wanglab/gogpt-training-data huggingface dataset:
Protein: Serine/threonine-protein kinase PLK (EC 2.7.11.21) (Polo-like kinase) (Q57VI0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- separase
- Mitotic cyclin
- Serine/threonine-protein kinase, putative
- Structural maintenance of chromosomes protein
- Structural maintenance of chromosomes protein
- Tubulin alpha chain
- Aurora kinase
- Tyrosine phosphatase, putative
- Cyclin 3
- Rev7, putative
Sequence:
MHATAETCETPSSSRRPPNDRPDFREGSTLKEFDKSGRLVGYFRCGRMLGRGGFAKCYEVEQGGDTYALKVVDRSLLQKTKTLQKLHSEISIHRRMKHKHIVNFIRTFHDDWNVYILLEKCSNQTLMEILKRRQRFSVPETQYIALQSLSAIQYMHEQCVIHRDLKLGNIMMDANMNVKIGDFGLAAELQYDGERKRTICGTPNYIAPEIIEGSREGHSYEVDVWSLGVILYTLLVGEPPFQTSDVKATYRRIRQCRYEFPSHVDVPESGKELIHSILQSRPDQRPTLLEIRSHPFFRLPPPPTTAPTTLFYSSRRRQHSDDPRGHAQGPLPLRRQKSGDIQAALQKQTPQRRQPQSQPKSVEAVRCISSPRVSREVLQPISTNLPKTDRYHLKPSCPAVASARFHGALGGDCNNNNNNNNNNINNNNNNNINSAAVSIPSPRADAIRPLTQVAAPGGADESAETTATTPRVQLRPHPAIEEEEKNELTAVHDQLHQTLREIGDISPREVATRTQTKRSPQVAPLPVPNSPTTSTVPALTPRCEDEPAPSLPLPTVWVTSFADFSEKYGLCYRLSTGHTGVHFNDSTKMVWEPITNRVEYYMRVKEVVARGNANVLQARDQQHAFHMDMFPESLTKKVTLIKYFKSYLSRTRNSHTNVEVVRCSPYVSEVTPSLSGPHMIEDIVYVKRWLITPQAIIFRLSNKTIQVCFHDKAEVILSSESRVVTYTEPTGNRVTMSLSSVATRSREIAARLRYTKDILSELIQNRDI
Protein: Selenoprotein N (SelN) (D3Z2R5)
Organism: Mus musculus (Mouse)
Function: Plays an important role in cell protection against oxidative stress and in the regulation of redox-related calcium homeostasis. Regulates the calcium level of the ER by protecting the calcium pump ATP2A2 against the oxidoreductase ERO1A-mediated oxidative damage. Within the ER, ERO1A activity increases the concentration of H(2)O(2), which attacks the luminal thiols in ATP2A2 and thus leads to cysteinyl sulfenic acid formation (-SOH) and SEPN1 reduces the SOH back to free thiol (-SH), thus restoring ATP2A2 activity. Acts as a modulator of ryanodine receptor (RyR) activity: protects RyR from oxidation due to increased oxidative stress, or directly controls the RyR redox state, regulating the RyR-mediated calcium mobilization required for normal muscle development and differentiation (By similarity). Essential for muscle regeneration and satellite cell maintenance in skeletal muscle.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9NZV5}.
Interaction partners:
- Selenoprotein K
- Selenoprotein M
- Selenoprotein S
- Protein adenylyltransferase SelO, mitochondrial
- Selenoprotein F
- Thioredoxin reductase-like selenoprotein T
- Selenide, water dikinase 2
- Selenoprotein W
- Selenoprotein H
- Selenoprotein V
Sequence:
MGQARPAARRPHSPDPGAQPAPPRRRARALALLGALLAAAAAVAAARACALLADAQAAARQESALKVLGTDGLFLFSSLDTDQDMYISPEEFKPIAEKLTGSVPVANYEEEELPHDPSEETLTIEARFQPLLMETMTKSKDGFLGVSRLALSGLRNWTTAASPSAAFAARHFRPFLPPPGQELGQPWWIIPGELSVFTGYLSNNRFYPPPPKGKEVIIHRLLSMFHPRPFVKTRFAPQGTVACLTAISDSYYTVMFRIHAEFQLSEPPDFPFWFSPGQFTGHIILSKDATHIRDFRLFVPNHRSLNVDMEWLYGASETSNMEVDIGYVPQMELEAVGPSVPSVILDEDGNMIDSRLPSGEPLQFVFEEIKWHQELSWEEAARRLEVAMYPFKKVNYLPFTEAFDRARAEKKLVHSILLWGALDDQSCUGSGRTLRETVLESPPILTLLNESFISTWSLVKELEDLQTQQENPLHRQLAGLHLEKYSFPVEMMICLPNGTVVHHINANYFLDITSMKPEDMENNNVFSFSSSFEDPSTATYMQFLREGLRRGLPLLQP
Protein: Protein Bouncer (H2LID1)
Organism: Oryzias latipes (Japanese rice fish) (Japanese killifish)
Function: Oocyte-expressed fertilization factor that mediates sperm-egg binding and is essential for sperm entry into the egg. Necessary and sufficient to mediate species-specific gamete recognition and fertilization, which is essential for vertebrate species performing external fertilization. External fertilization cannot guarantee that only conspecific sperm reaches the egg by precopulatory mate choice: proteins such as Bouncer can therefore support the selection of conspecific sperm.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P0DPQ9}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P0DPQ9}.
Interaction partners:
Sequence:
MGSLRTRQLFHAALLWLCLPLPLLLCENLHCYYSPVLEKEITFELVVTECPPNEMCFKGLGRYGNYTALSARGCMLEKDCSQVHSLRLLGTVYTMSYSCCDWPYCNRAVALEPLTAMLVAAAVVACSFCLT
Protein: Ferredoxin (Fer cargo protein) (A0A0F5HNC1)
Organism: Bacillus thermotolerans (Quasibacillus thermotolerans)
Function: Cargo protein of a type 1 encapsulin nanocompartment. An iron-binding protein probably involved in iron mineralization in the encapsulin nanocompartment. 2 different cargo proteins have been identified (IMEF and Fer); when both are expressed in E.coli with the shell protein only IMEF is detected within the nanocompartment. E.coli expressing all 3 genes stores the largest amount of iron and is protected from Fe/H2O2-induced oxidative stress.
Subcellular location: Encapsulin nanocompartment {ECO:0000269|PubMed:28263314}.
Interaction partners:
- assimilatory sulfite reductase
- Type 1 encapsulin shell protein
- Riboflavin biosynthesis protein RibBA
- Fumarate hydratase class I
- Putative iron-sulfur cluster assembly scaffold protein for SUF system, SufE2
- 2,4-dienoyl-CoA reductase
- Glyoxalase family protein
Sequence:
MSHDRRLTVGSLLPNQPRPVAVPKAPSVVQPSKQPLPEKAIIRLEQNGRSFSVRHVKGNLLTEGLSQGLPLQYKCRKGTCGVCTVKVTDGASRLSLPNQQEHKKLQGNIKSGFRLACQANME
Protein: Isocitrate dehydrogenase [NAD] subunit beta, mitochondrial (Isocitric dehydrogenase subunit beta) (NAD(+)-specific ICDH subunit beta) (O43837)
Organism: Homo sapiens (Human)
Function: Plays a structural role to facilitate the assembly and ensure the full activity of the enzyme catalyzing the decarboxylation of isocitrate (ICT) into alpha-ketoglutarate. The heterodimer composed of the alpha (IDH3A) and beta (IDH3B) subunits and the heterodimer composed of the alpha (IDH3A) and gamma (IDH3G) subunits, have considerable basal activity but the full activity of the heterotetramer (containing two subunits of IDH3A, one of IDH3B and one of IDH3G) requires the assembly and cooperative function of both heterodimers.
Subcellular location: Mitochondrion.
Interaction partners:
- Isocitrate dehydrogenase subunit alpha, mitochondrial
- Isocitrate dehydrogenase subunit gamma, mitochondrial
- Isocitrate dehydrogenase, mitochondrial
- Aconitate hydratase, mitochondrial
- Isocitrate dehydrogenase cytoplasmic
- 2-oxoglutarate dehydrogenase complex component E1
- 2-oxoglutarate dehydrogenase-like, mitochondrial
- Cytoplasmic aconitate hydratase
- Succinate--CoA ligase subunit alpha, mitochondrial
- Aspartate aminotransferase, mitochondrial
Sequence:
MAALSGVRWLTRALVSAGNPGAWRGLSTSAAAHAASRSQAEDVRVEGSFPVTMLPGDGVGPELMHAVKEVFKAAAVPVEFQEHHLSEVQNMASEEKLEQVLSSMKENKVAIIGKIHTPMEYKGELASYDMRLRRKLDLFANVVHVKSLPGYMTRHNNLDLVIIREQTEGEYSSLEHESARGVIECLKIVTRAKSQRIAKFAFDYATKKGRGKVTAVHKANIMKLGDGLFLQCCEEVAELYPKIKFETMIIDNCCMQLVQNPYQFDVLVMPNLYGNIIDNLAAGLVGGAGVVPGESYSAEYAVFETGARHPFAQAVGRNIANPTAMLLSASNMLRHLNLEYHSSMIADAVKKVIKVGKVRTRDMGGYSTTTDFIKSVIGHLQTKGS
Protein: Transcriptional repressor PaaX (P76086)
Organism: Escherichia coli (strain K12)
Function: Negative regulator of the paaZ and paaABCDEFGHIJK catabolic operons. Binds the consensus sequence 5'-WWTRTGATTCGYGWT-3'. Binding of PaaX is specifically inhibited by phenylacetyl-coenzyme A (PA-CoA).
Interaction partners:
- Phenylacetic acid degradation protein PaaY
- Putative 1,2-phenylacetyl-CoA epoxidase, subunit D
- 1,2-phenylacetyl-CoA epoxidase, subunit A
- 1,2-phenylacetyl-CoA epoxidase, subunit C
- Phenylacetate-coenzyme A ligase
- 1,2-phenylacetyl-CoA epoxidase, subunit B
- 1,2-epoxyphenylacetyl-CoA isomerase
- Acyl-coenzyme A thioesterase PaaI
- 3-hydroxyadipyl-CoA dehydrogenase
- Bifunctional protein PaaZ
Sequence:
MSKLDTFIQHAVNAVPVSGTSLISSLYGDSLSHRGGEIWLGSLAALLEGLGFGERFVRTALFRLNKEGWLDVSRIGRRSFYSLSDKGLRLTRRAESKIYRAEQPAWDGKWLLLLSEGLDKSTLADVKKQLIWQGFGALAPSLMASPSQKLADVQTLLHEAGVADNVICFEAQIPLALSRAALRARVEECWHLTEQNAMYETFIQSFRPLVPLLKEAADELTPERAFHIQLLLIHFYRRVVLKDPLLPEELLPAHWAGHTARQLCINIYQRVAPAALAFVSEKGETSVGELPAPGSLYFQRFGGLNIEQEALCQFIR
Protein: Uncharacterized protein (Q38AC6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MCLLSFFSLYPLGSFSSGKSNMDTPPISDDDKEVIDRLFASDVPQSLSRHAVLILHYHRTVFGSMVPSNVLLAGCLLYSCKWLSYPSGNSFLKNYFQGMKTSDIVGLEMVLHGTVRQNFMLVEACLRSEMSEIVRLNDVPHNRERIVLVCLNLVRALYRTRWCLLPETAARGALLVACEMCDVHLKSLPESFNTTMVTCAVDYLRSIFAQSRC
Protein: Agamous-like MADS-box protein AGL11 isoform X1 (Agamous-like MADS-box protein AGL11 isoform X2) (MADS-box protein MADS5) (A2IBV0)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGRGKIEIKRIENTTNRQVTFCKRRNGLLKKAYELSVLCDAEVALIVFSTRGRLYEYSNNNIRSTIERYKKACSGTSNTNTVTEINAQYYQQESAKLRQQIQMLQNSSRHLMGDSLSSLTVKELKQLENRLERGITRIRSKKHEMLLAEIEYFQKREVELENESVCLRAKIAEIERVEEANMVTGAELNAIQALASRNFFTPNVIERGTPTPYSHHDKKILHLG
Protein: NPC intracellular cholesterol transporter 1 (Niemann-Pick C1 protein) (O15118)
Organism: Homo sapiens (Human)
Function: Intracellular cholesterol transporter which acts in concert with NPC2 and plays an important role in the egress of cholesterol from the endosomal/lysosomal compartment. Unesterified cholesterol that has been released from LDLs in the lumen of the late endosomes/lysosomes is transferred by NPC2 to the cholesterol-binding pocket in the N-terminal domain of NPC1. Cholesterol binds to NPC1 with the hydroxyl group buried in the binding pocket. Binds oxysterol with higher affinity than cholesterol. May play a role in vesicular trafficking in glia, a process that may be crucial for maintaining the structural and functional integrity of nerve terminals (Probable). Inhibits cholesterol-mediated mTORC1 activation throught its interaction with SLC38A9.
Subcellular location: Late endosome membrane {ECO:0000269|PubMed:12554680, ECO:0000269|PubMed:27378690}; Multi-pass membrane protein {ECO:0000269|PubMed:10821832, ECO:0000269|PubMed:27238017, ECO:0000269|PubMed:28784760}. Lysosome membrane {ECO:0000269|PubMed:17897319, ECO:0000269|PubMed:27378690, ECO:0000269|PubMed:9927649}; Multi-pass membrane protein {ECO:0000269|PubMed:10821832, ECO:0000269|PubMed:27238017, ECO:0000269|PubMed:28784760}.
Interaction partners:
- Oxysterol-binding protein-related protein 5
- NPC intracellular cholesterol transporter 2
- GTP-binding protein 1
- Sigma intracellular receptor 2
- Neutral amino acid transporter 9
- Pancreatic secretory granule membrane major glycoprotein GP2
- Sterol regulatory element-binding protein 2
- StAR-related lipid transfer protein 3
- Sterol regulatory element-binding protein 1
- Phospholipid-transporting ATPase ABCA1
Sequence:
MTARGLALGLLLLLLCPAQVFSQSCVWYGECGIAYGDKRYNCEYSGPPKPLPKDGYDLVQELCPGFFFGNVSLCCDVRQLQTLKDNLQLPLQFLSRCPSCFYNLLNLFCELTCSPRQSQFLNVTATEDYVDPVTNQTKTNVKELQYYVGQSFANAMYNACRDVEAPSSNDKALGLLCGKDADACNATNWIEYMFNKDNGQAPFTITPVFSDFPVHGMEPMNNATKGCDESVDEVTAPCSCQDCSIVCGPKPQPPPPPAPWTILGLDAMYVIMWITYMAFLLVFFGAFFAVWCYRKRYFVSEYTPIDSNIAFSVNASDKGEASCCDPVSAAFEGCLRRLFTRWGSFCVRNPGCVIFFSLVFITACSSGLVFVRVTTNPVDLWSAPSSQARLEKEYFDQHFGPFFRTEQLIIRAPLTDKHIYQPYPSGADVPFGPPLDIQILHQVLDLQIAIENITASYDNETVTLQDICLAPLSPYNTNCTILSVLNYFQNSHSVLDHKKGDDFFVYADYHTHFLYCVRAPASLNDTSLLHDPCLGTFGGPVFPWLVLGGYDDQNYNNATALVITFPVNNYYNDTEKLQRAQAWEKEFINFVKNYKNPNLTISFTAERSIEDELNRESDSDVFTVVISYAIMFLYISLALGHMKSCRRLLVDSKVSLGIAGILIVLSSVACSLGVFSYIGLPLTLIVIEVIPFLVLAVGVDNIFILVQAYQRDERLQGETLDQQLGRVLGEVAPSMFLSSFSETVAFFLGALSVMPAVHTFSLFAGLAVFIDFLLQITCFVSLLGLDIKRQEKNRLDIFCCVRGAEDGTSVQASESCLFRFFKNSYSPLLLKDWMRPIVIAIFVGVLSFSIAVLNKVDIGLDQSLSMPDDSYMVDYFKSISQYLHAGPPVYFVLEEGHDYTSSKGQNMVCGGMGCNNDSLVQQIFNAAQLDNYTRIGFAPSSWIDDYFDWVKPQSSCCRVDNITDQFCNASVVDPACVRCRPLTPEGKQRPQGGDFMRFLPMFLSDNPNPKCGKGGHAAYSSAVNILLGHGTRVGATYFMTYHTVLQTSADFIDALKKARLIASNVTETMGINGSAYRVFPYSVFYVFYEQYLTIIDDTIFNLGVSLGAIFLVTMVLLGCELWSAVIMCATIAMVLVNMFGVMWLWGISLNAVSLVNLVMSCGISVEFCSHITRAFTVSMKGSRVERAEEALAHMGSSVFSGITLTKFGGIVVLAFAKSQIFQIFYFRMYLAMVLLGATHGLIFLPVLLSYIGPSVNKAKSCATEERYKGTERERLLNF
Protein: Mitochondrial ribonuclease P catalytic subunit (EC 3.1.26.5) (Mitochondrial ribonuclease P protein 3) (Mitochondrial RNase P protein 3) (Q8JZY4)
Organism: Mus musculus (Mouse)
Function: Catalytic ribonuclease component of mitochondrial ribonuclease P, a complex composed of TRMT10C/MRPP1, HSD17B10/MRPP2 and PRORP, which cleaves tRNA molecules in their 5'-ends. The presence of TRMT10C/MRPP1, HSD17B10/MRPP2 is required to catalyze tRNA molecules in their 5'-ends.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:O15091}.
Interaction partners:
- tRNA methyltransferase 10 homolog C
- 3-hydroxyacyl-CoA dehydrogenase type-2
- Ribonuclease P/MRP protein subunit POP5
- Ribonuclease P protein subunit p21
- Processing of 1, ribonuclease P/MRP family
- Ribonuclease P protein subunit p30
- Ribonuclease P protein subunit p29
- Ribonuclease P protein subunit p38
- ATP-dependent RNA helicase A
- Ribonuclease P protein subunit p25
Sequence:
MTFYLSGFRSIPKLWKSNPYFELGPATSSTPFFLCAIGNQQRWFSVKPTTPPNSKALNLLDTKARTHRKGNDNNGQVSSDPHYFAAGAAKKRSHIGANPQNQGHALPVRSSVQLPTKPLNSAEWDKLKEDFKGKASFEDFIISQMARNCCSVDVAKSLLAWVAAKNNGIVGYNLLVKYLYLCVFHKQTSEVIDVYEIMKAKYKSLESGGYTLLIRGLIHSDRWRESLLLLEDIKKVMVPSKKNYGDCIQGALLHQDVNTAWNLYQELIGHNLIPPLETLKAFFDYGKDINDDHYSDKLLDILLYLRNNQLYPGESFAHSIKTWFESIPGRQWKGQFTTIQKSGQCSGCGRTIEPIHLSPEEYEFLKEKIMRDVIDGGDQYKKTTPQELKRFESFVNSCPPFDIVIDGLNVAKMFPKGRESQNLLGVVSQLAQQNLQLLVLGRKHMLRPSSQWRKEEMEQVRKQAHCFFADNISEDDPFLLYATLNSGNHCKFITKDLLRDHKACLPDARTQRLFFKWQQGHQLAIMKGFQKSKLTFQHILSYDTVVQRTGDSWHIPYDEDLVQRSSCEVPTKWLCLQRKTPDPC
Protein: SH3 domain-binding glutamic acid-rich-like protein 2 (Fovea-associated SH3 domain-binding protein) (Q9UJC5)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000269|PubMed:12095696}.
Interaction partners:
Sequence:
MVIRVFIASSSGFVAIKKKQQDVVRFLEANKIEFEEVDITMSEEQRQWMYKNVPPEKKPTQGNPLPPQIFNGDRYCGDYDSFFESKESNTVFSFLGLKPRLASKAEP
Protein: Forkhead box protein M1 (Forkhead-related protein FKHL16) (Hepatocyte nuclear factor 3 forkhead homolog 11) (HFH-11) (HNF-3/fork-head homolog 11) (M-phase phosphoprotein 2) (MPM-2 reactive phosphoprotein 2) (Transcription factor Trident) (Winged-helix factor from INS-1 cells) (Q08050)
Organism: Homo sapiens (Human)
Function: Transcription factor regulating the expression of cell cycle genes essential for DNA replication and mitosis. Plays a role in the control of cell proliferation. Also plays a role in DNA break repair, participating in the DNA damage checkpoint response. Promotes transcription of PHB2.
Subcellular location: Nucleus.
Interaction partners:
- Myb-related protein B
- Serine/threonine-protein kinase PLK1
- Catenin beta-1
- Cyclin-dependent kinase 1
- Centromere protein F
- G2/mitotic-specific cyclin-B1
- Cyclin-A2
- Maternal embryonic leucine zipper kinase
- Baculoviral IAP repeat-containing protein 5
- Histone acetyltransferase p300
Sequence:
MKTSPRRPLILKRRRLPLPVQNAPSETSEEEPKRSPAQQESNQAEASKEVAESNSCKFPAGIKIINHPTMPNTQVVAIPNNANIHSIITALTAKGKESGSSGPNKFILISCGGAPTQPPGLRPQTQTSYDAKRTEVTLETLGPKPAARDVNLPRPPGALCEQKRETCADGEAAGCTINNSLSNIQWLRKMSSDGLGSRSIKQEMEEKENCHLEQRQVKVEEPSRPSASWQNSVSERPPYSYMAMIQFAINSTERKRMTLKDIYTWIEDHFPYFKHIAKPGWKNSIRHNLSLHDMFVRETSANGKVSFWTIHPSANRYLTLDQVFKPLDPGSPQLPEHLESQQKRPNPELRRNMTIKTELPLGARRKMKPLLPRVSSYLVPIQFPVNQSLVLQPSVKVPLPLAASLMSSELARHSKRVRIAPKVLLAEEGIAPLSSAGPGKEEKLLFGEGFSPLLPVQTIKEEEIQPGEEMPHLARPIKVESPPLEEWPSPAPSFKEESSHSWEDSSQSPTPRPKKSYSGLRSPTRCVSEMLVIQHRERRERSRSRRKQHLLPPCVDEPELLFSEGPSTSRWAAELPFPADSSDPASQLSYSQEVGGPFKTPIKETLPISSTPSKSVLPRTPESWRLTPPAKVGGLDFSPVQTSQGASDPLPDPLGLMDLSTTPLQSAPPLESPQRLLSSEPLDLISVPFGNSSPSDIDVPKPGSPEPQVSGLAANRSLTEGLVLDTMNDSLSKILLDISFPGLDEDPLGPDNINWSQFIPELQ
Protein: Type II NADH:quinone oxidoreductase Ndh (EC 1.6.5.9) (Type II NADH dehydrogenase Ndh) (P95160)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Alternative, nonproton pumping NADH:quinone oxidoreductase that delivers electrons to the respiratory chain by oxidation of NADH and reduction of quinones. Ndh is probably the main NADH dehydrogenase of M.tuberculosis.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15767566}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Enoyl-[acyl-carrier-protein] reductase
- Catalase-peroxidase
- 3-oxoacyl-[acyl-carrier-protein] synthase 1
- Alkyl hydroperoxide reductase C
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerase subunit alpha
- Cytochrome bc1 complex Rieske iron-sulfur subunit
Sequence:
MSPQQEPTAQPPRRHRVVIIGSGFGGLNAAKKLKRADVDIKLIARTTHHLFQPLLYQVATGIISEGEIAPPTRVVLRKQRNVQVLLGNVTHIDLAGQCVVSELLGHTYQTPYDSLIVAAGAGQSYFGNDHFAEFAPGMKSIDDALELRGRILSAFEQAERSSDPERRAKLLTFTVVGAGPTGVEMAGQIAELAEHTLKGAFRHIDSTKARVILLDAAPAVLPPMGAKLGQRAAARLQKLGVEIQLGAMVTDVDRNGITVKDSDGTVRRIESACKVWSAGVSASRLGRDLAEQSRVELDRAGRVQVLPDLSIPGYPNVFVVGDMAAVEGVPGVAQGAIQGAKYVASTIKAELAGANPAEREPFQYFDKGSMATVSRFSAVAKIGPVEFSGFIAWLIWLVLHLAYLIGFKTKITTLLSWTVTFLSTRRGQLTITDQQAFARTRLEQLAELAAEAQGSAASAKVAS
Protein: Peptide transport periplasmic protein (E0SFZ5)
Organism: Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))
Interaction partners:
- Predicted antimicrobial peptide transporter subunit membrane component of ABC superfamily
- Predicted antimicrobial peptide transporter subunit membrane component of ABC superfamily
- Peptide transport system ATP-binding protein
- Peptide transport system ATP-binding protein
- Dipeptide transporter membrane component of ABC superfamily
- Dipeptide transport system permease protein DppC
- Putative transporter, permease protein
- Putative transport system permease protein
- D-ala-D-ala transporter subunit
Sequence:
MSGKHTLALALAWLALPVLAQTPPATSTPAQAIRHSGFVYCVNDVLSTFNPQMARSGLMVDTLAAQLYDRLLGVDPYTYRLMPELAQHWDVTDNGSTYRFTLRRDVPFQQTSWFTPSRTMNADDVLFSFQRMLDKKHPFHDVNGGDYPYFDSLQLADNVQSIRKLGDYSIEIRLHSPDASFLWHLATHYAPILSAEYAQQLTRQDRRELLDRQPVGTGPYRLDEYRYGQYVRLKRNDDYWRGQPRMEQVVVDLGSGGTGRLSKLLTGECDVLAYPAASQLTILRNDPRLRLSLRPGMNVAYLAFNVRKPPLDDSRVRHAIALAINNDRLMQSIYYGTAETAASILPRASWAYDNEAQITEYNPEKARQQLKELGIANLQLQLWVPSASQSYNPSPVKTAELIQADLAQVGIKVTIMPVEGRFQEARLMEMNHDLTLAGWATDSNDPDSVFRPLLSCAAIRSQTNYAHWCDPGFDQVLQDALSSQQLSRRMEYYRVAHHILAAQLPVLPLASSLRMQAYRYDMKGLVLSPFGNASFAGVYRDDGSEEKNEEKPDGSAVDPSSSAPIQGEQP
Protein: N-acetylgalactosamine-N,N'-diacetylbacillosaminyl-diphospho-undecaprenol 4-alpha-N-acetylgalactosaminyltransferase (EC 2.4.1.291) (Protein glycosylation J) (Q0P9C7)
Organism: Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Function: Adds a GalNAc residue on to the Und-PP-Bac2,4diNAc-GalNAc disaccharide in the N-linked protein glycosylation pathway. Transfers the third sugar in the heptasaccharide biosynthesis.
Subcellular location: Cell inner membrane {ECO:0000305|PubMed:18034500}; Peripheral membrane protein {ECO:0000305|PubMed:18034500}.
Interaction partners:
- N,N'-diacetylbacillosaminyl-diphospho-undecaprenol alpha-1,3-N-acetylgalactosaminyltransferase
- Undecaprenyl phosphate N,N'-diacetylbacillosamine 1-phosphate transferase
- Protein glycosylation K
- GalNAc
- UDP-N-acetylbacillosamine N-acetyltransferase
- Undecaprenyl-diphosphooligosaccharide--protein glycotransferase
- Two-domain glucosyltransferase
- UDP-glucose 4-epimerase
- GalNAc-alpha-
- UDP-N-acetyl-alpha-D-glucosamine C6 dehydratase
Sequence:
MQKLGIFIYSLGSGGAERVVATLLPILSLKFEVHLILMNDKISYEIPECQIHFLECSKPSENPILKFLKLPFLALKYKKLCRNLGIDTEFVFLNRPNYIALMARMFGNKTRLVINECTTPSVMYMKNNFNSLVNKFLISLLYPKADLILPNSKGNLEDLVQNFSISPKKCEILYNAIDLENIGQKALEDIALKDKFILSVGRLDKGKNHALLIRAYARLKTDLKLVILGEGVLKDELLALIKELNLEEKVLLLGFDNNPYKYMAKCEFFAFASVFEGFSNVLIESLACSCAVVCTDHKSGARELFGDDEFGLLVEVDNENSMFQGLKTMLEDDKLRKAYKNKAKTRAKAFDKVKIARDALKYLLG
Protein: Hemolysin (P09545)
Organism: Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Function: Bacterial hemolysin that causes cytolysis by forming heptameric pores in target host membranes.
Subcellular location: Secreted {ECO:0000269|PubMed:15978620}. Host cell membrane {ECO:0000269|PubMed:15978620}; Multi-pass membrane protein {ECO:0000269|PubMed:15978620}. Note=In the hemolytic biotype El Tor the 80 kDa hemolysin precursor is secreted as monomer. After binding to target membranes the protein assembles into a heptameric prepore complex. Proteolytic cleavage triggers a conformation change that is required for membrane insertion and pore formation.
Interaction partners:
- Methyl-accepting chemotaxis protein HlyB
- Multifunctional-autoprocessing repeats-in-toxin
Sequence:
MPKLNRCAIAIFTILSAISSPTLLANINEPSGEAADIISQVADSHAIKYYNAADWQAEDNALPSLAELRDLVINQQKRVLVDFSQISDAEGQAEMQAQFRKAYGVGFANQFIVITEHKGELLFTPFDQAEEVDPQLLEAPRTARLLARSGFASPAPANSETNTLPHVAFYISVNRAISDEECTFNNSWLWKNEKGSRPFCKDANISLIYRVNLERSLQYGIVGSATPDAKIVRISLDDDSTGAGIHLNDQLGYRQFGASYTTLDAYFREWSTDAIAQDYRFVFNASNNKAQILKTFPVDNINEKFERKEVSGFELGVTGGVEVSGDGPKAKLEARASYTQSRWLTYNTQDYRIERNAKNAQAVSFTWNRQQYATAESLLNRSTDALWVNTYPVDVNRISPLSYASFVPKMDVIYKASATETGSTDFIIDSSVNIRPIYNGAYKHYYVVGAHQSYHGFEDTPRRRITKSASFTVDWDHPVFTGGRPVNLQLASFNNRCIQVDAQGRLAANTCDSQQSAQSFIYDQLGRYVSASNTKLCLDGEALDALQPCNQNLTQRWEWRKGTDELTNVYSGESLGHDKQTGELGLYASSNDAVSLRTITAYTDVFNAQESSPILGYTQGKMNQQRVGQDHRLYVRAGAAIDALGSASDLLVGGNGGSLSSVDLSGVKSITATSGDFQYGGQQLVALTFTYQDGRQQTVGSKAYVTNAHEDRFDLPAAAKITQLKIWSDDWLVKGVQFDLN
Protein: ABC transporter B family member 2 (ABC transporter ABCB.2) (AtABCB2) (Multidrug resistance protein 2) (P-glycoprotein 2) (Q8LPK2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000255|PROSITE-ProRule:PRU00441}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
Interaction partners:
Sequence:
MYISLIFFLSNHFPPLISIPIFIFLSFSSPTNYTHLKLKKMQPSGDPAPEKEKEMTQPKVSLLKLFSFADFYDCVLMTLGSVGACIHGASVPIFFIFFGKLINIIGLAYLFPKQASHRVAKYSLDFVYLSVAILFSSWLEVACWMHTGERQAAKMRRAYLRSMLSQDISLFDTEASTGEVISAITSDILVVQDALSEKVGNFLHYISRFIAGFAIGFTSVWQISLVTLSIVPLIALAGGIYAFVAIGLIARVRKSYIKAGEIAEEVIGNVRTVQAFTGEERAVRLYREALENTYKYGRKAGLTKGLGLGSMHCVLFLSWALLVWFTSVVVHKDIADGGKSFTTMLNVVIAGLSLGQAAPDISAFVRAKAAAYPIFKMIERNTVTKTSAKSGRKLGKVDGHIQFKDATFSYPSRPDVVIFDRLNLAIPAGKIVALVGGSGSGKSTVISLIERFYEPISGAVLLDGNNISELDIKWLRGQIGLVNQEPALFATTIRENILYGKDDATAEEITRAAKLSEAISFINNLPEGFETQVGERGIQLSGGQKQRIAISRAIVKNPSILLLDEATSALDAESEKSVQEALDRVMVGRTTVVVAHRLSTVRNADIIAVVHEGKIVEFGNHENLISNPDGAYSSLLRLQETASLQRNPSLNRTLSRPHSIKYSRELSRTRSSFCSERESVTRPDGADPSKKVKVTVGRLYSMIRPDWMYGVCGTICAFIAGSQMPLFALGVSQALVSYYSGWDETQKEIKKIAILFCCASVITLIVYTIEHICFGTMGERLTLRVRENMFRAILKNEIGWFDEVDNTSSMLASRLESDATLLKTIVVDRSTILLQNLGLVVTSFIIAFILNWRLTLVVLATYPLVISGHISEKLFMQGYGGDLNKAYLKANMLAGESVSNIRTVAAFCAEEKILELYSRELLEPSKSSFRRGQIAGLFYGVSQFFIFSSYGLALWYGSTLMDKGLAGFKSVMKTFMVLIVTALAMGETLALAPDLLKGNQMVASVFEILDRKTQIVGETSEELNNVEGTIELKGVHFSYPSRPDVVIFRDFDLIVRAGKSMALVGQSGSGKSSVISLILRFYDPTAGKVMIEGKDIKKLDLKALRKHIGLVQQEPALFATTIYENILYGNEGASQSEVVESAMLANAHSFITSLPEGYSTKVGERGVQMSGGQRQRIAIARAILKNPAILLLDEATSALDVESERVVQQALDRLMANRTTVVVAHRLSTIKNADTISVLHGGKIVEQGSHRKLVLNKSGPYFKLISLQQQQQP
Protein: Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 1 (Brain cyclic nucleotide-gated channel 1) (BCNG-1) (O60741)
Organism: Homo sapiens (Human)
Function: Hyperpolarization-activated ion channel exhibiting weak selectivity for potassium over sodium ions. Contributes to the native pacemaker currents in heart (If) and in neurons (Ih). May mediate responses to sour stimuli.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15351778, ECO:0000269|PubMed:28086084, ECO:0000269|PubMed:30351409}; Multi-pass membrane protein {ECO:0000269|PubMed:28086084, ECO:0000269|PubMed:31787376}.
Interaction partners:
- Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2
- Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 3
- Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 4
- PEX5-related protein
Sequence:
MEGGGKPNSSSNSRDDGNSVFPAKASATGAGPAAAEKRLGTPPGGGGAGAKEHGNSVCFKVDGGGGGGGGGGGGEEPAGGFEDAEGPRRQYGFMQRQFTSMLQPGVNKFSLRMFGSQKAVEKEQERVKTAGFWIIHPYSDFRFYWDLIMLIMMVGNLVIIPVGITFFTEQTTTPWIIFNVASDTVFLLDLIMNFRTGTVNEDSSEIILDPKVIKMNYLKSWFVVDFISSIPVDYIFLIVEKGMDSEVYKTARALRIVRFTKILSLLRLLRLSRLIRYIHQWEEIFHMTYDLASAVVRIFNLIGMMLLLCHWDGCLQFLVPLLQDFPPDCWVSLNEMVNDSWGKQYSYALFKAMSHMLCIGYGAQAPVSMSDLWITMLSMIVGATCYAMFVGHATALIQSLDSSRRQYQEKYKQVEQYMSFHKLPADMRQKIHDYYEHRYQGKIFDEENILNELNDPLREEIVNFNCRKLVATMPLFANADPNFVTAMLSKLRFEVFQPGDYIIREGAVGKKMYFIQHGVAGVITKSSKEMKLTDGSYFGEICLLTKGRRTASVRADTYCRLYSLSVDNFNEVLEEYPMMRRAFETVAIDRLDRIGKKNSILLQKFQKDLNTGVFNNQENEILKQIVKHDREMVQAIAPINYPQMTTLNSTSSTTTPTSRMRTQSPPVYTATSLSHSNLHSPSPSTQTPQPSAILSPCSYTTAVCSPPVQSPLAARTFHYASPTASQLSLMQQQPQQQVQQSQPPQTQPQQPSPQPQTPGSSTPKNEVHKSTQALHNTNLTREVRPLSASQPSLPHEVSTLISRPHPTVGESLASIPQPVTAVPGTGLQAGGRSTVPQRVTLFRQMSSGAIPPNRGVPPAPPPPAAALPRESSSVLNTDPDAEKPRFASNL