit epsilon) (ATP synthase F1 subunit epsilon) (P56382)
Organism: Mus musculus (Mouse)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits (By similarity).
Subcellular location: Mitochondrion. Mitochondrion inner membrane.
Interaction partners:
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit d, mitochondrial
- ATP synthase F
- ATP synthase peripheral stalk subunit b, mitochondrial
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit F6, mitochondrial
Sequence:
MVAYWRQAGLSYIRFSQICAKAVRDALKTEFKANAEKTSGSSIKIVKVSKKE
Protein: protein-tyrosine-phosphatase (EC 3.1.3.48) (Q9V3V3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell junction {ECO:0000256|ARBA:ARBA00004282}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- Protein kibra
- Transcriptional coactivator yorkie
- 6-pyruvoyl tetrahydrobiopterin synthase
- Myopic
- Dizzy isoform AII
Sequence:
MPLKFLKKCRQYNVTSKSLFVISVHHLLDTSSTVDCTISSESKGQECLDNVCQRLLIQQPEFFGLRYLVKGKDKEDEFKWIDLERSLSRQLEKYAAGPKIYLRVRHYVTTGVRHLSDEATRFYYFLQLKSDIYEGRIACDIRTAILLALYCRQAEYDSYQGDKQSKDYLKKSLVLPRNMQGLANDDSMLEGLIVEVLQQQAGIAHLSQSQAEEMYIQCCQQLEGYGEERFAAKDTLGNDLLLGLAINGMVVNADNGRQYFPWKEFHTVTIDKRTIKIEQNKLDGGGSIVGSFIFSEADTARYFWKLTISQHKFFKRYIDTATPSSLGSGADAESGPLGVDSVGYVDYDYNEAAAAEQLQQHHQQQQHMQQQQQIQQQQMISSNISLATSANQMLGQSSSCLDLSNNNLHSSSGMLHHGGSNNNNNNDERERLKAMLPTYRPAPDYETAVQLKYRTPSAEFHNVALAMAAPGNAYYAGSQPDVHNPGMHNENLLYGHMTAHRYPDVAQPAAALHHHINLYQAQHQPQSHPQPMSPAQAYLELSQRMHMMRHKAPPPYVNRLSSSSTPDLAVATPRPLQGFRNYVSGSSPDLVSNRTLFNGGQYVALPAGGHAGNIPTSSGATMLHQYQYVSHMGHSQPYLPPHGTFENLNMIEEQPSIMSQLRQSAMSQAAAAAAGSVVTQSSPTLPPSGYRSSVPPPASSPLPPPVVASSHKSATPAPLQRSLVNGSIEPIYENVPLPQRASGGSSGAANTEAMRQRASSIQSAPGVVPVPAARNASSNNVVTVTVNSPPDDGNIKKYGADRAASTELLFLEPQAPKRTNRAASAAPDMGATPPPRQHRSTASLNKSSTVDMITPAGDTLQQQFSAMNLSANTSASTSSMFNSTLDTTSSSAASKDLKRKKRWNFLSRSKTPDKQKSATLGREKATTAGQHSKLAAKLKLAQDDLNLPNRWSTGVNKPQPISGRYSKDKLCQILDQKLSDSQLFMEFERIPKRREHALYECALLEENEPKNHDPNFLPYDDNRVRLTPCRDNRHGYVNASSISATVGTKQRFYIVAQSPQEPLTMRIFWQCVWEADVYLVVQLTEDMSYIPRNSHQRLEFGQFQVYQEFSQTTDRCTTIKLRLYHVPSRRYRSVWYLQYADWAEQNCPRDVNHFLDFLEELNSVRLASTQEVPPGHNTNPPVLLHCLEGGGRSGVTLTADLLLYTLDHNEDLDIPRVIGQLRHQRDSIIPSLAQYKFIYNLLITYLKRTRLI
Protein: N(G),N(G)-dimethylarginine dimethylaminohydrolase 1 (DDAH-1) (Dimethylarginine dimethylaminohydrolase 1) (EC 3.5.3.18) (DDAHI) (Dimethylargininase-1) (O94760)
Organism: Homo sapiens (Human)
Function: Hydrolyzes N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-monomethyl-L-arginine (MMA) which act as inhibitors of NOS. Has therefore a role in the regulation of nitric oxide generation.
Interaction partners:
- Nitric oxide synthase 3
- Alanine--glyoxylate aminotransferase 2, mitochondrial
Sequence:
MAGLGHPAAFGRATHAVVRALPESLGQHALRSAKGEEVDVARAERQHQLYVGVLGSKLGLQVVELPADESLPDCVFVEDVAVVCEETALITRPGAPSRRKEVDMMKEALEKLQLNIVEMKDENATLDGGDVLFTGREFFVGLSKRTNQRGAEILADTFKDYAVSTVPVADGLHLKSFCSMAGPNLIAIGSSESAQKALKIMQQMSDHRYDKLTVPDDIAANCIYLNIPNKGHVLLHRTPEEYPESAKVYEKLKDHMLIPVSMSELEKVDGLLTCCSVLINKKVDS
Protein: Probable ATP-binding component of ABC transporter (Q9I2T7)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Inner membrane ABC transporter permease protein YejB
- Probable permease of ABC transporter
- Probable binding protein component of ABC transporter
- Probable solute-binding protein
- Probable permease of ABC transporter
- ABC-type dipeptide transporter
- Inner membrane ABC transporter permease protein YejB
- Probable permease of ABC transporter
- Enoyl-[acyl-carrier-protein] reductase FabI
- Probable permease of ABC transporter
Sequence:
MSENILEIRDLAVEFLSGEQRQRVVEGVSFDIRQGETLALVGESGSGKSVTAHSILRLLPYSVASHPAGSIHYQGEDLLKLPERRLRGIRGNRIAMVFQEPMTSLNPLHTIEKQLAEVLALHKGLGGAKASARILELLELVGIPEPAKRLKAYPHELSGGQRQRVMIAMALACEPQLLIADEPTTALDVTVQLKILDLLKDLQARLGMSLLLITHDLNLVRRIAHRVCVMQQGRIVEQASCQELFAAPRHPYTRELLNAEPSGAPASNPPGETLLAVDDLRVWFPIRKGVFRRTVDHVKAVDGVNFELPRGQTLGIVGESGSGKSTLGLAILRLLESQGGIRFEGTRLDGLAQHDVRPLRREMQVVFQDPYGSLSPRMCVGEIVGEGLRIHRIGSEAEQEQAIIDALVEVGLDPQTRYRYPHEFSGGQRQRIAIARALVLKPALILLDEPTSALDRTVQRQVVELLRQLQGKYNLTYLFISHDLAVVKALSHQLMVVRHGKVVEQGSAEAVFASPQHPYTQQLLEAAFMAPASAEN
Protein: Hyaluronidase PH-20 (Hyal-PH20) (EC 3.2.1.35) (Hyaluronoglucosaminidase PH-20) (Sperm adhesion molecule 1) (Sperm surface protein PH-20) (P38567)
Organism: Homo sapiens (Human)
Function: Involved in sperm-egg adhesion. Upon fertilization sperm must first penetrate a layer of cumulus cells that surrounds the egg before reaching the zona pellucida. The cumulus cells are embedded in a matrix containing hyaluronic acid which is formed prior to ovulation. This protein aids in penetrating the layer of cumulus cells by digesting hyaluronic acid.
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor.
Interaction partners:
- Alpha-L-iduronidase
- Beta-glucuronidase
- Arylsulfatase B
- C-Jun-amino-terminal kinase-interacting protein 4
- Macrophage-stimulating protein receptor
- Disintegrin and metalloproteinase domain-containing protein 2
- Zona pellucida sperm-binding protein 3
- Hyaluronan synthase 2
- Heat shock-related 70 kDa protein 2
- Zona pellucida sperm-binding protein 4
Sequence:
MGVLKFKHIFFRSFVKSSGVSQIVFTFLLIPCCLTLNFRAPPVIPNVPFLWAWNAPSEFCLGKFDEPLDMSLFSFIGSPRINATGQGVTIFYVDRLGYYPYIDSITGVTVNGGIPQKISLQDHLDKAKKDITFYMPVDNLGMAVIDWEEWRPTWARNWKPKDVYKNRSIELVQQQNVQLSLTEATEKAKQEFEKAGKDFLVETIKLGKLLRPNHLWGYYLFPDCYNHHYKKPGYNGSCFNVEIKRNDDLSWLWNESTALYPSIYLNTQQSPVAATLYVRNRVREAIRVSKIPDAKSPLPVFAYTRIVFTDQVLKFLSQDELVYTFGETVALGASGIVIWGTLSIMRSMKSCLLLDNYMETILNPYIINVTLAAKMCSQVLCQEQGVCIRKNWNSSDYLHLNPDNFAIQLEKGGKFTVRGKPTLEDLEQFSEKFYCSCYSTLSCKEKADVKDTDAVDVCIADGVCIDAFLKPPMETEEPQIFYNASPSTLSATMFIVSILFLIISSVASL
Protein: Vasopressin V2 receptor (V2R) (AVPR V2) (Antidiuretic hormone receptor) (Renal-type arginine vasopressin receptor) (O88721)
Organism: Mus musculus (Mouse)
Function: Receptor for arginine vasopressin. The activity of this receptor is mediated by G proteins which activate adenylate cyclase. Involved in renal water reabsorption (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P30518}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P30518}.
Interaction partners:
- Vasopressin-neurophysin 2-copeptin
- Beta-arrestin-1
- Guanine nucleotide-binding protein G
- Vasopressin V1a receptor
- Beta-arrestin-2
- Vasopressin V1b receptor
- Aquaporin-2
- Vomeronasal type-1 receptor 51
- Guanine nucleotide-binding protein subunit beta-4
- Guanine nucleotide-binding protein G
Sequence:
MILVSTTSAVPGALSSPSSPSNSSQEELLDDRDPLLVRAELALLSTIFVAVALSNGLVLGALIRRGRRGRWAPMHVFISHLCLADLAVALFQVLPQLAWDATDRFHGPDALCRAVKYLQMVGMYASSYMILAMTLDRHRAICRPMLAYRHGGGARWNRPVLVAWAFSLLLSLPQLFIFAQRDVGNGSGVFDCWARFAEPWGLRAYVTWIALMVFVAPALGIAACQVLIFREIHASLVPGPSERAGRRRRGHRTGSPSEGAHVSAAMAKTVRMTLVIVIVYVLCWAPFFLVQLWAAWDPEAPLERPPFVLLMLLASLNSCTNPWIYASFSSSVSSELRSLLCCAQRHTTHSLGPQDESCATASSSLMKDTPS
Protein: Ribosomal protein eL22-like (60S ribosomal protein L22-like 1) (Large ribosomal subunit protein eL22-like 1) (Q6P5R6)
Organism: Homo sapiens (Human)
Interaction partners:
- Ubiquitin-like protein FUBI
- Small ribosomal subunit protein eS24
- Large ribosomal subunit protein eL14
- Large ribosomal subunit protein eL31
- Small ribosomal subunit protein eS8
- Large ribosomal subunit protein eL43
- Large ribosomal subunit protein eL30
- Large ribosomal subunit protein eL6
- Large ribosomal subunit protein uL15
- Large ribosomal subunit protein eL38
Sequence:
MAPQKDRKPKRSTWRFNLDLTHPVEDGIFDSGNFEQFLREKVKVNGKTGNLGNVVHIERFKNKITVVSEKQFSKRYLKYLTKKYLKKNNLRDWLRVVASDKETYELRYFQISQDEDESESED
Protein: Eukaryotic translation initiation factor 2 subunit 2 (Eukaryotic translation initiation factor 2 subunit beta) (eIF2-beta) (Q99L45)
Organism: Mus musculus (Mouse)
Function: eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form a 43S preinitiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by eIF-2B (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P56329}.
Interaction partners:
- Eukaryotic translation initiation factor 2 subunit 1
- Eukaryotic translation initiation factor 5
- Translation initiation factor eIF2B subunit epsilon
- Translation initiation factor eIF2B subunit gamma
- Eukaryotic translation initiation factor 2 subunit 3, X-linked
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 2 subunit 3, Y-linked
- Translation initiation factor eIF2B subunit alpha
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 3 subunit A
Sequence:
MSGDEMIFDPTMSKKKKKKKKPFMLDEEGDAQTEETQPSETKEVEPEPTEEKDVDADEEDSRKKDASDDLDDLNFFNQKKKKKKTKKIFDIDEAEEAIKDVKIESDAQEPAEPEDDLDIMLGNKKKKKKNVKFPEEDEILEKDEALEDEDSKKDDGISFSSQTAWAGSERDYTYEELLNRVFNIMREKNPDMVAGEKRKFVMKPPQVVRVGTKKTSFVNFTDICKLLHRQPKHLLAFLLAELGTSGSIDGNNQLVIKGRFQQKQIENVLRRYIKEYVTCHTCRSPDTILQKDTRLYFLQCETCHSRCSVASIKTGFQAVTGKRAQLRAKAN
Protein: Gamma-butyrobetaine dioxygenase (EC 1.14.11.1) (Gamma-butyrobetaine hydroxylase) (Gamma-BBH) (Gamma-butyrobetaine,2-oxoglutarate dioxygenase) (Q9QZU7)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the formation of L-carnitine from gamma-butyrobetaine.
Subcellular location: Cytoplasm.
Interaction partners:
- 4-trimethylaminobutyraldehyde dehydrogenase
- Aldehyde dehydrogenase family 3 member A2
- Aldehyde dehydrogenase X, mitochondrial
- Alpha-aminoadipic semialdehyde dehydrogenase
- Aldehyde dehydrogenase, mitochondrial
Sequence:
MHCAILKAEAVDGARLMQIFWHDGAESLYPAVWLRDNCQCSDCYLHSAKARKLLLEALDVNIRMDDLTFDQKKVYITWPNGHYSEFEANWLKKRCFSQEARAGLQGELFLPECQYWGSELQLPTLNFEDVLNDDDHAYKWLSSLKKVGIVRLTGAADKRGEIIKLGKRIGFLYLTFYGHTWQVQDKIDANNVAYTTGKLSFHTDYPALHHPPGVQLLHCIKQTVTGGDSEIVDGFNVCQKLKEKNPQAFSILSSTFVDFTDIGVDYCDFSVQSKHKIIELDDKGQVVRINFNNATRDTVFDVPIERVQPFYAALKEFVDLMNSKEYKYTFKMNPGDVITFDNWRLLHGRRSYEAGTEISRHLEGAYADWDVVMSRLRILRQRVMNGN
Protein: Histone H2A.Z (Q12692)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Variant histone H2A which can replace H2A in some nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. This variant is enriched at promoters, it may keep them in a repressed state until the appropriate activation signal is received. Near telomeres, it may counteract gene silencing caused by the spread of heterochromatin proteins. Required for the RNA polymerase II and SPT15/TBP recruitment to the target genes. Involved in chromosome stability. Required to target MPS3 to the inner membrane of the nuclear envelope.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}. Chromosome {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Histone H2B.1
- Histone H2B.2
- Histone H3
- Histone H2A.Z-specific chaperone CHZ1
- Vacuolar protein sorting-associated protein 72
- Histone H4
- Helicase SWR1
- Nucleosome assembly protein
- Non-histone chromosomal protein 6A
- Histone H1
Sequence:
MSGKAHGGKGKSGAKDSGSLRSQSSSARAGLQFPVGRIKRYLKRHATGRTRVGSKAAIYLTAVLEYLTAEVLELAGNAAKDLKVKRITPRHLQLAIRGDDELDSLIRATIASGGVLPHINKALLLKVEKKGSKK
Protein: Spore coat protein GerQ (P39620)
Organism: Bacillus subtilis (strain 168)
Function: Essential for the localization of CwlJ in the spore coat and for spore germination triggered by calcium and dipicolinic acid (DPA). Its assembly into the spore coat is dependent on the coat morphogenetic proteins CotE and SpoIVA.
Subcellular location: Spore coat {ECO:0000269|PubMed:12644503, ECO:0000269|PubMed:16936016, ECO:0000269|PubMed:19933362}.
Interaction partners:
- Cell wall hydrolase CwlJ
- Spore coat protein E
- Sporulation-specific transcriptional regulator GerR
- Protein-glutamine gamma-glutamyltransferase
- Stage VI sporulation protein D
- SpoIVD-associated factor A
- Protein CotJC
- Small, acid-soluble spore protein B
- Protein CotJA
- Stage IV sporulation protein A
Sequence:
MKPKKNQYQQMQAFDNMQGYQPQFGANPYPQQGQGSQMQTMGMQPMMPMQQGQQGQQGQQGFGFPGQQQGGGFQIPSGPTPSGPGQSVPGMLPVEESYIENILRLNRGKTATIYMTFENSKEWGSKIFRGVIEAAGRDHIIISDPKSGTRYLLLTIYLDYITFDEEIAYTYPYSMASYSPR
Protein: Multifunctional CCA protein [Includes: CCA-adding enzyme (EC 2.7.7.72) (CCA tRNA nucleotidyltransferase) (tRNA CCA-pyrophosphorylase) (tRNA adenylyl-/cytidylyl-transferase) (tRNA nucleotidyltransferase) (tRNA-NT); 2'-nucleotidase (EC 3.1.3.-); 2',3'-cyclic phosphodiesterase (EC 3.1.4.-); Phosphatase (EC 3.1.3.-)] (P06961)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. Also shows highest phosphatase activity in the presence of Ni(2+) and hydrolyzes pyrophosphate, canonical 5'-nucleoside tri- and diphosphates, NADP, and 2'-AMP with the production of Pi. Displays a metal-independent phosphodiesterase activity toward 2',3'-cAMP, 2',3'-cGMP, and 2',3'-cCMP. Without metal or in the presence of Mg(2+), this protein hydrolyzes 2',3'-cyclic substrates with the formation of 2'-nucleotides, whereas in the presence of Ni(2+), it also produces some 3'-nucleotides. These phosphohydrolase activities are probably involved in the repair of the tRNA 3'-CCA terminus degraded by intracellular RNases.
Interaction partners:
- Uncharacterized protein YgiM
- Ribonuclease T
- 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase
- RNA-splicing ligase RtcB
- Methylglyoxal synthase
- Stringent starvation protein B
- 4-hydroxy-tetrahydrodipicolinate reductase
Sequence:
MKIYLVGGAVRDALLGLPVKDRDWVVVGSTPQEMLDAGYQQVGRDFPVFLHPQTHEEYALARTERKSGSGYTGFTCYAAPDVTLEDDLKRRDLTINALAQDDNGEIIDPYNGLGDLQNRLLRHVSPAFGEDPLRVLRVARFAARYAHLGFRIADETLALMREMTHAGELEHLTPERVWKETESALTTRNPQVFFQVLRDCGALRVLFPEIDALFGVPAPAKWHPEIDTGIHTLMTLSMAAMLSPQVDVRFATLCHDLGKGLTPPELWPRHHGHGPAGVKLVEQLCQRLRVPNEIRDLARLVAEFHDLIHTFPMLNPKTIVKLFDSIDAWRKPQRVEQLALTSEADVRGRTGFESADYPQGRWLREAWEVAQSVPTKAVVEAGFKGVEIREELTRRRIAAVASWKEQRCPKPE
Protein: Transcription factor bHLH79 (Basic helix-loop-helix protein 79) (AtbHLH79) (bHLH 79) (Transcription factor EN 81) (bHLH transcription factor bHLH079) (Q9LV17)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Transcription factor bHLH147
- Transcription factor GTE2
- Transcription factor bHLH117
- L-type lectin-domain containing receptor kinase VIII.2
- Transcription factor bHLH93
- Transcription factor bHLH30
Sequence:
MDPPLVNDSSFSAANPSSYTLSEIWPFPVNDAVRSGLRLAVNSGRVFTRSEHSGNKDVSAAEESTVTDLTAGWGSRKTRDLNSEDDSSKMVSSSSSGNELKESGDKKRKLCGSESGNGDGSMRPEGETSSGGGGSKATEQKNKPEPPKDYIHVRARRGQATDRHSLAERARREKISEKMTALQDIIPGCNKIIGKALVLDEIINYIQSLQRQVEFLSMKLEVVNSGASTGPTIGVFPSGDLGTLPIDVHRTIYEQQEANETRVSQPEWLHMQVDGNFNRTT
Protein: Uncharacterized protein C13E7.11 (O14364)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Rhomboid-type serine protease 2
- Mitochondrial inner membrane m-AAA protease component yta12
- Uncharacterized protein C18B11.08c
- Large ribosomal subunit protein uL30C
- Transmembrane GTPase fzo1
- Amino-acid permease 1
- Pyridoxal phosphate homeostasis protein
- Uncharacterized protein C56F8.13
- Uncharacterized protein C56F8.15
- Putative uncharacterized transmembrane protein SPBC713.13.
Sequence:
MNRLNFQSLLWKFGQKRFYYRPWIRIENIKPTPLWKPITFAVGVGSATFYTANYLDKRRKNYPKSSYGFPIPQTSSRSLVLSIIGINVGVFALWRAPRFSHLNRFLQKYAVMNPIFINMPSMIVSAFSHQSGWHLLFNMVAFYSFAPAIVDVFGNNQFVAFYISSILFSNVASLLHHRLRFGTKVTPGSLGASGAIYAIAAATSYFFPNASVSIIFLPFIPIKIGVALLGLMAFDAWGLISRGFSSFANFTLIDHAAHLGGGIFGWLYAKYGYSTYNRSTRPRPPSLSKPFFSRSVSF
Protein: Anon1A3 (Q9U4Q7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
GVENLPSVAEAKQNHVDEVKPISEEPGNSSEEVPKAEEPLKSSGETSENGAATETAAAPKEPASVMDVDEDETLVENTPSANKEKALDDEKEPEQKSEEHAASVLESKEQNEPAKEPTPEPMEVDGSSKGSSDTAQVDTPAIENVSAAPETEAAAKTTESSNDVVEVATEGKETVLEVPAAEPKEAESTVESAEELTETSTVVVTEPKEAASSEEEPSKVVDSAEPKEAESNTDESATPVPIDVSTAPASNDVSKPLEIDTTLVKTADSPAKEPQEICEVKKAEINVNGEPKIVNSSAEVGENAAPKVCN
Protein: Tyrosine-protein phosphatase non-receptor type 3 (EC 3.1.3.48) (Protein-tyrosine phosphatase H1) (PTP-H1) (P26045)
Organism: Homo sapiens (Human)
Function: May act at junctions between the membrane and the cytoskeleton. Possesses tyrosine phosphatase activity.
Subcellular location: Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton.
Interaction partners:
- Mitogen-activated protein kinase 12
- 6-pyruvoyl tetrahydrobiopterin synthase
- Transitional endoplasmic reticulum ATPase
- Epidermal growth factor receptor substrate 15
Sequence:
MTSRLRALGGRINNIRTSELPKEKTRSEVICSIHFLDGVVQTFKVTKQDTGQVLLDMVHNHLGVTEKEYFGLQHDDDSVDSPRWLEASKAIRKQLKGGFPCTLHFRVRFFIPDPNTLQQEQTRHLYFLQLKMDICEGRLTCPLNSAVVLASYAVQSHFGDYNSSIHHPGYLSDSHFIPDQNEDFLTKVESLHEQHSGLKQSEAESCYINIARTLDFYGVELHSGRDLHNLDLMIGIASAGVAVYRKYICTSFYPWVNILKISFKRKKFFIHQRQKQAESREHIVAFNMLNYRSCKNLWKSCVEHHTFFQAKKLLPQEKNVLSQYWTMGSRNTKKSVNNQYCKKVIGGMVWNPAMRRSLSVEHLETKSLPSRSPPITPNWRSPRLRHEIRKPRHSSADNLANEMTYITETEDVFYTYKGSLAPQDSDSEVSQNRSPHQESLSENNPAQSYLTQKSSSSVSPSSNAPGSCSPDGVDQQLLDDFHRVTKGGSTEDASQYYCDKNDNGDSYLVLIRITPDEDGKFGFNLKGGVDQKMPLVVSRINPESPADTCIPKLNEGDQIVLINGRDISEHTHDQVVMFIKASRESHSRELALVIRRRAVRSFADFKSEDELNQLFPEAIFPMCPEGGDTLEGSMAQLKKGLESGTVLIQFEQLYRKKPGLAITFAKLPQNLDKNRYKDVLPYDTTRVLLQGNEDYINASYVNMEIPAANLVNKYIATQGPLPHTCAQFWQVVWDQKLSLIVMLTTLTERGRTKCHQYWPDPPDVMNHGGFHIQCQSEDCTIAYVSREMLVTNTQTGEEHTVTHLQYVAWPDHGVPDDSSDFLEFVNYVRSLRVDSEPVLVHCSAGIGRTGVLVTMETAMCLTERNLPIYPLDIVRKMRDQRAMMVQTSSQYKFVCEAILRVYEEGLVQMLDPS
Protein: Uncharacterized hydrolase C9G1.08c (EC 3.1.-.-) (O14304)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Acyl-protein thioesterase 1
- NADPH--cytochrome P450 reductase
Sequence:
MSSLNSVLPSNACAEIIEGKDKVHNVVILMHGLGDSHKSFANMAKNVPLPNTSYISLRGPYRLPLDFENPGGNWMWGEDVHFDQNGELQSEADFSKSFTMISNLIGNLLSYGILSSRIFFFGFGQGAMVALYSCYKLSTKYQLGGIFSFGGTLPLSITLPNHPFHVPVYLFEKRLHCSCSEYEESRLRKTFKPFHLTCWNRDDKTDMPSSPREWYTFVQSISKHLYIHNTLFEDAIPLTSF