wanglab/gogpt-training-data huggingface dataset:
Protein: Attacin-C [Cleaved into: Immune-induced peptide 16 (DIM-16) (DIM16) (MPAC)] (Q95NH6)
Organism: Drosophila melanogaster (Fruit fly)
Function: Has antimicrobial activity in synergy with other peptides. Strongest activity observed against E.cloacae.
Subcellular location: Secreted {ECO:0000269|PubMed:14744858, ECO:0000269|PubMed:9736738}.
Interaction partners:
- Metchnikowin
- Diptericin B
- Diptericin A
- Drosocin antimicrobial peptides
- Attacin-A
- Peptidoglycan-recognition protein SB1
- Cecropin-C
- Cecropin-B
- Elevated during infection
- Peptidoglycan-recognition protein SD
Sequence:
MSKIVLLIVVIVGVLGSLAVALPQRPYTQPLIYYPPPPTPPRIYRARRQVLGGSLTSNPSGGADARLDLSKAVGTPDHHVIGQVFAAGNTQTKPVSTPVTSGATLGYNNHGHGLELTKTHTPGVRDSFQQTATANLFNNGVHNLDAKAFASQNQLANGFKFDRNGAALDYSHIKGHGATLTHANIPGLGKQLELGGRANLWQSQDRNTRLDLGSTASKWTSGPFKGQTDLGANLGLSHYFG
Protein: Nuclear factor interleukin-3-regulated protein (E4 promoter-binding protein 4) (Interleukin-3 promoter transcriptional activator) (Interleukin-3-binding protein 1) (Transcriptional activator NF-IL3A) (Q16649)
Organism: Homo sapiens (Human)
Function: Acts as a transcriptional regulator that recognizes and binds to the sequence 5'-[GA]TTA[CT]GTAA[CT]-3', a sequence present in many cellular and viral promoters. Represses transcription from promoters with activating transcription factor (ATF) sites. Represses promoter activity in osteoblasts (By similarity). Represses transcriptional activity of PER1 (By similarity). Represses transcriptional activity of PER2 via the B-site on the promoter (By similarity). Activates transcription from the interleukin-3 promoter in T-cells. Competes for the same consensus-binding site with PAR DNA-binding factors (DBP, HLF and TEF) (By similarity). Component of the circadian clock that acts as a negative regulator for the circadian expression of PER2 oscillation in the cell-autonomous core clock (By similarity). Protects pro-B cells from programmed cell death (By similarity). Represses the transcription of CYP2A5 (By similarity). Positively regulates the expression and activity of CES2 by antagonizing the repressive action of NR1D1 on CES2 (By similarity). Required for the development of natural killer cell precursors (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
Interaction partners:
- Class E basic helix-loop-helix protein 41
- Period circadian protein homolog 2
- Nuclear receptor subfamily 1 group D member 1
- Period circadian protein homolog 3
- Basic helix-loop-helix ARNT-like protein 1
- Cryptochrome-1
- Class E basic helix-loop-helix protein 40
- Nuclear receptor subfamily 1 group D member 2
- Neuronal PAS domain-containing protein 2
- Nuclear receptor ROR-alpha
Sequence:
MQLRKMQTVKKEQASLDASSNVDKMMVLNSALTEVSEDSTTGEELLLSEGSVGKNKSSACRRKREFIPDEKKDAMYWEKRRKNNEAAKRSREKRRLNDLVLENKLIALGEENATLKAELLSLKLKFGLISSTAYAQEIQKLSNSTAVYFQDYQTSKSNVSSFVDEHEPSMVSSSCISVIKHSPQSSLSDVSEVSSVEHTQESSVQGSCRSPENKFQIIKQEPMELESYTREPRDDRGSYTASIYQNYMGNSFSGYSHSPPLLQVNRSSSNSPRTSETDDGVVGKSSDGEDEQQVPKGPIHSPVELKHVHATVVKVPEVNSSALPHKLRIKAKAMQIKVEAFDNEFEATQKLSSPIDMTSKRHFELEKHSAPSMVHSSLTPFSVQVTNIQDWSLKSEHWHQKELSGKTQNSFKTGVVEMKDSGYKVSDPENLYLKQGIANLSAEVVSLKRLIATQPISASDSG
Protein: CD9 antigen (CD antigen CD9) (P40241)
Organism: Rattus norvegicus (Rat)
Function: Integral membrane protein associated with integrins, which regulates different processes, such as sperm-egg fusion, platelet activation and aggregation, and cell adhesion (By similarity). Present at the cell surface of oocytes and plays a key role in sperm-egg fusion, possibly by organizing multiprotein complexes and the morphology of the membrane required for the fusion (By similarity). In myoblasts, associates with CD81 and PTGFRN and inhibits myotube fusion during muscle regeneration (By similarity). In macrophages, associates with CD81 and beta-1 and beta-2 integrins, and prevents macrophage fusion into multinucleated giant cells specialized in ingesting complement-opsonized large particles (By similarity). Also prevents the fusion between mononuclear cell progenitors into osteoclasts in charge of bone resorption (By similarity). Acts as a receptor for PSG17 (By similarity). Involved in platelet activation and aggregation (By similarity). Regulates paranodal junction formation (By similarity). Involved in cell adhesion, cell motility and tumor metastasis (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P40240}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P40240}. Membrane {ECO:0000250|UniProtKB:P40240}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P40240}. Secreted, extracellular exosome {ECO:0000250|UniProtKB:P40240}. Note=Present at the cell surface of oocytes. Accumulates in the adhesion area between the sperm and egg following interaction between IZUMO1 and its receptor IZUMO1R/JUNO. {ECO:0000250|UniProtKB:P40240}.
Interaction partners:
- Prostaglandin F2 receptor negative regulator
- CD81 antigen
- CD63 antigen
- Tumor susceptibility gene 101 protein
- Integrin beta-1
- Immunoglobulin superfamily member 8
- CD44 antigen
- CD82 antigen
- Tetraspanin.
- Heat shock 70 kDa protein 4
Sequence:
MPVKGGSKCIKYLLFGFNFIFWLAGIAVLAIGLWLRFDSQTKSIFEQETNHSSFYTGVYILIGAGALMMLVGFLGCCGAVQESQCMLGLFFGFLLVIFAIEIAAAVWGYTHKDEVIKELQEFYKDTYQKLRNKDEPQRETLKAIHMALNCCGIAGGVEQFISDICPKKQVLESFQVKSCPDAIDEVFHSKFHIIGAVGIGIAVVMIFGMIFSMILCCAIRRSREMV
Protein: Ras-related protein Rap-1b (EC 3.6.5.2) (GTP-binding protein smg p21B) (Q99JI6)
Organism: Mus musculus (Mouse)
Function: GTP-binding protein that possesses intrinsic GTPase activity. Contributes to the polarizing activity of KRIT1 and CDH5 in the establishment and maintenance of correct endothelial cell polarity and vascular lumen. Required for the localization of phosphorylated PRKCZ, PARD3 and TIAM1 to the cell junction. Plays a role in the establishment of basal endothelial barrier function (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P61224}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P61224}. Cell junction {ECO:0000250|UniProtKB:P61224}. Note=May shuttle between plasma membrane and cytosol (By similarity). Presence of KRIT1 and CDH5 is required for its localization to the cell junction (By similarity). {ECO:0000250|UniProtKB:P61224}.
Interaction partners:
- Rap guanine nucleotide exchange factor 4
- RAS guanyl-releasing protein 2
- Krev interaction trapped protein 1
- Rap1 GTPase-activating protein 1
- Rap guanine nucleotide exchange factor 2
- Ral guanine nucleotide dissociation stimulator
- Serine/threonine-protein kinase B-raf
- Rap guanine nucleotide exchange factor 3
- Ras association domain-containing protein 5
- Afadin
Sequence:
MREYKLVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEVDAQQCMLEILDTAGTEQFTAMRDLYMKNGQGFALVYSITAQSTFNDLQDLREQILRVKDTDDVPMILVGNKCDLEDERVVGKEQGQNLARQWNNCAFLESSAKSKINVNEIFYDLVRQINRKTPVPGKARKKSSCQLL
Protein: DNA mismatch repair protein (A0A494C0M1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEGYPWWPCLVYNHPFDGTFIREKGKSVRVHVQFFDDSPTRGWVSKRLLKPYTGSKSKEAQKGGHFYSAKPEILRAMQRADEALNKDKIKRLELAVCDEPSEPEEEEEMEVGTTYVTDKSEEDNEIESEEEVQPKTQGSRRSSRQIKKRRVISDSESDIGGSDVEFKPDTKEEGSSDEISSGVGDSESEGLNSPVKVARKRKRMVTGNGSLKRKSSRKETPSATKQATSISSETKNTLRAFSAPQNSESQAHVSGGGDDSSRPTVWYHETLEWLKEEKRRDEHRRRPDHPDFDASTLYVPEDFLNSCTPGMRKWWQIKSQNFDLVICYKVGKFYELYHMDALIGVSELGLVFMKGNWAHSGFPEIAFGRYSDSLVQKGYKVARVEQTETPEMMEARCRKMAHISKYDRVVRREICRIITKGTQTYSVLEGDPSENYSKYLLSLKEKEEDSSGHTRAYGVCFVDTSLGKFFIGQFSDDRHCSRFRTLVAHYPPVQVLFEKGNLSKETKTILKSSLSCSLQEGLIPGSQFWDASKTLRTLLEEEYFREKLSDGIGVMLPQVLKGMTSESDSIGLTPGEKSELALSALGGCVFYLKKCLIDQELLSMANFEEYIPLDSDTVSTTRSGAIFTKAYQRMVLDAVTLNNLEIFLNGTNGSTEGTLLERVDTCHTPFGKRLLKQWLCAPLCNHYAINDRLDAIEDLMVVPDKISEVVELLKKLPDLERLLSKIHNVGSPLKSQNHPDSRAIMYEETTYSKKKIIDFLSALEGFKVMCKIIGIMEEVADGFKSKILKQVISLQTKNPEGRFPDLTVELNRWDTAFDHEKARKTGLITPKAGFDSDYDQALADIRENEQSLLEYLEKQRNRIGCRTIVYWGIGRNRYQLEIPENFTTRNLPEEYELKSTKKGCKRYWTKTIEKKLANLINAEERRDVSLKDCMRRLFYNFDKNYKDWQSAVECIAVLDVLLCLANYSRGGDGPMCRPVILLPEDTPPFLELKGSRHPCITKTFFGDDFIPNDILIGCEEEEQENGKAYCVLVTGPNMGGKSTLMRQAGLLAVMAQMGCYVPAEVCRLTPIDRVFTRLGASDRIMSGESTFFVELSETASILMHATAHSLVLVDELGRGTATFDGTAIANAVVKELAETIKCRTLFSTHYHSLVEDYSQNVAVRLGHMACMVENECEDPSQETITFLYKFIKGACPKSYGFNAARLANLPEEVIQKGHRKAREFEKMNQSLRLFREVCLASERSTVDAEAVHKLLTLIKEL
Protein: Ankycorbin (Ankyrin repeat and coiled-coil structure-containing protein) (Novel retinal pigment epithelial cell protein) (Retinoic acid-induced protein 14) (Q9P0K7)
Organism: Homo sapiens (Human)
Function: Plays a role in actin regulation at the ectoplasmic specialization, a type of cell junction specific to testis. Important for establishment of sperm polarity and normal spermatid adhesion. May also promote integrity of Sertoli cell tight junctions at the blood-testis barrier.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305|PubMed:11042181, ECO:0000305|PubMed:16729964}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:Q9EP71}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q5U312}. Cell junction {ECO:0000250|UniProtKB:Q5U312}. Nucleus {ECO:0000269|PubMed:16729964}. Note=Associated with the cortical actin cytoskeleton structures in terminal web and cell-cell adhesion sites (By similarity). Highly expressed at the ectoplasmic specialization, an actin-rich cell junction specific to the testis (By similarity). Predominantly nuclear in nonconfluent cells (PubMed:16729964). {ECO:0000250|UniProtKB:Q5U312, ECO:0000269|PubMed:16729964}.
Interaction partners:
Sequence:
MKSLKAKFRKSDTNEWNKNDDRLLQAVENGDAEKVASLLGKKGASATKHDSEGKTAFHLAAAKGHVECLRVMITHGVDVTAQDTTGHSALHLAAKNSHHECIRKLLQSKCPAESVDSSGKTALHYAAAQGCLQAVQILCEHKSPINLKDLDGNIPLLLAVQNGHSEICHFLLDHGADVNSRNKSGRTALMLACEIGSSNAVEALIKKGADLNLVDSLGYNALHYSKLSENAGIQSLLLSKISQDADLKTPTKPKQHDQVSKISSERSGTPKKRKAPPPPISPTQLSDVSSPRSITSTPLSGKESVFFAEPPFKAEISSIRENKDRLSDSTTGADSLLDISSEADQQDLLSLLQAKVASLTLHNKELQDKLQAKSPKEAEADLSFDSYHSTQTDLGPSLGKPGETSPPDSKSSPSVLIHSLGKSTTDNDVRIQQLQEILQDLQKRLESSEAERKQLQVELQSRRAELVCLNNTEISENSSDLSQKLKETQSKYEEAMKEVLSVQKQMKLGLVSPESMDNYSHFHELRVTEEEINVLKQDLQNALEESERNKEKVRELEEKLVEREKGTVIKPPVEEYEEMKSSYCSVIENMNKEKAFLFEKYQEAQEEIMKLKDTLKSQMTQEASDEAEDMKEAMNRMIDELNKQVSELSQLYKEAQAELEDYRKRKSLEDVTAEYIHKAEHEKLMQLTNVSRAKAEDALSEMKSQYSKVLNELTQLKQLVDAQKENSVSITEHLQVITTLRTAAKEMEEKISNLKEHLASKEVEVAKLEKQLLEEKAAMTDAMVPRSSYEKLQSSLESEVSVLASKLKESVKEKEKVHSEVVQIRSEVSQVKREKENIQTLLKSKEQEVNELLQKFQQAQEELAEMKRYAESSSKLEEDKDKKINEMSKEVTKLKEALNSLSQLSYSTSSSKRQSQQLEALQQQVKQLQNQLAECKKQHQEVISVYRMHLLYAVQGQMDEDVQKVLKQILTMCKNQSQKK
Protein: Period circadian regulator 1 (J3KSL6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSGPLEGADGGGDPRPGESFCPGGVPSPGPPQHRPCPGPSLADDTDANSNGSSGNESNGHESRGASQRSSHSSSSGNGKDSALLETTESSKSSEQSARARTQKELMTALRELKLRLP
Protein: Carbonic anhydrase (EC 4.2.1.1) (A8KB74)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- N-acetylglutamate synthase, mitochondrial
- Actin filament-associated protein 1-like 1
Sequence:
MVTLTAIVAPLGRQIHRHLVKHVRSQRWIPARACNLTACSSKLSILSQVHPMWQEPLAIPGGDRQSPIDIEVRKSIFNPQLRPLKVQYDPRTCQQIWNNGYSFLVEYDDTTDKSTVKGGPLENQYRLCQFHFHWGENNNWGSEHSIDRRLYAAELHIVHWNSDKYSLFEEAVMEENGLAVIGVFLKVGKRHEGLQKLVDALPAVRHKDSVVEFNKFDPSCLLPENISDYWTYPGSLTTPPLTEAVTWIVMKQHIEVSHDQLAVFRSLLFTSAEEQVQRSMVNNFRVQQDLKGRAVHSSFSPFLKETPSKE
Protein: Meiotic coiled-coil protein 6 (Horsetail movement protein hrs1) (Meiotically up-regulated gene 3 protein) (Q10336)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in meiotic nuclear oscillation and recombination. Required to remodel astral microtubules into the 'horsetail' astral array maintaining the 'horsetail' nuclear movement. Promotes homologous paring of chromosomes during this movement.
Subcellular location: Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Note=Localizes to the spindle pole body until the onset of meiosis I.
Interaction partners:
- Meiotically up-regulated gene 4 protein
- Meiotically up-regulated gene 43 protein
- Meiotic coiled-coil protein 5
- Karyogamy meiotic segregation protein 1
Sequence:
MEYQEEASLASAEDSTFIASSPVQSVSEMKSIKQKSFQYFDDYEKNVSDKTIQFQKLQMTAKEIIDAFERDSTQRTLQIESLESKIGEQERDLNNEKLASETLREKTQLLEKENGALKVENGYLYEKSRKLEEEMAHLKKKCNVYKSKFEESSLRCKSLYSSNTKLKDSMETMKRRMETETKEMNKIKPKNDSESDRFKRNSQSLSQQSPLLDVHSPDNSNHRTMLNINNSSPIKPKKIFKPNEVKNRISRLQKTFADLENQHHSFQQICQTLRKRLENDSSTTKQRLSKLEEIIRNRAPPSYSFSLNCSHTYQPVSCVEPVNHDLS
Protein: Voltage-gated potassium channel subunit beta-3 (EC 1.1.1.-) (K(+) channel subunit beta-3) (Kv-beta-3) (O43448)
Organism: Homo sapiens (Human)
Function: Accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. Alters the functional properties of Kv1.5.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q14722}.
Interaction partners:
- Potassium voltage-gated channel subfamily A member 4
- Potassium voltage-gated channel subfamily A member 5
- Potassium voltage-gated channel subfamily B member 2
- Potassium voltage-gated channel subfamily A member 1
- Potassium voltage-gated channel subfamily A member 2
- Potassium voltage-gated channel subfamily V member 1
- Potassium voltage-gated channel subfamily A member 3
- Voltage-gated inwardly rectifying potassium channel KCNH3
- Potassium voltage-gated channel subfamily A member 6
- Voltage-gated potassium channel KCNC1
Sequence:
MQVSIACTEQNLRSRSSEDRLCGPRPGPGGGNGGPAGGGHGNPPGGGGSGPKARAALVPRPPAPAGALRESTGRGTGMKYRNLGKSGLRVSCLGLGTWVTFGSQISDETAEDVLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGWRRSSYVITTKIFWGGQAETERGLSRKHIIEGLRGSLERLQLGYVDIVFANRSDPNCPMEEIVRAMTYVINQGLALYWGTSRWGAAEIMEAYSMARQFNLIPPVCEQAEHHLFQREKVEMQLPELYHKIGVGSVTWYPLACGLITSKYDGRVPDTCRASIKGYQWLKDKVQSEDGKKQQAKVMDLLPVAHQLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIEHLGALQVLSQLTPQTVMEIDGLLGNKPHSKK
Protein: PWWP domain-containing protein 3 (Q09842)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the mst2 complex which is a highly specific H3 lysine 14 (H3K14) acetyltransferase that functions together with gcn5 to regulate global levels of H3K14 acetylation (H3K14ac), critical for DNA damage checkpoint activation.
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Histone acetyltransferase mst2
- E3 ubiquitin-protein ligase brl1
- Mst2 complex subunit nto1
- Chromatin modification-related protein eaf6
- PWWP domain-containing protein 1
- PWWP domain-containing protein2
- Pdp3-interacting factor 1
- RNA polymerase II-associated protein 1 homolog
- Pdp3-interacting factor 2
Sequence:
MMVARTRSQKRKLEEINNQKKIKTKKKATGQQTSNTKNLRDVKKKGKQLAYVPRTSPRKSYKNGEYVLAKMSSFPWWPARVASQKSIPTEVRERLKRNFRMDNGIFVQFLPSRDYAIISSSNVLPLTVDESRFILDHDLSTKYIQKTVGLIIASVKRKVSFSDVEEDEFEPENTRKKLQKPIEKPKKEKIEATPKIDGGKRLKNEKSSAEISQTSKQRPSRRSARVRMATDNAQKSPSPIPSPKKTAKKRVRFAGSLEELPKFSLEYQLAQPISTVDMYAQVHYIRFNTLLYYRYQLQEILLSYNHYPQESDMSHVHQILEMIENFSAINSELLESTKLYSLFTLLVKLSDIPLDEKYDFSSRFSTLLLQFQAFVQPKTMTSNVSTAPIGKNAQVNTEAARPSVITT
Protein: Tyrosine--tRNA ligase, mitochondrial (EC 6.1.1.1) (Tyrosyl-tRNA synthetase) (TyrRS) (Q8BYL4)
Organism: Mus musculus (Mouse)
Function: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:Q9Y2Z4}.
Interaction partners:
- Tyrosine--tRNA ligase, cytoplasmic
- Bifunctional glutamate/proline--tRNA ligase
- Tryptophan--tRNA ligase, mitochondrial
- Tryptophan--tRNA ligase, cytoplasmic
- Methionine--tRNA ligase, mitochondrial
- Probable proline--tRNA ligase, mitochondrial
- Probable arginine--tRNA ligase, mitochondrial
- Methionine--tRNA ligase, cytoplasmic
- Alanine--tRNA ligase, cytoplasmic
- Glutamine--tRNA ligase
Sequence:
MAAPMLRRLCRVPQSLVWLRGSRAVRPGARGMLVAPRARGLFKEFFPESGTKTELPELFDRRRAGSSPQTVYCGFDPTGDSLHVGHLLTLLGLFHFQRAGHNVIALVGGSTALLGDPSGRTKGREALSAECVRANAHALRRGLEALAANHARLFADGRPWGSFTVLDNAAWFQEQHLVDFLATVGGHFRMGTLLSRLSVQSRLKSPEGMSLAEFFYQVLQAYDFYYLFQHYGCRVQLGGSDQLGNIMSGYEFIHKLTGEDVFGITVPLITSTTGAKLGKSAGNAVWLNREKTSPFELYQFFVRQQDDSVERYLKLFTFLPLPEIDHIMQLHVKEPEKRVAQKRLAAEVTKLVHGQEGLDSAKRCTQALYHSSIEALEVMSDQELKELFKEASFSELVLDPGTSVIDTCRKANAIPDGPRGYRMITEGGVSINHRQVTNPESVLVIGQHILKNGLSLLKIGKRNFYIIKWLQL
Protein: tRNA (cytosine(38)-C(5))-methyltransferase (EC 2.1.1.204) (DNA (cytosine-5)-methyltransferase-like protein 2) (Dnmt2) (DNA methyltransferase homolog MmuIIP) (DNA MTase homolog MmuIIP) (M.MmuIIP) (Met-2) (O55055)
Organism: Mus musculus (Mouse)
Function: Specifically methylates cytosine 38 in the anticodon loop of tRNA(Asp).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O14717}.
Interaction partners:
- RNA cytosine C
- tRNA
- DNA
- tRNA
- DNA
- DNA
- Heterogeneous nuclear ribonucleoprotein K
- 28S rRNA
- Putative methyltransferase NSUN7
- 5-cytosine rRNA methyltransferase NSUN4
Sequence:
MEPLRVLELYSGIGGMHHALRESHIPAHVVAAIDVNTVANEVYKHNFPHTHLLSKTIEGISLEDFDKLSFNMILMSPPCQPFTRIGLQGDMTDPRTTSFLYILDILPRLQKLPKYILLENVKGFEVSSTRGLLIQTIEACGFQYQEFLLSPSSLGIPNSRLRYFLIAKLQSEPFPFQAPGQILMEFPKIVTVEPQKYAVVEESQPRVQRTGPRICAESSSTQSSGKDTILFKLETVEERDRKHQQDSDLSVQMLKDFLEDGDTDEYLLPPKLLLRYALLLDIVKPTSRRSMCFTKGYGSYIEGTGSVLQAAEDAQIENIYKSLPDLPPEEKIAKLSMLKLRYFTPKEIANLQGFPPEFGFPEKTTVKQRYRLLGNSLNVHVVAKLLTVLCEGFGNASESCHKMPLILDSNSKILS
Protein: receptor protein-tyrosine kinase (EC 2.7.10.1) (Q9XZL6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MSLLRTILLIIISIHFKLAHADQVVLLDTTREATLEWTRYPYGPQAQTPGWVEESFTDFVKGINWRSYVVCDVAYHNVNNWLWSPFIDRGSANRLYIEIQFTIRDCSLFPGNALSCKETFSLLFYEFDAATREPPPWQTDSYRLIARIAAGEGRFNQNSDVDINTEVKSIAVNKKGVYFAFRDQGACISVLAVKVYYITCPAVTENFAHFNETPTGREITIIEKQNGTCVDNAEPYETPTYLCKGDGKWTILTGGCRCKAGYEPNYTNKTCTECPLGTFKSPEVTKCTPCPPNSNASKTGSPFCKCASGYYRHPNDGRHMPCYSPPAAPTNLTLLFVDQTSAIISWSAPAKNESFSSETNSKIYHSDIVYKIKCNICSPNVVYNPSTDTFNETKITLTNLEPVTTYTVQIHAINSVSHINEFKRHSNESSLVAVSDIVFSNTSLLNIPLDLNEVKTGQAEIVFTTESVLLSTVFNLRILAITNKDADLEWDKPVQSDFPLEFYEVGWFPKVELDAINKSALNTKETKAHIVGLLENTEYGFQVRCKTNNGFGSYSNMIYAQTLQSVGSVYDDSVQIRFIAGAIVTGVLFLVIFIIATVYFMRSKHQDDLDKKSTNHLPLPLDYASNEVNSMDTTPIVKKLHLNVTTPLFGNSRSYVDPHTYEDPNQAIREFAREIDANYITIEAIIGGGEFGDVCRGRLKIPPNFVQDIDVAIKTLKPGSSEKARCDFLTEASIMGQFDHPNVIYLQGVVTRSNPVMIITEYMENGSLDTFLRVNDGKFQTLQLIVMLRGIASGMSYLSDMNYVHRDLAARNVLVNAQLICKIADFGLSREIENASDAYTTRGGKIPVRWTAPEAIAFRKFTSASDVWSYGVVLWEVMSYGERPYWNWSNQDVIKCIEKGYRLPAPMDCPEALYQLMLDCWQKQRTHRPTFASIVSTLDNLARQPQSLLTTRPSPESDGNHILDGQRGQNIFISTDLWLEHIKMSRYCHHFKEANLINAQQISRLTAQQLSDMGITLVGHQKKILHQARQLDTII
Protein: Large ribosomal subunit protein P2B (60S acidic ribosomal protein P2-B) (CaRP2B) (Q9HFQ4)
Organism: Candida albicans (Yeast)
Function: Plays an important role in the elongation step of protein synthesis.
Interaction partners:
Sequence:
MKYLAAYLLLVQGGNTSPSASDITALLESVGVEAEESRLQALLKDLEGKDLQELIAEGNTKLASVPSGGAAAGGASASTGAAAGGAAEAEEEKEEEAKEESDDDMGFGLFD
Protein: Calmodulin 5 (F4IVN6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MADQLTDDQISEFKEAFSLFDKDGDGCITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLNLMARKMKDTDSEEELKEAFRVFDKDQNGFISAAELRHVMTNLGEKLTDEEVDEMIKEADVDGDGQINYEEFVKVMMAKRRGKRVMAAKRSSNSAEYKEKNGRRKSHCRIL
Protein: Hydrazine synthase subunit beta (HZS-beta) (Q1Q0T4)
Organism: Kuenenia stuttgartiensis
Function: Component of the hydrazine synthase complex that catalyzes the condensation of nitric oxide (NO) with ammonium to form hydrazine. The beta subunit may play a role in modulating transport of the hydroxylamine intermediate through a tunnel between the gamma and alpha subunit's active site. Is involved in anaerobic ammonium oxidation (anammox), a biological process in which nitrite is used as the electron acceptor in the conversion of ammonium to dinitrogen gas (N2) and water; this bacterial process has a major role in the Earth's nitrogen cycle and has been estimated to synthesize up to 50% of the dinitrogen gas emitted into our atmosphere from the oceans.
Subcellular location: Anammoxosome {ECO:0000305|PubMed:21964329}.
Interaction partners:
Sequence:
MVIRRKMNKMIRKGMIGAVMLGAAVAISGGVATAGYIQGTHVKTDLPGPFHITMSPDGSTLFISNQSGHSVTFVDARTQKVTGEVAVRVQPEASAVTPDGAFLYVCNAESDSVSVVDIQRKQEIKEIKVGDWPSGIKISPDGKTAYVACSGCMWNAIDVIDTGRMEKVRSIYTSDYGPRMVEISPDGKTLVAILDTVGSINRSVDFIDIASGRVVENRVIHESSNLRDVVYTPDGKYIAVTHQTPKNWLPVCEAENGQVFTNNVTIIETKAGGKVARLPLDDLNNYDGNPYGMAMDPKGKYLYIGVRGMHRVTILDMDKVLGLVRSSTQEELDYLRDDLGLVRDYLVARVPTGLGPSSVCLSPDGKFCYAANYFSNNVTVIRTAVD
Protein: C-type lectin domain family 4 member E (C-type lectin superfamily member 9) (Macrophage-inducible C-type lectin) (MINCLE) (Q9ULY5)
Organism: Homo sapiens (Human)
Function: Calcium-dependent lectin that acts as a pattern recognition receptor (PRR) of the innate immune system: recognizes damage-associated molecular patterns (DAMPs) of abnormal self and pathogen-associated molecular patterns (PAMPs) of bacteria and fungi. The PAMPs notably include mycobacterial trehalose 6,6'-dimycolate (TDM), a cell wall glycolipid with potent adjuvant immunomodulatory functions. Interacts with signaling adapter Fc receptor gamma chain/FCER1G to form a functional complex in myeloid cells (By similarity). Binding of mycobacterial trehalose 6,6'-dimycolate (TDM) to this receptor complex leads to phosphorylation of the immunoreceptor tyrosine-based activation motif (ITAM) of FCER1G, triggering activation of SYK, CARD9 and NF-kappa-B, consequently driving maturation of antigen-presenting cells and shaping antigen-specific priming of T-cells toward effector T-helper 1 and T-helper 17 cell subtypes (By similarity). Also recognizes alpha-mannose residues on pathogenic fungi of the genus Malassezia and mediates macrophage activation (By similarity). Through recognition of DAMPs released upon nonhomeostatic cell death, enables immune sensing of damaged self and promotes inflammatory cell infiltration into the damaged tissue (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:18490740, ECO:0000305|PubMed:24101491}; Single-pass type II membrane protein {ECO:0000305}. Cell projection, phagocytic cup {ECO:0000250|UniProtKB:Q9R0Q8}.
Interaction partners:
- High affinity immunoglobulin epsilon receptor subunit gamma
- Tyrosine-protein kinase SYK
- C-type lectin domain family 4 member D
- Splicing factor 3B subunit 3
- TYRO protein tyrosine kinase-binding protein
- Caspase recruitment domain-containing protein 9
- Toll-like receptor 2
- Interleukin-1 beta
- C-type lectin domain family 6 member A
- C-type lectin domain family 1 member A
Sequence:
MNSSKSSETQCTERGCFSSQMFLWTVAGIPILFLSACFITRCVVTFRIFQTCDEKKFQLPENFTELSCYNYGSGSVKNCCPLNWEYFQSSCYFFSTDTISWALSLKNCSAMGAHLVVINSQEEQEFLSYKKPKMREFFIGLSDQVVEGQWQWVDGTPLTKSLSFWDVGEPNNIATLEDCATMRDSSNPRQNWNDVTCFLNYFRICEMVGINPLNKGKSL