wanglab/gogpt-training-data huggingface dataset:
Protein: Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 3 (Oligosaccharyl transferase 34 kDa subunit) (Oligosaccharyl transferase subunit OST3) (Oligosaccharyl transferase subunit gamma) (Q8TFH3)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Uncharacterized protein C553.06
- Probable dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit ost2
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit stt3
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit wbp1
- Probable mannosyl-oligosaccharide glucosidase
- Dol-P-Glc:Glc
- Protein transport protein sec61 subunit beta
- Protein transport protein sec61 subunit alpha
- DnaJ-related protein spj1
Sequence:
MNFFKILSFFSLFVITCFAKLDLNSKTDADGVIQITGRLFHRIVNGKQDFTTVALFSADSSTMNCDVCRLIEPEFKALANSYKLKYGLDSGIRFTYADFGKNKNLFQDFSIESVPNFWIFKPKSIQAIHVDLSHGVTASHLAAIVEKHTGKIADIVYKQDQAKRVGAFLSYIIVGAALFFTRKIIVKIFTSRKVWAALTIITVITLSSGYMFTRIRFSPYSQRGEHGENLWLAGSQQFQFGAEVQVVSLLYTALTMSSIFLAIVAPKVEGAKRQTLFVIIWLAFLWIGYSFLVDIFKRKVSMYPFKLLI
Protein: Protein sip5 (O74775)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: May negatively regulate the snf1 kinase.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Ubiquitin-conjugating enzyme spm2
- Transcription initiation factor IIF subunit beta
- Ubiquitin-conjugating enzyme E2 13
- CUE domain-containing protein 4
Sequence:
MGNTIGKERQENDEELIQHLVQLVDGGFLDPQGVYSSAPAYKTNIVRKLMLERRLMPFYKGLDSYSKDWPADKVVEVVEKALGPHKSALLHCAIRQSRSLSVGNTRSLKRDSRGSSDHLLTRNRSNSTPGSISADYRTTAITTIYANAMECPICFLYYPSNFNYTRCCAQPICSECFVEIRRAEPHLPTVHANEPTPNEFDLISEPAKCPYCMTERFGVIYKPNPKLTPFSFNNNPDTLPSNIAPMGTLSKSSLPLHHIPWPPNQHIKFAHDDKNVVSTDFIHPDWQYKLERARRRALRRAANATLLNSHLLETGPANANANHNTDLSHDPTSHGGPRRTLSSRRQHYLANVEQLMLAEAIRQSLLDAQSNDSTNSLPSTEVSQPDSTNISNEQEIVQPQPTHTTNVALVEEINRPDSVESAITASSSIDTGNENETQEVNSDSLPQFVHQTMTQTNFQESSPSVAADETRVHNVDEYIEQQDLDELIHSPIASTNPFLADQFARSETVDLNAHICSPALSVSDDGVTATNKTQSSFPSVYEHQLKSNELERGH
Protein: Pannexin-3 (P60572)
Organism: Rattus norvegicus (Rat)
Function: Structural component of the gap junctions and the hemichannels.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q8CEG0}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00351}. Cell junction, gap junction {ECO:0000250|UniProtKB:Q8CEG0}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8CEG0}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00351}.
Interaction partners:
Sequence:
MSLAHTAAEYMLSDALLPDRRGSRLKGLRLELPLDKMVKFVTVGFPLLLMSLAFAQEFSSGSPISCFSPSNFSVRQAVFVDSSCWDSLAHYKQDEAGQYTVKSLWPHKALPYSLLALAVAMYLPVLLWQYAAVPALSSDLLFIISELDKSYNRSIRLVQHMLKIRQKSSDPHVFWDELEKARKERYFEFPLLERYLACKQRSHWLVATYLLRNALLLLFTSATYLYLGHFHLDVFFQEEFSCSIKTGLLHEETHVPELITCRLTSLSVFQIVSVSSVAIYTVLVPVIIYNLTRLCRWDKRLLSIYEMLPAFDLLSRKMLGCPINDLNVILLFLRANISELISFSWLSVLCVLKDTTTQKHNIDTVVDFMTLLAGLEPSKPKHLTQHTYDEHP
Protein: Hydroxyacylglutathione hydrolase cytoplasmic (EC 3.1.2.6) (Glyoxalase II) (Glx II) (O24496)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Subcellular location: Cytoplasm.
Interaction partners:
- Lactoylglutathione lyase GLX1
- Lactoylglutathione lyase
- Probable lactoylglutathione lyase, chloroplastic
- Protein DJ-1 homolog D
- DJ-1 protein homolog F
- DJ-1 protein homolog E
- D-lactate dehydrogenase [cytochrome], mitochondrial
- Protein DJ-1 homolog B
- Monodehydroascorbate reductase 3
- Protein DJ-1 homolog A
Sequence:
MKIFHVPCLQDNYSYLIIDESTGDAAVVDPVDPEKVIASAEKHQAKIKFVLTTHHHWDHAGGNEKIKQLVPDIKVYGGSLDKVKGCTDAVDNGDKLTLGQDINILALHTPCHTKGHISYYVNGKEGENPAVFTGDTLFVAGCGKFFEGTAEQMYQSLCVTLAALPKPTQVYCGHEYTVKNLEFALTVEPNNGKIQQKLAWARQQRQADLPTIPSTLEEELETNPFMRVDKPEIQEKLGCKSPIDTMREVRNKKDQWRG
Protein: Zinc finger protein ZFPM2 (Friend of GATA protein 2) (FOG-2) (Friend of GATA 2) (mFOG-2) (Zinc finger protein multitype 2) (Q8CCH7)
Organism: Mus musculus (Mouse)
Function: Transcription regulator that plays a central role in heart morphogenesis and development of coronary vessels from epicardium, by regulating genes that are essential during cardiogenesis. Essential cofactor that acts via the formation of a heterodimer with transcription factors of the GATA family GATA4, GATA5 and GATA6. Such heterodimer can both activate or repress transcriptional activity, depending on the cell and promoter context. Also required in gonadal differentiation, possibly be regulating expression of SRY. Probably acts a corepressor of NR2F2.
Subcellular location: Nucleus {ECO:0000269|PubMed:10330188, ECO:0000269|PubMed:9927674, ECO:0000269|PubMed:9927675}.
Interaction partners:
- Transcription factor GATA-4
- Phosphatidylinositol 3-kinase regulatory subunit alpha
- Transcription factor GATA-6
- Erythroid transcription factor
- Transcription factor GATA-5
- Wilms tumor protein homolog
- Steroidogenic factor 1
Sequence:
MSRRKQSKPRQIKRPLEDAIDDEEEECPVEEAEVISKGDFPLEGSFPAGFEPENLSCEDVEFFCNKGDDEGIQEPAESDGDSHSDKPGQPGVETDDWDGPGELEVFQRDGERKIQSRQQLPVGTTWGPFAGKMDLNNNSLKTKAQVPMVLTAGPKWLLDVTWQGVEDSKNNCIVYSKGGQLWCTTTKAISEGEELVAFVVDFDSRLQAASHMTLTEGMYPARLLDSIQLLPQQAAMASILPTAIVNKDIFPCKSCGIWYRSERNLQAHLMYYCSGRQREAAPVSEENEDNSHQVSSLCPFPQCTKSFSNARALEMHLNSHSGVKMEEFLPPGASLKCTVCSYTADSVINFHQHLFSHLTQAAFRCNHCHFGFQTQRELLQHQELHVPSGKLPRESDMEHSPSGTEDSLQPATDLLARSDLSQSQKAMPTKDASSDTELDKCEKKTQLFLTNQRPEIQPAANKQNFSYTKIKSEPSSPRLASSPVQPNIGPSFPVGPFLSQFAFPQDITMVPQASEILAKMSELVHRRLRHGSSSYPPVIYSPLMPKGATCFECNITFNNLDNYLVHKKHYCSSRWQQMAKSPEFPSVSEKMPEAVSPNTGQTSINLLNPAAHSSDPENPLLQTSCINSSTVLDLIGPNGKGHEKDFSTQVKKLPTSNSSDDKINGKPVDVKNPSGPLVDGESDPNKTTCEACNITFSRHETYMVHKQYYCATRHDPPLKRSASNKVPAMQRTMRTRKRRKMYEMCLPEQEQRPPLVQQRFLDVANLSNPCSSTQEPTEGLGECYHPRCDIFPGIVSKHLETSLAMNKCVPVPKCDTTHSNVSCLEMDVPIDLSKKCLSQSERTTASPKRLLDYHECTVCKISFNKVENYLAHKQNFCPVTAHQRNDLGQLDGKVFPNPESERSSPEVSFERNMIKCEKNGNPKQPSPNGNLFSSHLATLQGLKVFSEAAQLIATKEENKHLFLPQCLYPGAIKKTKGADQLSPYYGIKPSDYIASSLVIHNTDVEQSTNTENESPKGQASSNGCAVPKKDSLPLLPKNRGMVIVNGGLKQDERPTANPQQENISQNTQHEDGHKSPSWISENPLAANENVSPGIPCAEEQLSSIAKGVNGASQAPSSGKYCRLCDIQFNNLSNFITHKKFYCSSHAAEHVK
Protein: Ribokinase (RK) (EC 2.7.1.15) (Q387E8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03215}. Nucleus {ECO:0000256|HAMAP-Rule:MF_03215}.
Interaction partners:
- deoxyribose-phosphate aldolase
- Transketolase
- ribose-phosphate diphosphokinase
- ribose-phosphate diphosphokinase
- ribose-phosphate diphosphokinase
- Ribose 5-phosphate isomerase, putative
- Ribose-phosphate pyrophosphokinase, putative
- Bifunctional dihydrofolate reductase-thymidylate synthase
Sequence:
MSAAGVKSGNGCIADTPIVVVGACFVDYVAYVDHLPQVGESLRCRSFSKGFGGKGSNQAVCAGRLGASVSMVGAVGTDGDGADYIANFQRNGVQVSNVYRMENTSTGLAMIFVDSTTSHNEIVFSPNATGALTVDYLRKQSDNYNNFFGPKCRYIILQNEIPVETTLDVLKEAHTRGIYTVFNAAPAPSADEVAVVKPFLSYVSLFCVNEVEASMITGIDVKDTQSAILATEEMQKLGAHSVVTTLGGNGYVIGEKGKPPRHLPSITVKAVDSTGAGDCFVGAMVFYLSMGKSLEESCKRANMIAAISVQRPGTQSSYPTLDELPAEVKECKI
Protein: DNA gyrase subunit A (EC 5.6.2.2) (P48354)
Organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis)
Function: A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01897}.
Interaction partners:
- DNA gyrase subunit B
- DNA gyrase subunit B
- Topoisomerase subunit TopoN
- DNA-directed RNA polymerase subunit beta
- Enoyl-[acyl-carrier-protein] reductase
- Small ribosomal subunit protein uS12
- DNA-directed RNA polymerase subunit beta'
- DNA-directed RNA polymerase subunit alpha
- Beta sliding clamp
- Protein RecA
Sequence:
MTDTTLPPEGEAHDRIEPVDIQQEMQRSYIDYAMSVIVGRALPEVRDGLKPVHRRVLYAMYDSGFRPDRSHAKSARSVAETMGNYHPHGDASIYDTLVRMAQPWSLRYPLVDGQGNFGSPGNDPPAAMRYTEARLTPLAMEMLREIDEETVDFIPNYDGRVQEPTVLPSRFPNLLANGSGGIAVGMATNIPPHNLGELAEAVYWCLENYEADEEATCEAVMERVKGPDFPTSGLIVGTQGIEDTYKTGRGSIKMRGVVEIEEDSRGRTSIVITELPYQVNHDNFITSIAEQVRDGKLAGISNIEDQSSDRVGLRIVVELKRDAVAKVVLNNLYKHTQLQTSFGANMLSIVDGVPRTLRLDQLIRLYVDHQLDVIVRRTRYRLRKANERAHILRGLVKALDALDEVIALIRASQTVDIARAGLIELLDIDDIQAQAILDMQLRRLAALERQKIVDDLAKIEAEIADLEDILAKPERQRGIVRDELKEIVDKHGDARRTRIVPADGEVSDEDLIAREDVVVTITETGYAKRTKTDLYRSQKRGGKGVQGAGLKQDDMVNHFFVCSTHDWILFFTTQGRVYRAKAYELPEASRTARGQHVANLLAFQPEERIAQVIQIKSYEDAPYLVLATRNGLVKKSKLSDFDSNRSGGIVAINLREGDELVGAVLCSAEDDLLLVSANGQSIRFSATDEALRPMGRATSGVQGMRFNEDDRLLSLNVVRPDTYLLVATSGGYAKRTSIDEYSVQGRGGKGILTIQYDRKRGSLVGALIVDDDTELYAITSTGGVIRTAARQVRKAGRQTKGVRLMNLAEGDTLIAIARNADEDEAAESISESDADTAESPEA
Protein: Tyrosine-protein kinase Mer (EC 2.7.10.1) (Proto-oncogene c-Mer) (Receptor tyrosine kinase MerTK) (Q12866)
Organism: Homo sapiens (Human)
Function: Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to several ligands including LGALS3, TUB, TULP1 or GAS6. Regulates many physiological processes including cell survival, migration, differentiation, and phagocytosis of apoptotic cells (efferocytosis). Ligand binding at the cell surface induces autophosphorylation of MERTK on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with GRB2 or PLCG2 and induces phosphorylation of MAPK1, MAPK2, FAK/PTK2 or RAC1. MERTK signaling plays a role in various processes such as macrophage clearance of apoptotic cells, platelet aggregation, cytoskeleton reorganization and engulfment. Functions in the retinal pigment epithelium (RPE) as a regulator of rod outer segments fragments phagocytosis. Also plays an important role in inhibition of Toll-like receptors (TLRs)-mediated innate immune response by activating STAT1, which selectively induces production of suppressors of cytokine signaling SOCS1 and SOCS3.
Subcellular location: Cell membrane {ECO:0000269|PubMed:32640697}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Vitamin K-dependent protein S
- Growth arrest-specific protein 6
- Tubby-related protein 1
- Galectin-3
- Retinoid isomerohydrolase
- Guanylyl cyclase-activating protein 2
- Lactadherin
- Multiple epidermal growth factor-like domains protein 10
- Lecithin retinol acyltransferase
- Retinol dehydrogenase 12
Sequence:
MGPAPLPLLLGLFLPALWRRAITEAREEAKPYPLFPGPFPGSLQTDHTPLLSLPHASGYQPALMFSPTQPGRPHTGNVAIPQVTSVESKPLPPLAFKHTVGHIILSEHKGVKFNCSISVPNIYQDTTISWWKDGKELLGAHHAITQFYPDDEVTAIIASFSITSVQRSDNGSYICKMKINNEEIVSDPIYIEVQGLPHFTKQPESMNVTRNTAFNLTCQAVGPPEPVNIFWVQNSSRVNEQPEKSPSVLTVPGLTEMAVFSCEAHNDKGLTVSKGVQINIKAIPSPPTEVSIRNSTAHSILISWVPGFDGYSPFRNCSIQVKEADPLSNGSVMIFNTSALPHLYQIKQLQALANYSIGVSCMNEIGWSAVSPWILASTTEGAPSVAPLNVTVFLNESSDNVDIRWMKPPTKQQDGELVGYRISHVWQSAGISKELLEEVGQNGSRARISVQVHNATCTVRIAAVTRGGVGPFSDPVKIFIPAHGWVDYAPSSTPAPGNADPVLIIFGCFCGFILIGLILYISLAIRKRVQETKFGNAFTEEDSELVVNYIAKKSFCRRAIELTLHSLGVSEELQNKLEDVVIDRNLLILGKILGEGEFGSVMEGNLKQEDGTSLKVAVKTMKLDNSSQREIEEFLSEAACMKDFSHPNVIRLLGVCIEMSSQGIPKPMVILPFMKYGDLHTYLLYSRLETGPKHIPLQTLLKFMVDIALGMEYLSNRNFLHRDLAARNCMLRDDMTVCVADFGLSKKIYSGDYYRQGRIAKMPVKWIAIESLADRVYTSKSDVWAFGVTMWEIATRGMTPYPGVQNHEMYDYLLHGHRLKQPEDCLDELYEIMYSCWRTDPLDRPTFSVLRLQLEKLLESLPDVRNQADVIYVNTQLLESSEGLAQGSTLAPLDLNIDPDSIIASCTPRAAISVVTAEVHDSKPHEGRYILNGGSEEWEDLTSAPSAAVTAEKNSVLPGERLVRNGVSWSHSSMLPLGSSLPDELLFADDSSEGSEVLM
Protein: L-2-hydroxyglutarate dehydrogenase (L2HG dehydrogenase) (EC 1.1.5.13) (L2HG:quinone oxidoreductase) (P37339)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the dehydrogenation of L-2-hydroxyglutarate (L2HG) to alpha-ketoglutarate and couples to the respiratory chain by feeding electrons from the reaction into the membrane quinone pool. Functions in a L-lysine degradation pathway that proceeds via cadaverine, glutarate and L-2-hydroxyglutarate.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:30498244}.
Interaction partners:
- Glutarate 2-hydroxylase
- Succinate-semialdehyde dehydrogenase [NADP
- 4-aminobutyrate aminotransferase GabT
- HTH-type transcriptional repressor GlaR
- Gamma-aminobutyric acid permease
- Gamma-aminobutyraldehyde dehydrogenase
Sequence:
MYDFVIIGGGIIGMSTAMQLIDVYPDARIALLEKESAPACHQTGHNSGVIHAGVYYTPGSLKAQFCLAGNRATKAFCDQNGIRYDNCGKMLVATSDLEMERMRALWERTAANGIEREWLNADELREREPNITGLGGIFVPSSGIVSYRDVTAAMAKIFQSRGGEIIYNAEVSGLNEHKNGVVIRTRQGGEYEASTLISCSGLMADRLVKMLGLEPGFIICPFRGEYFRLAPEHNQIVNHLIYPIPDPAMPFLGVHLTRMIDGSVTVGPNAVLAFKREGYRKRDFSFSDTLEILGSSGIRRVLQNHLRSGLGEMKNSLCKSGYLRLVQKYCPRLSLSDLQPWPAGVRAQAVSPDGKLIDDFLFVTTPRTIHTCNAPSPAATSAIPIGAHIVSKVQTLLASQSNPGRTLRAARSVDALHAAFNQ
Protein: Protein phosphatase 1 regulatory subunit 1B (DARPP-32) (Dopamine- and cAMP-regulated neuronal phosphoprotein) (P07516)
Organism: Bos taurus (Bovine)
Function: Inhibitor of protein-phosphatase 1.
Subcellular location: Cytoplasm.
Interaction partners:
- Cyclin-dependent kinase 5
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit beta
- Serine/threonine-protein phosphatase PP1-beta catalytic subunit
- Protein phosphatase 3 catalytic subunit alpha
- Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
- Serine/threonine-protein phosphatase
- Serine/threonine-protein phosphatase
- Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
- Phosphodiesterase
Sequence:
MDPKDRKKIQFSVPAPPSQLDPRQVEMIRRRRPTPAMLFRLSEHSSPEEEASPHQRASGEGHHLKSKRSNPCAYTPPSLKAVQRIAESHLQSISNLGENQASEEEDELGELRELGYPREEEEEEEEEDEEEEEDSQAEVLKGSRGSAGQKTTYGQGLEGPWERPPPLDGPQRDGSSEDQVEDPALNEPGEEPQRPAHPEPGT
Protein: Na(+)-translocating NADH-quinone reductase subunit E (Na(+)-NQR subunit E) (Na(+)-translocating NQR subunit E) (EC 7.2.1.1) (NQR complex subunit E) (NQR-1 subunit E) (A5F5Y5)
Organism: Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)
Function: NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00429, ECO:0000305}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00429}.
Interaction partners:
Sequence:
MEHYISLLVKSIFIENMALSFFLGMCTFLAVSKKVKTSFGLGIAVIVVLTISVPVNNLVYNLVLKPDALVEGVDLSFLNFITFIGVIAALVQILEMILDRFFPPLYNALGIFLPLITVNCAIFGGVSFMVQRDYSFAESVVYGFGSGVGWMLAIVALAGIREKMKYSDVPPGLRGLGITFITAGLMALGFMSFSGVQL
Protein: Type 3 secretion system secretin (T3SS secretin) (P95431)
Organism: Pseudomonas aeruginosa
Subcellular location: Cell outer membrane {ECO:0000256|ARBA:ARBA00004442, ECO:0000256|HAMAP-Rule:MF_02219, ECO:0000256|RuleBase:RU004004}.
Interaction partners:
Sequence:
MRRLLIGGLLALLPGAVLRAQPLDWPSLPYDYVAQGESLRDVLANFGANYDASVIVSDKVNDQVSGRFDLESPQAFLQLMASLYNLGWYYDGTVLYVFKTTEMQSRLVRLEQVGEAELKRALTAAGIWEPRFGWRADPSGRLVHVSGPGRYLELVEQTAQVLEQQYTLRSEKTGDLSVEIFPLRYAVAEDRKIEYRDDEIEAPGIASILSRVLSDANVVAVGDEPGKLRPGPQSSHAVVQAEPSLNAVVVRDHKDRLPMYRRLIEALDRPSARIEVGLSIIDINAENLAQLGVDWSAGIRLGNNKSIQIRTTGQDSEEGGGAGNGAVGSLVDSRGLDFLLAKVTLLQSQGQAQIGSRPTLLTQENTQAVLDQSETYYVRVTGERVAELKAITYGTMLKMTPRVVTLGDTPEISLSLHIEDGSQKPNSAGLDKIPTINRTVIDTIARVGHGQSLLIGGIYRDELSQSQRKVPWLGDIPYLGALFRTTADTVRRSVRLFLIEPRLIDDGVGHYLALNNRRDLRGGLLEIDELSNQSLSLRKLLGSARCQALAPARAEQERLRQAGQGSFLTPCRMGAQEGWRVTDGACPKDGAWCVGAERGN
Protein: PHAF1 protein T01G9.2 (P34692)
Organism: Caenorhabditis elegans
Function: May play a regulatory role in autophagic activity.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9BSU1}. Preautophagosomal structure {ECO:0000250|UniProtKB:Q9BSU1}. Note=The BCAS3:PHAF1 complex is recruited to the preautophagosomal structures adjacent to the damaged mitochondria upon mitophagy in a PRKN-PINK1 dependent manner. {ECO:0000250|UniProtKB:Q9BSU1}.
Interaction partners:
- BCAS3 WD40 domain-containing protein
Sequence:
MNGKQQVTKKPSTEEDLSFTKFKVVPDVGLKSSQFEFVLGMPINQCIAMIQQHPRMLTKVELKYSKKDPFYQDIIIYIGSTGIRLYFDGLSQLIKLIEVDNLSMITLTYNDTIFSDPNNMATLDRVNEFFGSTHPGSYDDKHNIYVQSWPGLSFCFPYGGENSNLEVRPGFGGNLRSLKYDANSQPKLTKMSIYRGPNPSEPESVDTPFSCYCGQNRTRKVEAIWENGNIVGIDIQFDTQNGRIVDGEYDVSTYTRQIYFGDSVSDVQSILGAPTKVFYKSDDKMKIHRGLHKETLYGPPNFFFNYFVMGLDILFDFVSKRVVKFVLHTNAPGHCDFGMYSRCNFSIFLNDKQYEIRTDSKFDEFSHAFMNDSNPPRPVVLARQEQQPFGSTFCYGIKQIIVERTENGFLTSVTIYDGAKEK
Protein: Aspartate aminotransferase (EC 2.6.1.1) (F4I0D4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MNSILSSVLPAPEDPVLSVIFACRDDPSPVKLNLSAGTYRTEEGKPLVLDVVRRAEQQLANDLSRDKEYLPLNGLPEFNKLSTKLILGDDSPALKENRVVTTQCLSGTGSLRVGAEFLATHNKESVIFVPNPTWGNHPRIFTLAGLSVQYFRYYDPKSRGLDFKGMLEDLGAAPPGAIVVLQACAHNPTGVDPTFEQWEKIRRLVRSKSLLPFFDSAYQGFASGSLDADAQAVRMFVADGGECLIAQSYAKNMGLYGERIGSLTIVCTSEDVAKKVENQVLLVVRPMYLTPPIHGASIVATILKNSDMYNDWTIELKGMADRIISMRQQLYAALEARGTPGDWSHIIKHIGMFTFTGLSEEQVRLMAKEYHIYMTYDGRISMASLSSKTVPQLADAIHAVVTRIA
Protein: Bublin coiled-coil protein (UPF0184 protein C9orf16) (Q9BUW7)
Organism: Homo sapiens (Human)
Function: Essential for intermediate filament organization in intestinal cells, interacts with intermediate filament and regulates intestinal lumen morphology.
Subcellular location: Cell junction {ECO:0000269|PubMed:33857431}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:33857431}. Note=In the intestine, localizes subapically and at cell junctions. Interacts with intermediate filament (IF) proteins and localizes to the IF network in an IF-dependent manner (PubMed:33857431). In dividing cells, localizes to interpolar and kinetochore microtubules (PubMed:33857431). {ECO:0000269|PubMed:33857431}.
Interaction partners:
- V-type proton ATPase subunit D
Sequence:
MSGPNGDLGMPVEAGAEGEEDGFGEAEYAAINSMLDQINSCLDHLEEKNDHLHARLQELLESNRQTRLEFQQQLGEAPSDASP
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (F1MYJ4)
Organism: Bos taurus (Bovine)
Interaction partners:
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform
- Phosphatidylinositol 3-kinase regulatory subunit alpha
- PH domain leucine-rich repeat-containing protein phosphatase 2
- Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit gamma
- Forkhead box protein O1
- TSC complex subunit 2.
- non-specific serine/threonine protein kinase
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform
- protein-serine/threonine phosphatase
- Phosphatidylinositol 3-kinase regulatory subunit beta
Sequence:
MSDVTIVKEGWVQKRGEYIKNWRPRYFLLKTDGSFIGYKEKPQDVDLPYPLNNFSVAKCQLMKTERPKPNTFIIRCLQWTTVIERTFHVDTPEEREEWTEAIQAVADRLQRQEEERMNCSPTSQIDNIGEEEMDASTTHHKRKTMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTLFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRYFDEEFTAQTITITPPEKYDEDGMDCMDNERRPHFPQFSYSASGRE
Protein: Immunoglobulin heavy constant gamma 2C (F6TQW2)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
XKTTAPSVYPLAPVCGGTTGSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPALLQSGLYTLSSSVTVTSNTWPSQTITCNVAHPASSTKVDKKIEPRVPITQNPCPPLKECPPCAAPDLLGGPSVFIFPPKIKDVLMISLSPMVTCVVVDVSEDDPDVQISWFVNNVEVHTAQTQTHREDYNSTLRVVSALPIQHQDWMSGKEFKCKVNNRALPSPIEKTISKPRGPVRAPQVYVLPPPAEEMTKKEFSLTCMITGFLPAEIAVDWTSNGRTEQNYKNTATVLDSDGSYFMYSKLRVQKSTWERGSLFACSVVHEGLHNHLTTKTISRSLGLDLDDVCTEAQDGELDGLWTTITIFISLFLLSVCYSASVTLFKVKWIFSSVVELKQKISPDYRNMIGQGA
Protein: Arginine N-succinyltransferase subunit alpha (ARUAI) (EC 2.3.1.109) (AOST) (AST) (P80357)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Catalyzes the transfer of succinyl-CoA to arginine to produce N(2)-succinylarginine. Also acts on L-ornithine.
Interaction partners:
- N-succinylarginine dihydrolase
- N-succinylglutamate 5-semialdehyde dehydrogenase
- Arginine N-succinyltransferase subunit beta
- Succinylglutamate desuccinylase
- Succinylornithine transaminase/acetylornithine aminotransferase
- Arginine--pyruvate transaminase AruH
- Lysine decarboxylase LdcA
- Biosynthetic arginine decarboxylase
- Arginine/ornithine transport ATP-binding protein AotP
- HTH-type transcriptional regulator ArgR
Sequence:
MLVMRPAQAADLPQVQRLAADSPVGVTSLPDDAERLRDKILASEASFAAEVSYNGEESYFFVLEDSASGELVGCSAIVASAGFSEPFYSFRNETFVHASRSLSIHNKIHVLSLCHDLTGNSLLTSFYVQRDLVQSVYAELNSRGRLLFMASHPERFADAVVVEIVGYSDEQGESPFWNAVGRNFFDLNYIEAEKLSGLKSRTFLAELMPHYPIYVPLLPDAAQESMGQVHPRAQITFDILMREGFETDNYIDIFDGGPTLHARTSGIRSIAQSRVVPVKIGEAPKSGRPYLVTNGQLQDFRAVVLDLDWAPGKPVALSVEAAEALGVGEGASVRLVAV
Protein: L-alanine exporter AlaE (P64550)
Organism: Escherichia coli (strain K12)
Function: Exports L-alanine.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00914, ECO:0000269|PubMed:21531828}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00914, ECO:0000269|PubMed:21531828}.
Interaction partners:
- Inner membrane protein YtfF
- Leucine efflux protein
- Uncharacterized membrane protein YahN
- D-amino acid dehydrogenase
Sequence:
MFSPQSRLRHAVADTFAMVVYCSVVNMCIEVFLSGMSFEQSFYSRLVAIPVNILIAWPYGMYRDLFMRAARKVSPSGWIKNLADILAYVTFQSPVYVAILLVVGADWHQIMAAVSSNIVVSMLMGAVYGYFLDYCRRLFKVSRYQQVKA
Protein: Metal transporter CNNM2 (Ancient conserved domain-containing protein 2) (mACDP2) (Cyclin-M2) (Q3TWN3)
Organism: Mus musculus (Mouse)
Function: Divalent metal cation transporter. Mediates transport of divalent metal cations in an order of Mg(2+) > Co(2+) > Mn(2+) > Sr(2+) > Ba(2+) > Cu(2+) > Fe(2+).
Subcellular location: Cell membrane {ECO:0000269|PubMed:22399287}; Multi-pass membrane protein {ECO:0000269|PubMed:22399287}.
Interaction partners:
- Arsenite methyltransferase methyltransferase)
- Solute carrier family 41 member 1
- Transient receptor potential cation channel subfamily M member 6
- Solute carrier family 41 member 3
- Protein tyrosine phosphatase type IVA 2
Sequence:
MIGCGACEPEVKMAGGQAAAALPTWKMAARRSLSARGRGVLQAAAGRLLPLLLLSCCWGAGGCTAAGENEETVIIGLRLEDTNDVSFMEGGALRVSERTRVKLRVYGQNINNETWSRIAFTEHERRRHTPSERGLGGPAPPEPDSGPQRCGIRTSDIIILPHIILNRRTSGIIEIEIKPLRKMEKSKSYYLCTSLSTPALGAGGSGSASGTVGGKGGAGVAGLPPPPWAETTWIYHDGEDTKMIVGEEKKFLLPFWLQVIFISLLLCLSGMFSGLNLGLMALDPMELRIVQNCGTEKEKNYAKRIEPVRRQGNYLLCSLLLGNVLVNTTLTILLDDIAGSGLVAVVVSTIGIVIFGEIVPQAICSRHGLAVGANTIFLTKFFMMMTFPASYPVSKLLDCVLGQEIGTVYNREKLLEMLRVTDPYNDLVKEELNIIQGALELRTKTVEDVMTPLRDCFMITGEAILDFNTMSEIMESGYTRIPVFEGERSNIVDLLFVKDLAFVDPDDCTPLKTITKFYNHPLHFVFNDTKLDAMLEEFKKGKSHLAIVQRVNNEGEGDPFYEVLGIVTLEDVIEEIIKSEILDETDLYTDNRTKKKVAHRERKQDFSAFKQTDSEMKVKISPQLLLAMHRFLATEVEAFSPSQMSEKILLRLLKHPNVIQELKYDEKNKKAPECYLYQRNKPVDYFVLILQGKVEVEAGKEGMKFEASAFSYYGVMALTASPVPLSLSRTFVVSRTEVLAAGSPGENKSPPRPCGLNHSDSLSRSDRIDAMTPTLGSSNNQLSSSFLQVYIPDYSVRALSDLQFVKISRQQYQNALMASRMDKTPQSSDSENTKIELTLTELHDGLPDETANLLNEQNCVSHNKANHSLHSEGAI
Protein: Transmembrane protein (Q57XK0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSSCERLSPKQFHSQESRLYTEKCVRELMQTRAFRDYVGHLEYSERMQFSWFVALIGLALASYYHAIFMFPVNCGTYAGNFDEATPFFLVATLLMALFVAPSVMVAQISGFFEPISREEVSSLLTYITFVNAAVVSFGGSWLHNPPYIVSEPPVPWLSGTISQLDELATRTILRALPLHGIVVGSWLLYLWQSRGWRRVWKLPLPLLTAPVLLAVFTWFWFRVTSPICAQLLSSSTDALELVDVFFSASDEMIKSFSSIFSTPLRLGAFISPQDCCRLWCSTLAFSLLYFAGALAIPVIGGIAILISWVLPTHPTTWGLSFILSIAGLVMQVQRNESSVVALFALLVAIWALGRNGFSLMN