wanglab/gogpt-training-data huggingface dataset:
Protein: Soluble guanylate cyclase gcy-31 (EC 4.6.1.2) (Q86C56)
Organism: Caenorhabditis elegans
Function: Synthesizes cyclic GMP (cGMP) from GTP. May play a role in embryogenesis.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Soluble guanylate cyclase gcy-33
- FMRF-Like Peptide
- Cyclic nucleotide-gated channel
- Soluble guanylate cyclase gcy-34
- Cyclic nucleotide-binding domain-containing protein
- Soluble guanylate cyclase gcy-37
- Soluble guanylate cyclase gcy-36
Sequence:
MYGLIIDHIATYIKEKYGESTWSEVKFVSGVTDDTFQMDKKFSEGLSHKLIWACHDVTGDPVDELMTNIGTSFYKFLTKFEFNKVLRVLGRTFPQFLNGLDNLHEYLRFTFPKLKPPSFYCEHESRTGLTLHYRSKRRGFLHYVQGQIRNISQELFQTEVVIELLDIEHDLNLEHVIMRLHFNNLDFNRQGTAYRNLNDSILEKVKITSDIFFDIFPFIIVFNRGMRIRNIGIGLLRVMAGIVGKKINQTFLLMRPFIRFRWEEIMLHSNNIFELISSDPIQEDEDGILVYKTTDVDQMTEERHRMGDGEREKFLSLKGQMFYMEEWESICFVGIPVMSHLPQMYKSGLFINDFALHDSSRDLVLASTQQSAELKLLLHQEAQKSRNMRENMNRLKKERRRTDKLLYQMLPKSVANQLRHGESAVACCERFDSVTILFTDIVEFTKMCSSLTPLEVIEFLKVIYTNFDKIIDTHGVYKVETIGDAYMVVSGAPTKTEHDAEFILDCASQFLVEAGKMVNMNNKIHKIDIRAGVHSGSVVAGVVGLSMPRYCLFGETVYVANKMEQNSSPMKILVSETTHNKIEESDPGLYQFERREEIEIKDDQTIQTFFVVSRHGPHRVPSPRNCESRQDDSQTEDDDDDELLLPRKSGRKSPTSEAEEELKKKGQLSFTPVSDAGIECHSRNSNKTPRQSQDLTPRKSIT
Protein: Conserved oligomeric Golgi complex subunit 7 (COG complex subunit 7) (Complexed with DOR1 protein 5) (Component of oligomeric Golgi complex 7) (P53195)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acts as component of the peripheral membrane COG complex that is involved in intra-Golgi protein trafficking. COG is located at the cis-Golgi, and regulates tethering of retrograde intra-Golgi vesicles and possibly a number of other membrane trafficking events.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Conserved oligomeric Golgi complex subunit 5
- Conserved oligomeric Golgi complex subunit 8
- Conserved oligomeric Golgi complex subunit 6
- Conserved oligomeric Golgi complex subunit 1
- Conserved oligomeric Golgi complex subunit 4
- Conserved oligomeric Golgi complex subunit 3
- Conserved oligomeric Golgi complex subunit 2
- t-SNARE affecting a late Golgi compartment protein 2
- GTPase-activating protein GYP1
- ADP-ribosylation factor-like protein 1
Sequence:
MVELTITGDDDDILSMFFDEEFVPHAFVDILLSNALNEDQIQTQSVSSLLLTRLDFYTKNLTKELESTIWNLDKLSQTLPRTWASSRYHKEAEQNDSSLYSTESLKSSKLEYYLDTLASAVRALETGMHNVTEKLSDLDNENNRNTNVRQQLQSLMLIKERIEKVVYYLEQVRTVTNISTVRENNTTSTGTDLSITDFRTSLKALEDTIDESLSSAIDNEAKDETNKDLIGRIDSLSELKCLFKGLDKFFAEYSNFSESIKSKAQSYLSTKNIDDGMIS
Protein: Myelin basic protein (F8W4C1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Myelin membrane {ECO:0000256|ARBA:ARBA00004392}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004392}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004392}.
Interaction partners:
Sequence:
MASASSSQSTFRLGRTKKNPTVMDQIGKFFGGEKKKKGKGSFRGGLSSSPQRSSASPRRRPDENAVMHFLRTIVSPSTPKSRREQKSQSSTKGQKGRGESQGTLTRIFKMGGSQSASSSKR
Protein: Monocarboxylate transporter 8 (MCT 8) (Solute carrier family 16 member 2) (G8XYX6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Specific thyroid hormone transmembrane transporter, that mediates both uptake and efflux of thyroid hormones across the cell membrane independently of pH or a Na(+) gradient. The substrate preference is 3,3-diiodothyronine (3,3'-T2) and T3 and to a lesser extentd T4 and rT3. Acts as a crucial regulator during embryonic development.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P36021}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MHSESDDNTAGGTPGSEDPQAEESSSPAEEFEEQERKLAPEDSTVQLIHTGCTDKRPATPPGAHPGQGFVPPEGGFGWVVVFAATWCNGSIFGIQNSFGILHMMLVKHHEKQPDQASQFKVAWVGALAMGMIFFCSPVVSMFTDHFGCRKTAVCGAFVAFIGLLTSSFATTLGLWYFTYGILFGCGSSFAFQPSLVILGHYFRQRLGLANGVVTAGSSLFSMGLPVLLKKVVEPLGLPRTFQILSIFMLVQALLALAFKPLLPSGMCPMPGMALDGGPSTPESASRWQKGLAKIRRYFNVRVFSILTYRIWAFGVATAVLGYFVPYVHLLNFVKEQFGDTQREWLLLVCIGASSGVGRLLFGKIGDLIPGVKKIYMQVASFILLGVMSMMIPQCAVFEGLVVVFVLMGLCDGCFITIMAPIAFELVGPMQASQAIGYLLGLMAIPMTAGPPIAGLLHDHFGNYHVAFYLAGVPPIVGGIVMFFVPLVHQRMQKRRKETDDPSMDKMLKNCSNGDMLPGYTDMETHI
Protein: Interferon-induced GTP-binding protein Mx1 (H9KVC9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVVSEVDIAKADPAAASHPLLLNGDATVAQKNPGSVAENNLCSQYEEKVRPCIDLIDSLRALGVEQDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIVTRCPLVLKLKKLVNEDKWRGKVSYQDYEIEISDASEVEKEINKAQNAIAGEGMGISHELITLEISSRDVPDLTLIDLPGITRVAVGNQPADIGYKIKTL
Protein: Cytochrome P-450 monooxygenase DoxA (EC 1.14.13.181) (13-deoxycarminomycin C-13 hydroxylase) (13-deoxydaunorubicin C-13 hydroxylase) (13-dihydrocarminomycin C-13 hydroxylase) (13-dihydrodaunorubicin C-13 hydroxylase) (Q59971)
Organism: Streptomyces sp. (strain C5)
Function: Involved in the biosynthesis of the anthracyclines carminomycin and daunorubicin (daunomycin) which are aromatic polyketide antibiotics that exhibit high cytotoxicity and are widely applied in the chemotherapy of a variety of cancers. In vivo, DoxA catalyzes the C-13 hydroxylation of 13-deoxycarminomycin and 13-deoxydaunorubicin to yield 13-dihydrocarminomycin and 13-dihydrodaunorubicin, respectively, as well as the oxidation of these 13-dihydro-anthracyclines to their respective 13-keto forms, carminomycin and daunorubicin. In vitro, it also catalyzes the C-14 hydroxylation of daunorubicin to form doxorubicin (adriamycin), although this strain is not a doxorubicin producer. It is not able to accept anthracyclinones (aglycones) and anthracyclines with a 10-carbomethoxyl moiety. 13-oxidation of the anthracyclines possessing the 4-methoxy substitution is greatly favored. The anthracycline analog desacetyladriamycin can be oxidized to 10-hydroxydesacetyladriamycin. It can only use NADP. DoxA acts jointly with DauV.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
Sequence:
MSGEAPRVAVDPFSCPMMTMQRKPEVHDAFREAGPVVEVNAPAGGPAWVITDDALAREVLADPRFVKDPDLAPTAWRGVDDGLDIPVPELRPFTLIAVDGEDHRRLRRIHAPAFNPRRLAERTDRIAAIADRLLTELADSSDRSGEPAELIGGFAYHFPLLVICELLGVPVTDPAMAREAVGVLKALGLGGPQSAGGDGTDPAGDVPDTSALESLLLEAVHAARRKDTRTMTRVLYERAQAEFGSVSDDQLVYMITGLIFAGHDTTGSFLGFLLAEVLAGRLAADADGDAISRFVEEALRHHPPVPYTLWRFAATEVVIRGVRLPRGAPVLVDIEGTNTDGRHHDAPHAFHPDRPSRRRLTFGDGPHYCIGEQLAQLESRTMIGVLRSRFPQARLAVPYEELRWCRKGAQTARLTDLPVWLR
Protein: Glutathione S-transferase Mu 5 (EC 2.5.1.18) (GST class-mu 5) (GSTM5-5) (P46439)
Organism: Homo sapiens (Human)
Function: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
Subcellular location: Cytoplasm.
Interaction partners:
- Glutathione S-transferase Mu 3
- Glutathione S-transferase Mu 4
- Glutathione S-transferase Mu 2
- Phospholipid hydroperoxide glutathione peroxidase GPX4
- Maleylacetoacetate isomerase
- Epoxide hydrolase 1
- Peroxiredoxin-6
- Cytochrome P450 2E1
- Glutathione reductase, mitochondrial
- Cytochrome P450 1A1
Sequence:
MPMTLGYWDIRGLAHAIRLLLEYTDSSYVEKKYTLGDAPDYDRSQWLNEKFKLGLDFPNLPYLIDGAHKITQSNAILRYIARKHNLCGETEEEKIRVDILENQVMDNHMELVRLCYDPDFEKLKPKYLEELPEKLKLYSEFLGKRPWFAGDKITFVDFLAYDVLDMKRIFEPKCLDAFLNLKDFISRFEGLKKISAYMKSSQFLRGLLFGKSATWNSK
Protein: Homeobox protein Nkx-2.4 (Homeobox protein NK-2 homolog D) (Q9H2Z4)
Organism: Homo sapiens (Human)
Function: Probable transcription factor.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
Interaction partners:
- DCN1-like protein 1
Sequence:
MSLSPKHTTPFSVSDILSPIEETYKKFSGAMDGAPPGLGAPLGAAAAYRAPPPGPSSQAATVAGMQPSHAMAGHNAAAAAAAAAAAAAAAATYHMPPGVSQFPHGAMGSYCNGGLGNMGELPAYTDGMRGGAATGWYGANPDPRYSSISRFMGPSAGVNVAGMGSLTGIADAAKSLGPLHAAAAAAAPRRKRRVLFSQAQVYELERRFKQQKYLSAPEREHLASMIHLTPTQVKIWFQNHRYKMKRQAKDKAAQQLQQEGGLGPPPPPPPSPRRVAVPVLVKDGKPCQNGASTPTPGQAGPQPPAPTPAPELEELSPSPPALHGPGGGLAALDAAAGEYSGGVLGANLLYGRTW
Protein: 4-hydroxyproline epimerase (EC 5.1.1.8) (Hydroxyproline-2-epimerase) (HyPRE) (Q2YLF3)
Organism: Brucella abortus (strain 2308)
Function: Allows intracellular utilization of 4-hydroxyproline, one of the major constituents of host collagen, by converting 4-hydroxy-L-proline to 4-hydroxy-D-proline, which can be further metabolized by intracellular 4-hydroxy-D-proline oxidases. Strong B-cell mitogen. Plays an important role in the regulation of intra- and extracellular amino acid pools, allowing the bacterium to profit from host precursors and enzymatic pathways (By similarity). Directly involved in the immune regulation of host. Elicits B-lymphocyte polyclonal activation, resulting in early and transient nonresponsive immune condition of the host.
Interaction partners:
- NAD binding site:TrkA potassium uptake protein
Sequence:
MARHSFFCVDGHTCGNPVRLVAGGGPNLNGSTMMEKRAHFLAEYDWIRTGLMFEPRGHDMMSGSILYPPTRPDCDVAVLFIETSGCLPMCGHGTIGTVTMAIEQGLVTPKTPGKLNLDTPAGLVAIEYEQDGQYVERVRLTNVPAFLYAEGLEVECPDLGPIKVDVAYGGNFYAIVEPQENYTDMDDYSALQLIAWSPVLRQRLNEKYKFQHPELPDINRLSHILWTGKPKHPQAHARNAVFYGDKAIDRSPCGTGTSARMAQLAAKGKLKPCDEFIHESIIGSLFHGRVERAAEVAGRPAIVPSIAGWARMTGYNTIFIDDRDPFAHGFSMA
Protein: Beta-amyrin synthase 1 (Pgb-AS) (EC 5.4.99.39) (Oxidosqualene cyclase 1) (O82140)
Organism: Panax ginseng (Korean ginseng)
Function: Component of the oleanane-type triterpene saponins biosynthetic pathway. Oxidosqualene cyclase converting oxidosqualene into beta-amyrin, generating five rings and eight asymmetric centers in a single transformation.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P48449}; Peripheral membrane protein {ECO:0000250|UniProtKB:P48449}.
Interaction partners:
Sequence:
MWKLKIAEGNKNDPYLYSTNNFVGRQTWEFDPDYVASPGELEEVEQVRRQFWDNRYQVKPSGDLLWRMQFLREKNFRQTIPQVKVGDDEAVTYEAATTTLRRAVHFFSALQASDGHWPAENSGPLFFLPPLVMCVYITGHLDTVFPAEHRKEILRYIYCHQNEDGGWGLHIEGHSTMFCTTLSYICMRILGEGPDGGVNNACARGRKWILDHGSVTAIPSWGKTWLSILGVYEWIGSNPMPPEFWILPSFLPMHPAKMWCYCRMVYMPMSYLYGKRFVGPITPLILQLREELYGQPYNEINWRKTRRVCAKEDIYYPHPLIQDLLWDSLYVLTEPLLTRWPFNKLREKALQTTMKHIHYEDENSRYITIGCVEKVLCMLVCWVEDPNGDYFRKHLARIPDYIWVAEDGMKMQSFGSQEWDTGFSIQALLDSDLTHEIGPTLMKGHDFIKKSQVKDNPSGDFKSMYRHISKGSWTFSDQDHGWQVSDCTAEGLKCCLIFSTMPEEIVGKKIKPERLYDSVNVLLSLQRKNGGLSAWEPAGAQEWLELLNPTEFFADIVIEHEYVECTSSAIQALVLFKKLYPGHRKKEIDNFITNAVRYLEDTQMPDGSWYGNWGVCFTYGSWFALGGLAAAGKTYYNCAAVRKAVEFLLKSQMDDGGWGESYLSCPKKVYVPLEGNRSNLVHTGWALMGLIHSEQAERDPTPLHRAAKLLINSQMEDGDFPQQEISGVFMKNCMLHYAAYRNIYPLWALAEYRRRVPLPSLGT
Protein: Homeobox protein pal-1 (Caudal homolog 1) (Homeobox protein ceh-3) (Posterior alae in males protein 1) (P34766)
Organism: Caenorhabditis elegans
Function: Transcriptional activator. Interacts with promoter regions for tbx-8.9, tbx-9, elt-1, hnd-1, scrt-1, and vab-7 genes. Binds the sequence ATTTATGAC. Binds to the enhancer region of the hlh-1 gene promoter during embryonic body wall muscle development. Activates the gene for mab-5 in embryo development. Necessary for vab-7 expression in C blastomeres in the posterior of embryos. Required for posterior V6 neuroectoblast cell fate specification during postembryonic neurogenesis (patterning) which generates the characteristic ray lineage during male tail development. Binds to ced-3 promoter and activated expression which is crucial for tail-spike cell death. Has a role in E cell specification in endoderm development and body wall muscle development.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:8861906}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:8861906}. Chromosome {ECO:0000269|PubMed:8861906}. Note=Localized to condensed chromosomes.
Interaction partners:
- K Homology domain-containing protein
- T-box transcription factor tbx-8
- Pharynx and intestine in excess protein 1
- PIP-1
- RNA-binding protein pos-1
- Serum response factor homolog
- Female germline-specific tumor suppressor gld-1
- T-box transcription factor tbx-35
- C2H2-type domain-containing protein
Sequence:
MSVDVKSDFSENESSSTPSPTTVPADVTWPHYPMMPFMQPHPLREKMLQPTFDPQIYGRWSQMGDTGFYGHPDLYPFGLPQLAANGQIPAVEAVDVKPPLSNGSSSSDSGMYPSPSDMMTPFPSTSSGAASSSELSAAAAAAANYQMRAATCYQQSVWPFMDYQQFQGFSWKMPLGNNHGKDRRSSSDGKTLPTGPGTNNVRVRTADKYRMVYSDYQRLELEKEFHTSPFITSDRKSQLSTMLSLTERQIKIWFQNRRAKDRRDKQKIRL
Protein: Non-specific serine/threonine protein kinase (H2KYA6)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MPVGNSGSRSGRLARISQSNIRPFGSNGGGATNSYGPGTHPMSGAEPCSPTKKEKHRFEITKKLGSGTYGKVSLAYDHKFDREVAVKLIKKSAIESKADLVRIRREIRIMSALNHPNIIQIYEVFENKDKIILVMEYSSGGELYDYVSRCGSLPEAEARRIFRQITSAVLYCHKHRVAHRDLKLENILLDQNNNAKIADFGLSNYFADKNLLTTFCGSPLYASPEIINGTPYKGPEVDCWSLGILLYTLVYGSMPFDGRDFNRMVRQIKRGAYFEPETPSTASMLIRNMLRVNPERRATIFDIASHWWLNLEENMPVIQELPENQIIDHTPLTEREETMIVQDLADEQDVFMEFGHLSSETRRKIEDFRIRRKEAEEFNDNSPVKPPKARKTDELTGKISKEQPEEMKSAEKSLRGVKEEKEKPKVVDPNDPLERLRQIENRLGQNKKDKEAAKTSARVETVKLKEVKKEKSPEQQPEDPKTARGTSKPADSRAPSFVPVKDRPETSEPERPRTRPHLTASAYRIETDSLNMLMNQVLEQMEKGPVNLNIIARIKAHPLYDTRPMVKELLESIIAAQPEPVQKQTSKVVEQQTFSRQNTLTRKKKEDPLEEEIPEVPSPSRKMKERPWHSVEVGFDPDEEPEHDRMQESIASNATEVTVQDTSFEDDSSDEEERKKTPVASTPKTPVLIVEKQESSTNAEDEESDEGDDYSDAEMEELADEVDKKGPSDSKLAPVVENLEANPPPDPSSSPQFLDAFDRGLIKRQSKGKYQHTLINNYGRGVSTECESPTQQRKFFGGPQPSAELSPFLFDKAKEILQTYPNNKLDARGIDVELRRKLRMEKVKADLLKQPKDGDKPRNSYVGSVPPRSPPPIVVKSDGEELDDEEEEEEDEEEIEETDSEEGSDFENFKPKRPIIAAVRRDDGEKVPVAGTSAKYLVTVAELKLKPTDKKEEAQLKEQLKDSEINSERKTSQTNLLFRPSAYRESDLYRRINAALERPSVDPYDDRAFSPLSTDPFYSHHSSGSAAPSALGYVRPRYHDDSYRTHRDSDYRPMSPTSRYTAAVTRDDRGKSTSYDPHETTRPSYDRGYITSSNASPSYTRKFEHEQPTLNSWANDRKFEVYKTRAERDAERNTYHPTGTTGASSYRPSSYYTSASDRPVTGLRRPEESYTSSTNYGRYDGRSTTPSNDQYAISTALAENQASSMNNRFRPTARRVASAMTDADRRNYHRSRSMDRNKVDYEYGSNLLNRLTTPDSHGDYSYVNYHDSSNGRSNITLEKDGQPRSILKNKQSADIEPRVESSYEPSNGVRSVFERLRRHLSLEKSVSPQRQNTSFYGRQLRVASVGPHSRNIDSTSSALDNPKKKRSLLSFNRRKTSEVRMGADGKLVTNGYDSTPSSRDFKRPSSPIDRIKSLFRKNESSGTGHSDYYNSSRNYTSSNPVSTTREPYVAQYRKYPGSTSRDTSSALNRYSYTPGLTDQRRHWYDDPNIY
Protein: NF-protocadherin (Protocadherin 7 L homeolog precursor) (O57537)
Organism: Xenopus laevis (African clawed frog)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MMRTEGTQSCWSSWLLMLLHISLTVAATKQLLKYRIAEEGPADVRIGNVAKEIGIVKGSGDVTFSLESGSDYFKIDNVTGELSTTERRIDREKLQQCQMIFDENECFIDFEVSVIGPAQSWVELFEGRVVILDINDNTPTFPSPVLTLTVEENRPVGTLYLLPTATDRDFGRNGIERYELIQDAGESLYVSGRRGAPESGLYPGKRRMESDGRSSVFELQVADTSDGEKQPQLIVKGPLDREQRDSYELLRVRDGGEPPRSSQSILRVLITDVNDNSPRFEKSVYEADLAENSAPGTPILQLRAADYDVGVNGQIEYVFGAATESVRRLLRLDENSGWLSVLHRIDREEVNQLRFTVMARDRGQPPKTDKATVVLNIKDENDNVPLIDIRKIGRIPVKDGMANVAEDVLVDTPIALVQVSDRDQGENGVVTCTVVGDVPFQLKPASDGEGEQNKKKYFLHTSAPLDYENVKEYNVIIVAVDSGSPSLSSNNSLLVKVGDTNDNPPVFSQAAVEVAFPENNVLGERVATVLATDADSGKNAEIAYSLEPPMDGIFSIHPDTGDITVNIILDREQTDRYEFRVVAKDKGIPVLQGATSVVVQVADRNDNEPKFMQDVFTFYVKENLQPNSPVGMVTVMDSDKGRNAEMSLFIEEDSDIFSIENETGTIYSTVSFDREHQTSYTFRVKAVDGGDPPRSATATVSLFVMDENDNAPSISIPINTSYAVLSPASNVRTVVASVVATDSDNGVNADLNYSIVGGNPYKLFEIDSTSGVVSLVGKLTSKHYGLHRLVVQVNDSGQPPQSTIALVHVFVNETISNATVVDFQIARSLHTPLTQDIAGDPSYDMSKQRLSIVIGVVAGIMTVILIILVVVMARYCRAKSKNGYEAGKKDHEDFFTPQQHDKSKKPKKDKKNKKSKQPLYSSIVTVEASKPNGQRYDSVNEKLSDSPSMGRYRTVNGGPGSPDLARHYKSSSPLPTVQLHPQSPTAGKKHQAVQDLPPANTFVGAGDNISIGSDHCSEYSCQTNNKYSKQSHFLF
Protein: Menin (E7EN32)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGLKAAQKTLFPLRSIDDVVRLFAAELGREEPDLVLLSLVLGFVEHFLAVNRVIPTNVPELTFQPSPAPDPPGGLTYFPVADLSIIAALYARFTAQIRGAVDLSLYPREGGVSSRELVKKVSDVIWNSLSRSYFKDRAHIQSLFSFITGTKLDSSGVAFAVVGACQALGLRDVHLALSEDHAWVVFGPNGEQTAEVTWHGKGNEDRRGQTVNAGVAERSWLYLKGSYMRCDRKMEVAFMVCAINPSIDLHTDSLELLQLQQKLLWLLYDLGHLERYPMALGNLADLEELEPTPGRPDPLTLYHKGIASAKTYYRDEHIYPYMYLAGYHCRNRNVREALQAWADTATVIQDYNYCREDEEIYKEFFEVANDVIPNLLKEAASLLEAGEERPGEQSQVRQKVRIVSREAEAAEAEEPWGEEAREGRRRGPRRESKPEEPPPPKKPALDKGLGTGQGAVSGPPRKPPGTVAGTARGPEGGSTAQVPAPTASPPPEGPVLTFQSEKMKGMKELLVATKINSSAIKLQLTAQSQVQMKKQKVSTPSDYTLSFLKRQRKGL
Protein: Ribonuclease H2 subunit B (RNase H2 subunit B) (Rnh2B) (RNase H(202)) (Ribonuclease HI subunit B) (O94627)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Non catalytic subunit of RNase H2, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging-strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA:RNA duplexes (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}. Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Ribonuclease H2 subunit A
- Uncharacterized protein C12B10.15c
- DNA topoisomerase 1
- Proliferating cell nuclear antigen
- DNA polymerase delta catalytic subunit
- DNA polymerase epsilon catalytic subunit A
Sequence:
MQGKIFILPKDSTNQQFVELSHPLTGRPLRYLLTNDHLLQILQVGDSSKQRSWFVGDHVVSDGYLYVCTPIDLLALVLPIIQELTWSRRKEPNRYVSFEDFIEHFDNMGPHYPRVSEVLSPNLLNTLHRICKVNEPVGSLPKTFQLDESSVVKILLRKAKVAQENLPPSIVTELKKQLAPLDLRTPLPQDLLELSCKWHAASLVCEDLQPEWYNKLAYWQEELAPLHAYTKNLEESRKILVEKEALLNSKKRPQNSDITSSLLKKPNRKQATKKSKYFSGEGMTKISSFFTKK
Protein: All trans-polyprenyl-diphosphate synthase PDSS2 (All-trans-decaprenyl-diphosphate synthase subunit 2) (EC 2.5.1.91) (Candidate tumor suppressor protein) (Decaprenyl pyrophosphate synthase subunit 2) (Decaprenyl-diphosphate synthase subunit 2) (Solanesyl-diphosphate synthase subunit 2) (Q86YH6)
Organism: Homo sapiens (Human)
Function: Heterotetrameric enzyme that catalyzes the condensation of farnesyl diphosphate (FPP), which acts as a primer, and isopentenyl diphosphate (IPP) to produce prenyl diphosphates of varying chain lengths and participates in the determination of the side chain of ubiquinone. Supplies nona and decaprenyl diphosphate, the precursors for the side chain of the isoprenoid quinones ubiquinone-9 (Q9) and ubiquinone-10 (Q10) respectively. The enzyme adds isopentenyl diphosphate molecules sequentially to farnesyl diphosphate with trans stereochemistry. May play a role during cerebellar development (By similarity). May regulate mitochondrial respiratory chain function (By similarity).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:34800366}.
Interaction partners:
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
- All trans-polyprenyl-diphosphate synthase PDSS1
- Ubiquinone biosynthesis protein COQ9
- Atypical kinase COQ8A, mitochondrial
- Farnesyl pyrophosphate synthase
- Dehydrodolichyl diphosphate synthase complex subunit DHDDS
- Geranylgeranyl pyrophosphate synthase
- Dehydrodolichyl diphosphate synthase complex subunit NUS1
- Squalene synthase
- Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
Sequence:
MNFRQLLLHLPRYLGASGSPRRLWWSPSLDTISSVGSWRGRSSKSPAHWNQVVSEAEKIVGYPTSFMSLRCLLSDELSNIAMQVRKLVGTQHPLLTTARGLVHDSWNSLQLRGLVVLLISKAAGPSSVNTSCQNYDMVSGIYSCQRSLAEITELIHIALLVHRGIVNLNELQSSDGPLKDMQFGNKIAILSGDFLLANACNGLALLQNTKVVELLASALMDLVQGVYHENSTSKESYITDDIGISTWKEQTFLSHGALLAKSCQAAMELAKHDAEVQNMAFQYGKHMAMSHKINSDVQPFIKEKTSDSMTFNLNSAPVVLHQEFLGRDLWIKQIGEAQEKGRLDYAKLRERIKAGKGVTSAIDLCRYHGNKALEALESFPPSEARSALENIVFAVTRFS
Protein: Xaa-Pro aminopeptidase 2 (EC 3.4.11.9) (Aminoacylproline aminopeptidase) (Membrane-bound aminopeptidase P) (Membrane-bound APP) (Membrane-bound AmP) (mAmP) (X-Pro aminopeptidase 2) (O43895)
Organism: Homo sapiens (Human)
Function: Membrane-bound metalloprotease which catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro. May play a role in the metabolism of the vasodilator bradykinin.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q95333}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q95333}.
Interaction partners:
- Angiotensin-converting enzyme 2
- Meprin A subunit alpha
- Meprin A subunit beta
- Dipeptidyl peptidase 4
- Neprilysin
- Lysosomal Pro-X carboxypeptidase
- Xaa-Pro aminopeptidase 3
- Cytosol aminopeptidase
- Amyloid-beta precursor protein
- Kininogen-1
Sequence:
MARAHWGCCPWLVLLCACAWGHTKPVDLGGQDVRNCSTNPPYLPVTVVNTTMSLTALRQQMQTQNLSAYIIPGTDAHMNEYIGQHDERRAWITGFTGSAGTAVVTMKKAAVWTDSRYWTQAERQMDCNWELHKEVGTTPIVTWLLTEIPAGGRVGFDPFLLSIDTWESYDLALQGSNRQLVSITTNLVDLVWGSERPPVPNQPIYALQEAFTGSTWQEKVSGVRSQMQKHQKVPTAVLLSALEETAWLFNLRASDIPYNPFFYSYTLLTDSSIRLFANKSRFSSETLSYLNSSCTGPMCVQIEDYSQVRDSIQAYSLGDVRIWIGTSYTMYGIYEMIPKEKLVTDTYSPVMMTKAVKNSKEQALLKASHVRDAVAVIRYLVWLEKNVPKGTVDEFSGAEIVDKFRGEEQFSSGPSFETISASGLNAALAHYSPTKELNRKLSSDEMYLLDSGGQYWDGTTDITRTVHWGTPSAFQKEAYTRVLIGNIDLSRLIFPAATSGRMVEAFARRALWDAGLNYGHGTGHGIGNFLCVHEWPVGFQSNNIAMAKGMFTSIEPGYYKDGEFGIRLEDVALVVEAKTKYPGSYLTFEVVSFVPYDRNLIDVSLLSPEHLQYLNRYYQTIREKVGPELQRRQLLEEFEWLQQHTEPLAARAPDTASWASVLVVSTLAILGWSV
Protein: sn-glycerol-3-phosphate-binding periplasmic protein UgpB (Bile-responsive chaperone) (P0AG80)
Organism: Escherichia coli (strain K12)
Function: Part of the ABC transporter complex UgpBAEC involved in sn-glycerol-3-phosphate (G3P) import. Can also transport glycerophosphoryl diesters, which are hydrolyzed to G3P and alcohol during transport. The G3P moiety can be detected in the cytoplasm whereas the corresponding alcohol is usually found in the culture medium. Binds G3P and glycerophosphocholine, but not glycerol-2-phosphate. It was proposed by Yang et al that the complex could also transport glycerol-2-phosphate (G2P) in vivo, but as it was shown later by Wuttge et al that UgpB does not bind G2P, this transport activity is questioned. G2P might be converted in the periplasm to G3P before its transport.
Subcellular location: Periplasm {ECO:0000269|PubMed:32882062}.
Interaction partners:
- sn-glycerol-3-phosphate transport system permease protein UgpE
- sn-glycerol-3-phosphate import ATP-binding protein UgpC
- sn-glycerol-3-phosphate transport system permease protein UgpA
- Inner membrane ABC transporter permease protein YcjP
- Inner membrane ABC transporter permease protein YcjO
- Maltose/maltodextrin import ATP-binding protein MalK
- Glycerophosphodiester phosphodiesterase, cytoplasmic
- Maltose/maltodextrin transport system permease protein MalF
- Phosphate-binding protein PstS
- Glutathione-binding protein GsiB
Sequence:
MKPLHYTASALALGLALMGNAQAVTTIPFWHSMEGELGKEVDSLAQRFNAENPDYKIVPTYKGNYEQNLSAGIAAFRTGNAPAILQVYEVGTATMMASKAIKPVYDVFKEAGIQFDESQFVPTVSGYYSDSKTGHLLSQPFNSSTPVLYYNKDAFKKAGLDPEQPPKTWQDLADYAAKLKASGMKCGYASGWQGWIQLENFSAWNGLPFASKNNGFDGTDAVLEFNKPEQVKHIAMLEEMNKKGDFSYVGRKDESTEKFYNGDCAMTTASSGSLANIREYAKFNYGVGMMPYDADAKDAPQNAIIGGASLWVMQGKDKETYTGVAKFLDFLAKPENAAEWHQKTGYLPITKAAYDLTREQGFYEKNPGADTATRQMLNKPPLPFTKGLRLGNMPQIRVIVDEELESVWTGKKTPQQALDTAVERGNQLLRRFEKSTKS
Protein: Probable serine/threonine-protein kinase glkA (EC 2.7.11.26) (Glycogen synthase kinase-like kinase A) (Q55C57)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Rho-related protein rac1A
Sequence:
MTIPTDNNSSNNKGYNDNNNNNNNNNNNNNNNNNNNNNNNKEHPNINNNNNNNNNNNNNNIKESSSSNSNHSSSQSSSTATVNSNPKVYPYEIIKQVGQGTFGKVYEAKNQDNKRVAIKKVEKSNHFISREYDILKIVAHPNCLRILDMFYTAEDNKKMQNLVFDFIPYTLASLLKKRQLSINFIKVLFYQLCQAIKHIHSKAICHRDITPNNILLSSKGELTLADFGSAKILESNHTSMSYICSRYYRAPELLVGCSNYTTKIDIWSIGCILAEMLIGKPLFPGTNSNDQLGRIIEVLGSPTKDDMEAMKPSKPYHLQLPNINPKFFESLHNVEDKTVVDLLSKIFIFDPVKRASIDEIIAHPFLRDVNINSLELFDEMKCFSVSGNGKSSLTTNSTSSSSTTANMTSLASSSSNNKTTCSETYLSRLPTSAITSSSNLKSIDNSNNGKSSSSSNNIPSLNNSNNGVITNTI