wanglab/gogpt-training-data huggingface dataset:
Protein: Aip56 (Q2VL32)
Organism: Photobacterium damsela subsp. piscicida (causative agent of fish pasteurellosis) (Pasteurella piscicida)
Interaction partners:
Sequence:
MTAIFSLAINSNFVLANNDKPDASDDKYADYVVRLGSEHPLNHTQIIELSSAVSRAVLLSYPNIIDRYTAAATEYTVIDALFHSPTFRHIVSFGLHNQQENLGHIRYTNEYEINNNREDEFSLVSEVSYDDIKSSNAQQVPLVAFYEAREDRATGTPIVNMGVAPSLFSGRYSWWQEALIHEIVHHVTGSSDTHEENKQGPTEILAQMVAAELHWAIPTFKGYSDPARVEAIQERDFHSLLNMFQRHGSELGFLFTRLATIAKGKKASPDFGTLTSFCSEGISSFPKYPDHDDDFNGGGAFFLPSASADSSVECTFDVLNRIEPVDDSIKFEGGNLLIKNDFKNLNLRVAQLSFLNAKKGSGFYRKNWDSWKSWYQASSWKNGLNSGLYGYGHDESEGNLIYSPYGITFNDGSFSIGFSSRKHINDNTKDDNFVKLNNANWSSFYYAGQMFFDKNKRPVALVITEPLNAAFGAGWSYIYKDGKWHYEAQDDWDQRLFKDSTLSLDPHAPQFIN
Protein: Protein NRT1/ PTR FAMILY 5.11 (AtNPF5.11) (Q8RX67)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Chloride channel protein CLC-b
- Chloride channel protein CLC-a
Sequence:
MAITYSSADELGNTTEGFLEIRENTSGGWKSARLIIVVQMAERFAYFGIASNLIMYLTGPLGESTAAAAANVNAWTGTVAFLPLLGGFLADSYLGRFRTIIISSSLYILGLGLLSFSTMIPSHQSKDSNQLQETIFFFSLYLVAIGQGGYNPCIKVFGADQFDGNDHKEARDKSSFFNWLMFGNCISILTTRLVSTYIQENLSWSLGFGIPSVSMLLSLFLFLLGTTSYRFSTERVGKKNPFARISRVFMEALKNRRQPDLDIANANANETLLLLAHQSSKQFRFLDRAAISCELAEIEEAKAVLRLIPIWITSVVYTIVHAQSPTFFTKQGATMDRSISPGLLVPAATLQSFINLSVVVFIPIYDRLLVPFARSFTQNSSGITTLQRIGTGIFLSILAMVLAALVETKRLQAARDELSIPMSVWWLIPQYVIFGVSDMFTMVGLQEFFYGQVPSELRSVGMALNLSIYGAGNYLSSFMISVIDKITNQYGQRSWFDNDLDQAHLDYFYWLLACLGFIGFAFYLWFAKSYVYSRSNTF
Protein: Advanced glycosylation end product-specific receptor (Receptor for advanced glycosylation end products) (Q62151)
Organism: Mus musculus (Mouse)
Function: Mediates interactions of advanced glycosylation end products (AGE). These are nonenzymatically glycosylated proteins which accumulate in vascular tissue in aging and at an accelerated rate in diabetes. Acts as a mediator of both acute and chronic vascular inflammation in conditions such as atherosclerosis and in particular as a complication of diabetes. AGE/RAGE signaling plays an important role in regulating the production/expression of TNF-alpha, oxidative stress, and endothelial dysfunction in type 2 diabetes. Interaction with S100A12 on endothelium, mononuclear phagocytes, and lymphocytes triggers cellular activation, with generation of key pro-inflammatory mediators. Interaction with S100B after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling. Can also bind oligonucleotides. Receptor for amyloid beta peptide. Contributes to the translocation of amyloid-beta peptide (ABPP) across the cell membrane from the extracellular to the intracellular space in cortical neurons. ABPP-initiated RAGE signaling, especially stimulation of p38 mitogen-activated protein kinase (MAPK), has the capacity to drive a transport system delivering ABPP as a complex with RAGE to the intraneuronal space. RAGE-dependent signaling in microglia contributes to neuroinflammation, amyloid accumulation, and impaired learning/memory in a mouse model of Alzheimer disease.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q15109}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, phagocytic cup {ECO:0000250|UniProtKB:Q15109}. Early endosome {ECO:0000250|UniProtKB:Q15109}. Nucleus {ECO:0000269|PubMed:28977635}. Note=Nuclear translocation is enhanced by irradiation, hypoxia and reperfusion injury to brain or kidney. {ECO:0000269|PubMed:28977635}.; SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000250|UniProtKB:Q15109}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000269|PubMed:16503878}.; SUBCELLULAR LOCATION: [Isoform 10]: Cell membrane {ECO:0000269|PubMed:24260107}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- High mobility group protein B1
- Protein S100-B
- GTPase KRas
- Surfactant protein C
- Protein diaphanous homolog 1
- NADPH oxidase 4
- NADPH oxidase 2
- GTPase HRas
- NADPH oxidase 1
- GTPase NRas
Sequence:
MPAGTAARAWVLVLALWGAVAGGQNITARIGEPLVLSCKGAPKKPPQQLEWKLNTGRTEAWKVLSPQGGPWDSVARILPNGSLLLPATGIVDEGTFRCRATNRRGKEVKSNYRVRVYQIPGKPEIVDPASELTASVPNKVGTCVSEGSYPAGTLSWHLDGKLLIPDGKETLVKEETRRHPETGLFTLRSELTVIPTQGGTHPTFSCSFSLGLPRRRPLNTAPIQLRVREPGPPEGIQLLVEPEGGIVAPGGTVTLTCAISAQPPPQVHWIKDGAPLPLAPSPVLLLPEVGHEDEGTYSCVATHPSHGPQESPPVSIRVTETGDEGPAEGSVGESGLGTLALALGILGGLGVVALLVGAILWRKRQPRREERKAPESQEDEEERAELNQSEEAEMPENGAGGP
Protein: Probable sugar-transport integral membrane protein ABC transporter (O53484)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU363032}.
Interaction partners:
- Probable sugar-transport integral membrane protein ABC transporter
- Trehalose import ATP-binding protein SugC
- Probable sugar-binding lipoprotein
- Probable Sn-glycerol-3-phosphate transport integral membrane protein ABC transporter UgpE
- Probable sugar-transport integral membrane protein ABC transporter UspB
- Trehalose import ATP-binding protein SugC
- Trehalose transport system permease protein SugB
- Trehalose import ATP-binding protein SugC
- Probable Sn-glycerol-3-phosphate-binding lipoprotein UgpB
- Probable periplasmic sugar-binding lipoprotein UspC
Sequence:
MTRRRGRRAWAGRMFVAPNLAAVVVFMLFPLGFSLYMSFQKWDLFTHATFVRLDNFRNLFTSDPLFLIAVVNTAVYTVGTVVPTVIVSLVVAAFLNRKIKGISLFRTVVFLPLAISSVVMAVVWQFVFNTDNGLLNIMLGWLGIGPIPWLIEPRWAMVSLCLVSVWRSVPFATVVLLAAMQGVPETVYEAARIDGAGEIRQFVSITVPLIRGALSFVVVISIIHAFQAFDLVYVLTGANGGPETATYVLGIMLFQHAFSFLEFGYASALAWVMFAILLVLTVLQLRITHRRSWEASRGLG
Protein: Fractalkine (FK) (ABCD-3) (C-X3-C motif chemokine 1) (CX3C membrane-anchored chemokine) (Neurotactin) (Small-inducible cytokine D1) [Cleaved into: Processed fractalkine] (O35188)
Organism: Mus musculus (Mouse)
Function: Chemokine that acts as a ligand for both CX3CR1 and integrins ITGAV:ITGB3 and ITGA4:ITGB1. The CX3CR1-CX3CL1 signaling exerts distinct functions in different tissue compartments, such as immune response, inflammation, cell adhesion and chemotaxis. Regulates leukocyte adhesion and migration processes at the endothelium. Can activate integrins in both a CX3CR1-dependent and CX3CR1-independent manner (By similarity). In the presence of CX3CR1, activates integrins by binding to the classical ligand-binding site (site 1) in integrins (By similarity). In the absence of CX3CR1, binds to a second site (site 2) in integrins which is distinct from site 1 and enhances the binding of other integrin ligands to site 1 (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:9177350}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Processed fractalkine]: Secreted {ECO:0000269|PubMed:10382755}.
Interaction partners:
- CX3C chemokine receptor 1
- C-C chemokine receptor type 2
- C-X-C chemokine receptor type 4
- C-X-C chemokine receptor type 1
- Cell surface glycoprotein CD200 receptor 1
- C-C chemokine receptor type 5
- C-X-C chemokine receptor type 3
- Eotaxin
- C-C motif chemokine 5
- C-X-C chemokine receptor type 6
Sequence:
MAPSPLAWLLRLAAFFHLCTLLPGQHLGMTKCEIMCDKMTSRIPVALLIRYQLNQESCGKRAIVLETTQHRRFCADPKEKWVQDAMKHLDHQAAALTKNGGKFEKRVDNVTPGITLATRGLSPSALTKPESATLEDLALELTTISQEARGTMGTSQEPPAAVTGSSLSTSEAQDAGLTAKPQSIGSFEAADISTTVWPSPAVYQSGSSSWAEEKATESPSTTAPSPQVSTTSPSTPEENVGSEGQPPWVQGQDLSPEKSLGSEEINPVHTDNFQERGPGNTVHPSVAPISSEETPSPELVASGSQAPKIEEPIHATADPQKLSVLITPVPDTQAATRRQAVGLLAFLGLLFCLGVAMFAYQSLQGCPRKMAGEMVEGLRYVPRSCGSNSYVLVPV
Protein: Histatin-1 (Hst1) (Histidine-rich protein 1) (Post-PB protein) (PPB) [Cleaved into: His1-(31-57)-peptide (His1 31/57) (His1-(12-38)-peptide) (His1 12/38) (Histatin 2) (Hst2) (Histatin-2)] (P15515)
Organism: Homo sapiens (Human)
Function: Histatins are salivary proteins that are considered to be major precursors of the protective proteinaceous structure on tooth surfaces (enamel pellicle). In addition, histatins exhibit antibacterial and antifungal activities.
Subcellular location: [Histatin-1]: Secreted. Mitochondrion {ECO:0000269|PubMed:32225006, ECO:0000269|PubMed:35970844}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:32225006, ECO:0000269|PubMed:34233061, ECO:0000269|PubMed:35970844}. Note=Hst 1 co-localized with mitochondria as well as the endoplasmic reticulum (ER) after internalization in host cells. {ECO:0000269|PubMed:32225006, ECO:0000269|PubMed:34233061, ECO:0000269|PubMed:35970844}.; SUBCELLULAR LOCATION: [His1-(31-57)-peptide]: Secreted. Mitochondrion {ECO:0000269|PubMed:32225006}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:32225006}. Note=Hst 2 co-localized with mitochondria as well as the endoplasmic reticulum (ER) after internalization in host cells. {ECO:0000269|PubMed:32225006}.
Interaction partners:
- Statherin
- Histatin-3
- Mucin-7
- Mucin-5B
- Platelet-derived growth factor receptor beta
- Cystatin-S
Sequence:
MKFFVFALVLALMISMISADSHEKRHHGYRRKFHEKHHSHREFPFYGDYGSNYLYDN
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (B8ZZI5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGHALCVCSRGTVIIDNKRYLFIQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDREEAQREADMHRLFNHPNILRLVAYCLRERGAKHEAWLLLPFFKRGTLWNEIERLKDKGNFLTEDQILWLLLGICRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQACIHVEGSRQALTLQSLGCVLYAMMFGEGPYDMVFQKGDSVALAVQNQLSIPQSPRHSSALRQLLNSMMTVDPHQRPHIPLLLSQLEALQPPAPGQHTTQI
Protein: MYG1 exonuclease (F8VR84)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MYENFVEEVDAVDNGISQWAEGEPRYALTTTLSARVARLNPTWNHPDQDTEAGFKRAMDLVQEEFLQRLDFYQHSWLPARALVEEALAQRFQVDPSGEIVELAKGACPWKEHLYHLESGLSPPVAIFFVIYTDQAGQWRIQCVPKEPHSFQSRLPLPEPWRGLRDEALDQVSGIPGCIFVHASGFTGGHHTREGALSMARATLAQRSYLPQIS
Protein: bMERB domain-containing protein 1 (Q96MC5)
Organism: Homo sapiens (Human)
Interaction partners:
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Centrosomal protein 20
Sequence:
MELKQSLSTHLEAEKPLRRYGAVEETAWKTERLGRNQLDIISMAETTMMPEEIELEMAKIQRLREVLVRRESELRFMMDDIQLCKDIMDLKQELQNLVAIPEKEKTKLQKQREDELIQKIHKLVQKRDFLVDDAEVERLREQEEDKEMADFLRIKLKPLDKVTKSPASSRAEKKAEPPPSKPTVAKTGLALIKDCCGATQCNIM
Protein: Centrosomal protein of 164 kDa (Cep164) (Q5DU05)
Organism: Mus musculus (Mouse)
Function: Plays a role in microtubule organization and/or maintenance for the formation of primary cilia (PC), a microtubule-based structure that protrudes from the surface of epithelial cells. Plays a critical role in G2/M checkpoint and nuclear divisions. A key player in the DNA damage-activated ATR/ATM signaling cascade since it is required for the proper phosphorylation of H2AX, RPA, CHEK2 and CHEK1. Plays a critical role in chromosome segregation, acting as a mediator required for the maintenance of genomic stability through modulation of MDC1, RPA and CHEK1 (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:22863007, ECO:0000269|PubMed:26337392}. Nucleus {ECO:0000250|UniProtKB:Q9UPV0}. Note=Localizes specifically to very distally located appendage structures on the mature centriole from which initiate PC formation (PubMed:26337392). Persisted at centrioles throughout mitosis (By similarity). In response to DNA damage, it translocates to nuclear foci that contain the DNA damage response proteins KAT5/TIP60 and CHEK1 (By similarity). {ECO:0000250|UniProtKB:Q9UPV0, ECO:0000269|PubMed:26337392}.
Interaction partners:
- Centrosomal protein of 83 kDa
- Sodium channel and clathrin linker 1
- Centrosomal protein of 89 kDa
- Outer dense fiber protein 2
- Ninein
- Fas-binding factor 1
- Tau-tubulin kinase 2
- Trichoplein keratin filament-binding protein
- Centromere protein F
- Serine/threonine-protein kinase PLK1
Sequence:
MARRPILLGDQLVLEEDSDETYVPSEQEILDFARVIGIDPIKEPELMWLAREGIEAPLPKGWKPCQNITGDLYYFNFDTGQSIWDHPCDEHYRKLVIQERERWSAPGAIKKKDKKKKKEKKNKKDKETSKSPLVLGSPLALVQAPLWGLAPLRGLGDAPPSALRGSQSVSLGSSADSGHLGEPTLPPQGLKAAACAKGLLASVHEGKNALSLLTLGEETNEEDEEESDNQSVRSSSELLKNLHLDLGALGGNFEYEESPRTSQPDKKDVSLDSDADRPPTPGKLFSQGADSSVASANGSKSQGRGASPWNPQKENENSDPKASSSQMAPELDPGGDQPSRASKKQQAEDPVQAGKEGECRRESAAKEPKEASALENTSDVSEESEIHGHLKDARHSGSEASGPKSFLGLDLGFRSRISEHLLDGDTLSPVLGGGHWEAQGLDQEEQDDSKSSIAEPQSKHTQGSEREHLQSSLHSQATEEGPLQTLEGQPEWKEAEGPGKDSVASPAPLSLLQREQVLSPPASPERAEEKHSQAEELGLEQPEAEETEEKVAVCPSSPVSPEVQTAEPAAPQKLFSEAILKGMELEEDQRLLLEFQKEKPQQLEERLWEEEEEEVCQLYQQKEKSLSLLKAQLQKATAEEKEKEEETKIREEESRRLVCLRAQVQSRTEAFENQIRTEQQAALQRLREEAETLQKAERASLEQKSRRALEQLREQLEAEERSAQAALRAEKEAEKEAALLQLREQLEGERKEAVAGLEKKHSAELEQLCSSLEAKHQEVISSLQKKIEGAQQKEEAQLQESLGWAEQRAHQKVHQVTEYEQELSSLLRDKRQEVEREHERKMDKMKEEHWQEMADARERYEAEERKQRADLLGHLTGELERLRRAHERELESMRQEQDQQLEDLRRRHRDHERKLQDLEVELSSRTKDVKARLAQLNVQEENIRKEKQLLLDAQRQAALEREEATATHQHLEEAKKEHTHLLETKQQLRRTIDDLRVRRVELESQVDLLQAQSQRLQKHLSSLEAEVQRKQDVLKEMAAEMNASPHPEPGLHIEDLRKSLDTNKNQEVSSSLSLSKEEIDLSMESVRQFLSAEGVAVRNAKEFLVRQTRSMRRRQTALKAAQQHWRHELASAQEVDEDLPGTEVLGNMRKNLNEETRHLDEMKSAMRKGHDLLKKKEEKLIQLESSLQEEVSDEDTLKGSSIKKVTFDLSDMDDLSSESLESSPVLHITPTPTSADPNKIHYLSSSLQRISSELNGVLNVLGSLNSQPPPQGLGSQPPPPLFTSSLRSSKNVLDPAYSSQAKLSSLSSITPMSTQWAWDPGQGTKLTSSSSSQTVDDFLLEKWRKYFPSGIPLLSGSPPPPENKLGYVSVSEQLHFLQRSHPRVPRTDGVSIQSLIDSNRKWLEHFRNDPKVQLFSSAPKATTTSNLSNLLQLGLDENNRLNVFHY
Protein: Probable cytochrome P450 301a1, mitochondrial (EC 1.14.-.-) (CYPCCCIA1) (Q9V6D6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion membrane {ECO:0000305}.
Interaction partners:
- Spookier
Sequence:
MNNLSLKAWRSTVSCGPNLRQCVPRISGAGSRRAQCRESSTGVATCPHLADSEEASAPRIHSTSEWQNALPYNQIPGPKPIPILGNTWRLMPIIGQYTISDVAKISSLLHDRYGRIVRFGGLIGRPDLLFIYDADEIEKCYRSEGPTPFRPSMPSLVKYKSVVRKDFFGDLGGVVGVHGEPWREFRSRVQKPVLQLSTIRRYLQPLEVITEDFLVRCENLLDENQELPEDFDNEIHKWSLECIGRVALDTRLGCLESNLKPDSEPQQIIDAAKYALRNVATLELKAPYWRYFPTPLWTRYVKNMNFFVGVCMKYIQSATERLKTQDPSLRAGEPSLVEKVILSQKDEKIATIMALDLILVGIDTISMAVCSMLYQLATRPVDQQKVHEELKRLLPDPNTPLTIPLLDQMHHLKGFIKEVFRMYSTVIGNGRTLMEDSVICGYQVPKGVQAVFPTIVTGNMEEYVTDAATFRPERWLKPQHGGTPGKLHPFASLPYGYGARMCLGRRFADLEMQILLAKLLRNYKLEYNHKPLDYAVTFMYAPDGPLRFKMTRV
Protein: GMP synthase (glutamine-hydrolyzing) (EC 6.3.5.2) (Glutamine amidotransferase) (Q9VIE7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Inosine-5'-monophosphate dehydrogenase
- Ubiquitin carboxyl-terminal hydrolase 7
- Adenine phosphoribosyltransferase
- CTP synthase
- Inosine triphosphate pyrophosphatase
- Guanylate kinase
- Phosphoribosylformylglycinamidine synthase
- Bifunctional glutamate/proline--tRNA ligase
- Lysine--tRNA ligase
- nucleoside diphosphate phosphatase
Sequence:
MNSNIFLGTAENGLRHDKIVILDAGAQYGKVIDRKVRELFVETDILPLDTPAATIRNNGYRGIIISGGPNSVYAEDAPSYDPDLFKLKIPMLGICYGMQLINKEFGGTVLKKDVREDGQQNIEIETSCPLFSRLSRTQSVLLTHGDSVERVGENLKIGGWSTNRIVTAIYNEVLRIYGVQFHPEVDLTINGKQMLSNFLYEICELTPNFTMGSRKEECIRYIREKVGNNKVLLLVSGGVDSSVCAALLRRALYPHQIIAVHVDNGFMRKKESEKVERSLRDIGIDLIVRKEGYTFLKGTTQVKRPGQYSVVETPMLCQTYNPEEKRKIIGDIFVKVTNDVVAELKLKPEEVMLAQGTLRPDLIESASSMVSTNAETIKTHHNDTDLIRELRNAGRVVEPLCDFHKDEVRDLGNDLGLPQELVERQPFPGPGLAIRVLCAEEAYMEKDYSETQVIIRVIVDYKNKLQKNHALINRVTAATSEAEQKDLMRISSNSQIQATLLPIRSVGVQGDKRSYSYVVGLSTSQEPNWQDLLFLAKIIPRILHNVNRVCYIFGEPVQYLVTDITHTTLNTVVLSQLRQADDIANEIIMQAGLYRKISQMPVVLIPVHFDRDPINRTPSCRRSVVLRPFITNDFMTGVPAEPGSVQMPLQVLNQIVRDISKLDGISRVLYDLTAKPPGTTEWE
Protein: Superoxide dismutase [Mn] 2, mitochondrial (EC 1.15.1.1) (Protein MANGANESE SUPEROXIDE DISMUTASE 2) (AtMSD2) (Q9LYK8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Subcellular location: Mitochondrion matrix {ECO:0000250}.
Interaction partners:
- Superoxide dismutase 3
- Superoxide dismutase 2, chloroplastic
- Superoxide dismutase 1
- Superoxide dismutase 2, chloroplastic
- Superoxide dismutase 3, chloroplastic
- Superoxide dismutase 1, chloroplastic
- Superoxide dismutase 1, mitochondrial
- 1-Cys peroxiredoxin PER1
- Large ribosomal subunit protein uL29m
- Large ribosomal subunit protein mL46
Sequence:
MTTTVIIIIFVAIFATTLHDARGATMEPCLESMKTASLPDLPYAYDALEPAISEEIMRLHHQKHHQTYVTQYNKALNSLRSAMADGDHSSVVKLQSLIKFNGGGHVNHAIFWKNLAPVHEGGGKPPHDPLASAIDAHFGSLEGLIQKMNAEGAAVQGSGWVWFGLDRELKRLVVETTANQDPLVTKGSHLVPLIGIDVWEHAYYPQYKNARAEYLKNIWTVINWKYAADVFEKHTRDLDIN
Protein: Kumgang (LP08967p) (Q9VK36)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MELPSMVERSGDRLVVRSLVSGAPLYQSSIEGGAGAVLPMSQSVQPLIGQDFLEQQLEQYKANNFMFPLSMAGFVSADSAPPGDLAKENMENSLPDGNPCNNNNDDELPQCKIRRNYSCNQCAFFTQNPRSHLSHLRDVHGERIVINECKLCLYASRHFQKLVRHMKMVHGCSDDGGAVQGSGAQPRGKRNLSREVRKRRLEESIEGQGATGQCLDLSVLRMIQNGPPLEQLKVELQQQEMQLLASVQAYNRQQEMLQLQQIVESHDNIFSMAYEFQTKLMPPKQAESLKLEQQNSSSDSEETAKSPSPDTRELVSGKEQFQCQKCSYSTPIRARFKKHVKYHSMPLIKCSSCDFHTPYKWNLDRHTKNHGANGHFKCSCCDFSTDIKQSLTIHESNHHVPMPVHQMGNRSRDEAEDLVDQQSSGSRKPETFKNGGATVASTESLLPRTSGIVCSHCQKRVGNAMQLINHLQVCTLALHNTTQLQASINAEVDLHDEDFPNAPTDLSYCGVETAPGYGEVTEVLPEEPEDLAPLKKVFKCPHCSFWAATASRFHVHIVGHLNRKPFECSLCAYRSNWRWDITKHIRLKALRDRSHNQAQVLMNDETGRRNYAKYNQYLTMMKVSAEQLADSKGMRTGEMIVMPPEKLDDHHPMETEEIIEMVDSAHSTSALDLRKPRDDQTEDLAGNSDELPQEGAKTEPNLEPLSFKSLNSSQVMPKPKGSPMNLTKTDGGQSDETTSADESNESD
Protein: Keratin-associated protein 5-7 (Keratin-associated protein 5-3) (Keratin-associated protein 5.3) (Keratin-associated protein 5.7) (Ultrahigh sulfur keratin-associated protein 5.7) (Q6L8G8)
Organism: Homo sapiens (Human)
Function: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated protein (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins.
Interaction partners:
- Keratin-associated protein 5-6
- Keratin-associated protein 5-11
- Keratin-associated protein 5-5
- Keratin-associated protein 5-10
Sequence:
MGCCGCSEGCGSGCGGCGSGCGGCGSGCGGCGSSCCVPVCCCKPVCCCVPACSCSSCGSCGGSKGGCGSCGGSKGGCGSCGGSKGGCGSCGCSQCSCYKPCCCSSGCGSSCCQSSCCKPCCCQSSCCKPCCCSSGCGSSCCQSSCCNPCCSQSSCCVPVCCQCKI
Protein: NACHT, LRR and PYD domains-containing protein 9 (Nucleotide-binding oligomerization domain protein 6) (PYRIN and NACHT-containing protein 12) (Q7RTR0)
Organism: Homo sapiens (Human)
Function: As the sensor component of the NLRP9 inflammasome, plays a crucial role in innate immunity and inflammation. In response to pathogens, including rotavirus, initiates the formation of the inflammasome polymeric complex, made of NLRP9, PYCARD and CASP1. Recruitment of proCASP1 to the inflammasome promotes its activation and CASP1-catalyzed IL1B and IL18 maturation and release in the extracellular milieu. The active cytokines stimulate inflammatory responses. Inflammasomes can also induce pyroptosis, an inflammatory form of programmed cell death. NLRP9 inflammasome activation may be initiated by DHX9 interaction with viral double-stranded RNA (dsRNA), preferentially to short dsRNA segments.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q66X22}. Inflammasome {ECO:0000269|PubMed:28636595}.
Interaction partners:
- Caspase-1
- NACHT, LRR and PYD domains-containing protein 1
- NACHT, LRR and PYD domains-containing protein 6
- Interferon-inducible protein AIM2
- NACHT, LRR and PYD domains-containing protein 3
- Apoptosis-associated speck-like protein containing a CARD
- Caspase recruitment domain-containing protein 8
- Caspase-5
- ATP-dependent RNA helicase DHX33
- Pyrin
Sequence:
MAESFFSDFGLLWYLKELRKEEFWKFKELLKQPLEKFELKPIPWAELKKASKEDVAKLLDKHYPGKQAWEVTLNLFLQINRKDLWTKAQEEMRNKLNPYRKHMKETFQLIWEKETCLHVPEHFYKETMKNEYKELNDAYTAAARRHTVVLEGPDGIGKTTLLRKVMLDWAEGNLWKDRFTFVFFLNVCEMNGIAETSLLELLSRDWPESSEKIEDIFSQPERILFIMDGFEQLKFNLQLKADLSDDWRQRQPMPIILSSLLQKKMLPESSLLIALGKLAMQKHYFMLRHPKLIKLLGFSESEKKSYFSYFFGEKSKALKVFNFVRDNGPLFILCHNPFTCWLVCTCVKQRLERGEDLEINSQNTTYLYASFLTTVFKAGSQSFPPKVNRARLKSLCALAAEGIWTYTFVFSHGDLRRNGLSESEGVMWVGMRLLQRRGDCFAFMHLCIQEFCAAMFYLLKRPKDDPNPAIGSITQLVRASVVQPQTLLTQVGIFMFGISTEEIVSMLETSFGFPLSKDLKQEITQCLESLSQCEADREAIAFQELFIGLFETQEKEFVTKVMNFFEEVFIYIGNIEHLVIASFCLKHCQHLTTLRMCVENIFPDDSGCISDYNEKLVYWRELCSMFITNKNFQILDMENTSLDDPSLAILCKALAQPVCKLRKLIFTSVYFGHDSELFKAVLHNPHLKLLSLYGTSLSQSDIRHLCETLKHPMCKIEELILGKCDISSEVCEDIASVLACNSKLKHLSLVENPLRDEGMTLLCEALKHSHCALERLMLMYCCLTSVSCDSISEVLLCSKSLSLLDLGSNALEDNGVASLCAALKHPGCSIRELWLMGCFLTSDSCKDIAAVLICNGKLKTLKLGHNEIGDTGVRQLCAALQHPHCKLECLGLQTCPITRACCDDIAAALIACKTLRSLNLDWIALDADAVVVLCEALSHPDCALQMLGLHKSGFDEETQKILMSVEEKIPHLTISHGPWIDEEYKIRGVLL
Protein: RPE-retinal G protein-coupled receptor (Q9Z2B3)
Organism: Mus musculus (Mouse)
Function: Receptor for all-trans- and 11-cis-retinal. Binds preferentially to the former and may catalyze the isomerization of the chromophore by a retinochrome-like mechanism (By similarity).
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Retinol dehydrogenase 10
- Short-wave-sensitive opsin 1
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Retinaldehyde-binding protein 1
- Retinoid isomerohydrolase
Sequence:
MAATRALPAGLGELEVLAVGTVLLMEALSGISLNGLTIFSFCKTPDLRTPSNLLVLSLALADTGISLNALVAAVSSLLRRWPHGSEGCQVHGFQGFATALASICGSAAVAWGRYHHYCTRRQLAWDTAIPLVLFVWMSSAFWASLPLMGWGHYDYEPVGTCCTLDYSRGDRNFISFLFTMAFFNFLVPLFITHTSYRFMEQKFSRSGHLPVNTTLPGRMLLLGWGPYALLYLYAAIADVSFISPKLQMVPALIAKTMPTINAINYALHREMVCRGTWQCLSPQKSKKDRTQ
Protein: Disintegrin and metalloproteinase domain-containing protein 17 (ADAM 17) (EC 3.4.24.86) (Snake venom-like protease) (TNF-alpha convertase) (TNF-alpha-converting enzyme) (CD antigen CD156b) (P78536)
Organism: Homo sapiens (Human)
Function: Cleaves the membrane-bound precursor of TNF-alpha to its mature soluble form. Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface. Responsible for the proteolytic release of several other cell-surface proteins, including p75 TNF-receptor, interleukin 1 receptor type II, p55 TNF-receptor, transforming growth factor-alpha, L-selectin, growth hormone receptor, MUC1 and the amyloid precursor protein. Acts as an activator of Notch pathway by mediating cleavage of Notch, generating the membrane-associated intermediate fragment called Notch extracellular truncation (NEXT). Plays a role in the proteolytic processing of ACE2. Plays a role in hemostasis through shedding of GP1BA, the platelet glycoprotein Ib alpha chain (By similarity). Mediates the proteolytic cleavage of LAG3, leading to release the secreted form of LAG3 (By similarity). Mediates the proteolytic cleavage of IL6R, leading to the release of secreted form of IL6R. Mediates the proteolytic cleavage and shedding of FCGR3A upon NK cell stimulation, a mechanism that allows for increased NK cell motility and detachment from opsonized target cells.
Subcellular location: Cell membrane {ECO:0000269|PubMed:36078095}; Single-pass type I membrane protein.
Interaction partners:
- Metalloproteinase inhibitor 3
- Inactive rhomboid protein 2
- Proheparin-binding EGF-like growth factor
- Disintegrin and metalloproteinase domain-containing protein 10
- Neurogenic locus notch homolog protein 1
- Tumor necrosis factor
- Neurogenic locus notch homolog protein 2
- Neurogenic locus notch homolog protein 3
- Furin
- Neurogenic locus notch homolog protein 4
Sequence:
MRQSLLFLTSVVPFVLAPRPPDDPGFGPHQRLEKLDSLLSDYDILSLSNIQQHSVRKRDLQTSTHVETLLTFSALKRHFKLYLTSSTERFSQNFKVVVVDGKNESEYTVKWQDFFTGHVVGEPDSRVLAHIRDDDVIIRINTDGAEYNIEPLWRFVNDTKDKRMLVYKSEDIKNVSRLQSPKVCGYLKVDNEELLPKGLVDREPPEELVHRVKRRADPDPMKNTCKLLVVADHRFYRYMGRGEESTTTNYLIELIDRVDDIYRNTSWDNAGFKGYGIQIEQIRILKSPQEVKPGEKHYNMAKSYPNEEKDAWDVKMLLEQFSFDIAEEASKVCLAHLFTYQDFDMGTLGLAYVGSPRANSHGGVCPKAYYSPVGKKNIYLNSGLTSTKNYGKTILTKEADLVTTHELGHNFGAEHDPDGLAECAPNEDQGGKYVMYPIAVSGDHENNKMFSNCSKQSIYKTIESKAQECFQERSNKVCGNSRVDEGEECDPGIMYLNNDTCCNSDCTLKEGVQCSDRNSPCCKNCQFETAQKKCQEAINATCKGVSYCTGNSSECPPPGNAEDDTVCLDLGKCKDGKCIPFCEREQQLESCACNETDNSCKVCCRDLSGRCVPYVDAEQKNLFLRKGKPCTVGFCDMNGKCEKRVQDVIERFWDFIDQLSINTFGKFLADNIVGSVLVFSLIFWIPFSILVHCVDKKLDKQYESLSLFHPSNVEMLSSMDSASVRIIKPFPAPQTPGRLQPAPVIPSAPAAPKLDHQRMDTIQEDPSTDSHMDEDGFEKDPFPNSSTAAKSFEDLTDHPVTRSEKAASFKLQRQNRVDSKETEC