wanglab/gogpt-training-data huggingface dataset:
Protein: Caspase-1 (CASP-1) (EC 3.4.22.36) (Interleukin-1 beta convertase) (IL-1BC) (Interleukin-1 beta-converting enzyme) (ICE) (IL-1 beta-converting enzyme) (p45) [Cleaved into: Caspase-1 subunit p20; Caspase-1 subunit p10] (P29452)
Organism: Mus musculus (Mouse)
Function: Thiol protease involved in a variety of inflammatory processes by proteolytically cleaving other proteins, such as the precursors of the inflammatory cytokines interleukin-1 beta (IL1B) and interleukin 18 (IL18) as well as the pyroptosis inducer Gasdermin-D (GSDMD), into active mature peptides. Plays a key role in cell immunity as an inflammatory response initiator: once activated through formation of an inflammasome complex, it initiates a pro-inflammatory response through the cleavage of the two inflammatory cytokines IL1B and IL18, releasing the mature cytokines which are involved in a variety of inflammatory processes. Cleaves a tetrapeptide after an Asp residue at position P1. Also initiates pyroptosis, a programmed lytic cell death pathway, through cleavage of GSDMD. In contrast to cleavage of interleukins IL1B and IL1B, recognition and cleavage of GSDMD is not strictly dependent on the consensus cleavage site but depends on an exosite interface on CASP1 that recognizes and binds the Gasdermin-D, C-terminal (GSDMD-CT) part. Cleaves and activates CASP7 in response to bacterial infection, promoting plasma membrane repair. Upon inflammasome activation, during DNA virus infection but not RNA virus challenge, controls antiviral immunity through the cleavage of CGAS, rendering it inactive. In apoptotic cells, cleaves SPHK2 which is released from cells and remains enzymatically active extracellularly (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21147462}. Cell membrane {ECO:0000250|UniProtKB:P29466}.
Interaction partners:
- Interferon-inducible protein AIM2
- Interleukin-1 beta
- Pyrin
- NLR family CARD domain-containing protein 4
- NACHT, LRR and PYD domains-containing protein 3
- Apoptosis-associated speck-like protein containing a CARD
- NACHT, LRR and PYD domains-containing protein 1a
- Gasdermin-D
- Caspase-8
- NACHT, LRR and PYD domains-containing protein 6
Sequence:
MADKILRAKRKQFINSVSIGTINGLLDELLEKRVLNQEEMDKIKLANITAMDKARDLCDHVSKKGPQASQIFITYICNEDCYLAGILELQSAPSAETFVATEDSKGGHPSSSETKEEQNKEDGTFPGLTGTLKFCPLEKAQKLWKENPSEIYPIMNTTTRTRLALIICNTEFQHLSPRVGAQVDLREMKLLLEDLGYTVKVKENLTALEMVKEVKEFAACPEHKTSDSTFLVFMSHGIQEGICGTTYSNEVSDILKVDTIFQMMNTLKCPSLKDKPKVIIIQACRGEKQGVVLLKDSVRDSEEDFLTDAIFEDDGIKKAHIEKDFIAFCSSTPDNVSWRHPVRGSLFIESLIKHMKEYAWSCDLEDIFRKVRFSFEQPEFRLQMPTADRVTLTKRFYLFPGH
Protein: Disintegrin and metalloproteinase domain-containing protein 1a (ADAM 1a) (EC 3.4.24.-) (Fertilin subunit alpha-a) (Q60813)
Organism: Mus musculus (Mouse)
Function: May be involved in sperm-egg fusion.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Disintegrin and metalloproteinase domain-containing protein 2
- Calmegin
Sequence:
MSVAAAGRGFASSLSSPQIRRIALKEAKLTPHIWAALHWNLGLRLVPSVRVGILVLLIFLPSTFCDIGSVYNSSYETVIPERLPGKGGKDPGGKVSYMLLMQGQKQLLHLEVKGHYPENNFPVYSYHNGILRQEMPLLSQDCHYEGYMEGVPGSFVSVNICSGLRGVLIKEETSYGIEPMLSSKNFEHVLYTMEHQPVVSCSVTPKDSPGDTSHPPRSRKPDDLLVLTDWWSHTKYVEMFVVVNHQRFQMWGSNINETVQAVMDIIALANSFTRGINTEVVLVGLEIWTEGDPIEVPVDLQTTLRNFNFWRQEKLVGRVRHDVAHLIVGHRPGENEGQAFLRGACSGEFAAAVEAFHHEDVLLFAALMAHELGHNLGIQHDHPTCTCGPKHFCLMGEKIGKDSGFSNCSSDHFLRFLHDHRGACLLDEPGRQSRMRRAANCGNGVVEDLEECDCGSDCDSHPCCSPTCTLKEGAQCSEGLCCYNCTFKKKGSLCRPAEDVCDLPEYCDGSTQECPANSYMQDGTQCDRIYYCLGGWCKNPDKQCSRIYGYPARSAPEECYISVNTKANRFGNCGHPTSANFRYETCSDEDVFCGKLVCTDVRYLPKVKPLHSLLQVPYGEDWCWSMDAYNITDVPDDGDVQSGTFCAPNKVCMEYICTGRGVLQYNCEPQEMCHGNGVCNNFKHCHCDAGFAPPDCSSPGNGGSVDSGPVGKPADRHLSLSFLAEESPDDKMEDEEVNLKVMVLVVPIFLVVLLCCLMLIAYLWSEVQEVVSPPSSSESSSSSSWSDSDSQ
Protein: Apolipoprotein B receptor (Apolipoprotein B-100 receptor) (Apolipoprotein B-48 receptor) (Apolipoprotein B48 receptor) (apoB-48R) (Q0VD83)
Organism: Homo sapiens (Human)
Function: Macrophage receptor that binds to the apolipoprotein B48 (APOB) of dietary triglyceride (TG)-rich lipoproteins (TRL) or to a like domain of APOB in hypertriglyceridemic very low density lipoprotein (HTG-VLDL). Binds and internalizes TRL when out of the context of the macrophage. May provide essential lipids to reticuloendothelial cells. Could also be involved in foam cell formation with elevated TRL and remnant lipoprotein (RLP). Mediates the rapid high-affinity uptake of chylomicrons (CM), HTG-VLDL, and trypsinized (tryp) VLDL devoid of APOE in vitro in macrophages.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10191299, ECO:0000269|PubMed:7619811}; Peripheral membrane protein {ECO:0000269|PubMed:10191299, ECO:0000269|PubMed:7619811}. Note=Binds monocyte-macrophage membrane. Thought to be anchored in the membrane through an interaction with an integral membrane protein.
Interaction partners:
- Apolipoprotein B-100
- Apolipoprotein A-V
Sequence:
MDFLRLYLPGLHQALRGALDSLGTFVSYLLGDAVPTVEREAQAAEELGVVAVGKTGKIVEEEAQEDLEGLRGSQNEGAGRLRGPGDDRRHEVGSSAVEQTWGWGDGSSHGSQAERQDSGAGETAKAARCQEPSAHLEARKKSKAGSGACQDRSGQAQERQESHEQEVNREERLRSWEQEEEEEEVRAREPGMARGAESEWTWHGETEGKAGAVGPKAAGDNREMEQGVREADAGETEEPGAEGAGKGEEVVVVEKACESTRAWGTWGPGAEPEDWGILGREEARTTPGREEARAILDGEEARTISGGEEAETASGGEEAETASGGEEAGTASGGEEAGIASGGEAGTASGGEEAGTASGGEEAGTASGGDEAWTTSGKEEADLLGVRQTEYGAVPGERLLEATGKVWVLEEEGDEEREAEVSPFPKQPQVLGTERTEEAAESQTAGREAVGGQEAGESFEGQVDLRGKEAEMRQDLGIRADRARMEELVQAEEAQEERGSSRDPVAELPSDGEAEGTADLEATPEARPEEELTGEESEAAQTSCGLLGVEWGGLTHSVTKGQGPELMGGAQTPTKQPEEREAGEVELMGVLALSKEEQERSLEAGPRHAGSVKPEASEAFPGAWENRTRKDMERGNTQEDAADGEQREEEETAGGQTLAAEAEGDRESELSEVPEAGGEGLTTQDAGCGTEEGEASVSENQELDGSTGADAGPCPSLGEAYARETEDEEAEADRTSRRGWRLQAVAVGLPDREDAQTGSVAAGIMGGDVVPHISAAGAGEALEGVLGQGWDSKEKEEAAAGEHAGGQEFGLEGSAEEEVTGRGSQVEAFESREGGPWGGRVEAEESAGAEDSCGLDPAGSQTARAEGMGAMVEAGGLLEKWTLLEEEAVGWQEREQREDSEGRCGDYHPEGEAPRLLDAEGLMVTGGRRAEAKETEPESLEHVRGQEEQPTHQAPAEAAPESVGEAETAEAMGSARGGAANSWSEAPLPGSLLDVSVPRSRVHLSRSSSQRRSRPSFRRTPAWEQQEEPPAPNPPEEELSAPEQRPLQLEEPLEPSPLRHDGTPVPARRRPLGHGFGLAHPGMMQELQARLGRPKPQ
Protein: FKBP-type peptidyl-prolyl cis-trans isomerase SlyD (PPIase) (EC 5.2.1.8) (Metallochaperone SlyD) (Q7CFU4)
Organism: Yersinia pestis
Function: Folding helper with both chaperone and peptidyl-prolyl cis-trans isomerase (PPIase) activities. Chaperone activity prevents aggregation of unfolded or partially folded proteins and promotes their correct folding. PPIases catalyze the cis-trans isomerization of Xaa-Pro bonds of peptides, which accelerates slow steps of protein folding and thus shortens the lifetime of intermediates. Both strategies lower the concentration of intermediates and increase the productivity and yield of the folding reaction.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Small ribosomal subunit protein uS2
- Small ribosomal subunit protein uS3
- Urease accessory protein UreG
- NADH-quinone oxidoreductase subunit C/D
- Similar to Escherichia coli FKBP-type 16 kDa peptidyl-prolyl cis-trans isomerase FkpB SW:FKBX_ECOLI
Sequence:
MKVTKDLVVSLAYQVRTEDGVLVDESPVSAPLDYLHGHGSLIAGLENALEGHEAGDSFDVRVNADEGYGSYDENLVQRVPKDVFMGVDELEVGMRFLADTDQGPVPVEITAVEDEHVVVDGNHMLAGQDLNFHVEVVAVREATEEELQHGHVHGEHDHHHEHGDGCCGGHGHDDHEHEHEHGKGGCGKSGGCGCH
Protein: CBBY-like protein (AtCbby) (EC 3.1.3.-) (Q94K71)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Highly selective xylulose-1,5-bisphosphate (XuBP) phosphatase. Shows also activity towards ribulose-1,5-bisphosphate (RuBP) and fructose-1,6-bisphosphate (FBP), but not towards fructose-6-phosphate (F6P) or ribulose-5-phosphate (Ru5P). Degrades xylulose-1,5-bisphosphate, a potent inhibitor of rubisco produced by the rubisco itself.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Haloacid dehalogenase-like hydrolase domain-containing protein At2g33255
- Peptidyl-prolyl cis-trans isomerase FKBP16-3, chloroplastic
- Catalytic/ hydrolase
- Haloacid dehalogenase-like hydrolase domain-containing protein Sgpp
- Calvin cycle protein CP12-1, chloroplastic
- 5-amino-6-
Sequence:
MATVKISLSLASLSPSSSSSSIQSKLSPSFIPNAAPAKAVKLRFNGKSLRAKPMVYRSSRSVGVTCSASSSLTTLPSALLFDCDGVLVDTEKDGHRISFNDTFKERDLNVTWDVDLYGELLKIGGGKERMTAYFNKVGWPEKAPKDEAERKEFIAGLHKQKTELFMVLIEKKLLPLRPGVAKLVDQALTNGVKVAVCSTSNEKAVSAIVSCLLGPERAEKIKIFAGDVVPKKKPDPAIYNLAAETLGVDPSKCVVVEDSAIGLAAAKAAGMTCIVTKSGYTADEDFENADAVFDCIGDPPEERFDLAFCGSLLRKQFVS
Protein: Transcription initiation factor IIA subunit 1 (General transcription factor IIA subunit 1) [Cleaved into: Transcription initiation factor IIA alpha chain (TFIIA p35 subunit); Transcription initiation factor IIA beta chain (TFIIA p19 subunit)] (Q99PM3)
Organism: Mus musculus (Mouse)
Function: TFIIA is a component of the transcription machinery of RNA polymerase II and plays an important role in transcriptional activation. TFIIA in a complex with TBP mediates transcriptional activity (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Transcription initiation factor IIA subunit 2
- TATA-box-binding protein
- Transcription initiation factor IIB
- TATA box-binding protein-like 1
- General transcription factor IIE subunit 1
- General transcription factor IIF subunit 2
- General transcription factor IIE subunit 2
- General transcription factor IIH subunit 4
- General transcription factor IIF subunit 1
- General transcription and DNA repair factor IIH helicase/translocase subunit XPB
Sequence:
MANSANTNTVPKLYRSVIEDVINDVRDIFLDDGVDEQVLMELKTLWENKLMQSRAVDGFHSEEQQLLLQVQQQHQPQQQQHHHHHHQHQQAQPQQTVPQQAQTQQVLIPASQQATAPQVIVPDSKLLQHMNASSITSAAATAATLALPAGVTPVQQLLTNSGQLLQVVRAANGAQYILQPQQSVVLQQQVIPQMQPGGVQAPVIQQVLAPLPGGISPQTGVIIQPQQILFTGNKTQVIPTTVAAPAPAQAPMPAAGQQQPQAQPAQQQAPLVLQVDGTGDTSSEEDEDEEEDYDDDEEEDKEKDGAEDGQVEEEPLNSEDDVSDEEGQELFDTENVVVCQYDKIHRSKNKWKFHLKDGIMNLNGRDYIFSKAIGDAEW
Protein: Major urinary protein (MUP) (allergen Cav p 1) (P83507)
Organism: Cavia porcellus (Guinea pig)
Function: Binds pheromones that are released from drying urine of males. These pheromones affect the sexual behavior of females (By similarity).
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
SEINGDWNTIALSAD
Protein: V-type proton ATPase subunit a, vacuolar isoform (V-ATPase a 1 subunit) (V-ATPase 95 kDa subunit) (Vacuolar pH protein 1) (Vacuolar proton pump a subunit) (Vacuolar proton translocating ATPase subunit a 1) (P32563)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments. Is present only in vacuolar V-ATPase complexes; enzymes containing this subunit have a 4-fold higher ratio of proton transport to ATP hydrolysis than complexes containing the Golgi/endosomal isoform and undergo reversible dissociation of V1 and V0 in response to glucose depletion.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095}.
Interaction partners:
- V-type proton ATPase subunit c
- V-type proton ATPase subunit e
- Vacuolar ATPase assembly integral membrane protein VPH2
- V-type proton ATPase subunit F
- V-type proton ATPase subunit C
- V-type proton ATPase subunit E
- V-type proton ATPase subunit G
- V-type proton ATPase subunit c'
- V-type proton ATPase subunit D
- V-type proton ATPase subunit B
Sequence:
MAEKEEAIFRSAEMALVQFYIPQEISRDSAYTLGQLGLVQFRDLNSKVRAFQRTFVNEIRRLDNVERQYRYFYSLLKKHDIKLYEGDTDKYLDGSGELYVPPSGSVIDDYVRNASYLEERLIQMEDATDQIEVQKNDLEQYRFILQSGDEFFLKGDNTDSTSYMDEDMIDANGENIAAAIGASVNYVTGVIARDKVATLEQILWRVLRGNLFFKTVEIEQPVYDVKTREYKHKNAFIVFSHGDLIIKRIRKIAESLDANLYDVDSSNEGRSQQLAKVNKNLSDLYTVLKTTSTTLESELYAIAKELDSWFQDVTREKAIFEILNKSNYDTNRKILIAEGWIPRDELATLQARLGEMIARLGIDVPSIIQVLDTNHTPPTFHRTNKFTAGFQSICDCYGIAQYREINAGLPTIVTFPFMFAIMFGDMGHGFLMTLAALSLVLNEKKINKMKRGEIFDMAFTGRYIILLMGVFSMYTGFLYNDIFSKTMTIFKSGWKWPDHWKKGESITATSVGTYPIGLDWAWHGTENALLFSNSYKMKLSILMGFIHMTYSYFFSLANHLYFNSMIDIIGNFIPGLLFMQGIFGYLSVCIVYKWAVDWVKDGKPAPGLLNMLINMFLSPGTIDDELYPHQAKVQVFLLLMALVCIPWLLLVKPLHFKFTHKKKSHEPLPSTEADASSEDLEAQQLISAMDADDAEEEEVGSGSHGEDFGDIMIHQVIHTIEFCLNCVSHTASYLRLWALSLAHAQLSSVLWTMTIQIAFGFRGFVGVFMTVALFAMWFALTCAVLVLMEGTSAMLHSLRLHWVESMSKFFVGEGLPYEPFAFEYKDMEVAVASASSSASS
Protein: Cyclin-D1-1 (Cyclin-delta-1) (Cyclin-d1) (G1/S-specific cyclin-D1-1) (CycD1;1) (P42751)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May activate cell cycle in the root apical meristem (RAM) and promote embryonic root (radicle) protrusion.
Interaction partners:
- Retinoblastoma-related protein 1
- Cyclin-dependent kinase B1-1
- Cyclin-dependent kinase B2-1
- Cyclin-dependent kinase A-1
- Cyclin-A3-4
- Cyclin-dependent kinase B2-2
- Cyclin-dependent kinase B1-2
- Transcription factor E2FA
- Wee1-like protein kinase
- Metalloendoproteinase 2-MMP
Sequence:
MRSYRFSDYLHMSVSFSNDMDLFCGEDSGVFSGESTVDFSSSEVDSWPGDSIACFIEDERHFVPGHDYLSRFQTRSLDASAREDSVAWILKVQAYYNFQPLTAYLAVNYMDRFLYARRLPETSGWPMQLLAVACLSLAAKMEEILVPSLFDFQVAGVKYLFEAKTIKRMELLVLSVLDWRLRSVTPFDFISFFAYKIDPSGTFLGFFISHATEIILSNIKEASFLEYWPSSIAAAAILCVANELPSLSSVVNPHESPETWCDGLSKEKIVRCYRLMKAMAIENNRLNTPKVIAKLRVSVRASSTLTRPSDESSFSSSSPCKRRKLSGYSWVGDETSTSN
Protein: Glandular kallikrein-12, submandibular/renal (EC 3.4.21.35) (RSKG-3) (Tissue kallikrein) (P36376)
Organism: Rattus norvegicus (Rat)
Function: Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin.
Interaction partners:
- Serine protease inhibitor A3K
- Kininogen-1
Sequence:
MWLQILFLVLSVGRIDAAPPGQSRVVGGYKCEKNSQPWQVAVINRYLCGGVLIDPSWVITAAHCYSHNYHVLLGRNNLFKDEPFAQYRVVNQSFPHPDYNPFFMKNHTLFPGDDHSNDLMLLHLSEPADITDGVKVIDLPTEEPKVGSTCLASGWSSTKPLEWEFPDDLQCVNINILSNEKCIKAHTQMVTDVMLCAGELEGGKDTCNGDSGGPLLCDGVLQGITSWSSVPCGETNRPAIYTKLIKFTSWIKEVMKENS
Protein: Major urinary protein 4 (MUP 4) (P11590)
Organism: Mus musculus (Mouse)
Function: Binds pheromones, likely to displace pheromones complexed to urinary MUPs and transport them to the vomeronasal organ (VNO) where they associate with their neuronal receptor(s). MUP4 is highly specific for the male mouse pheromone 2-sec-butyl-4,5-dihydrothiazole (SBT).
Subcellular location: Secreted.
Interaction partners:
- Major urinary protein 5
- Major urinary protein 3
Sequence:
MKLLLCLGLTLVCIHAEEATSKGQNLNVEKINGEWFSILLASDKREKIEEHGSMRVFVEHIHVLENSLAFKFHTVIDGECSEIFLVADKTEKAGEYSVMYDGFNTFTILKTDYDNYIMFHLINEKDGKTFQLMELYGRKADLNSDIKEKFVKLCEEHGIIKENIIDLTKTNRCLKARE
Protein: Peptidyl-prolyl cis-trans isomerase (PPIase) (EC 5.2.1.8) (Q57WF8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Large ribosomal subunit protein uL3m
- 50S ribosomal protein L13, putative
- Large ribosomal subunit protein uL15/eL18 domain-containing protein
- Ribosomal protein L11, putative
- 50S ribosomal protein L14, putative
- AMP-dependent synthetase/ligase domain-containing protein
- KOW domain-containing protein
- Large ribosomal subunit protein bL21m
- 50S ribosomal protein L17, putative
- Large ribosomal subunit protein uL29m
Sequence:
MLHRTRLAQLINGRILQYFVPYERDEVNPVVFMDVTVEGDALGRVSVELFHDIVPKTTENFRSLCTGERGYSQCPLFYKGIPFHRVIPGFIVQGGDILLKDGRGNVSVFGFPFPDESFEGKAGKHLRGTVAMAHSAPNQNGSQFFFNLARNDHLDGKFVVCGQVIDGWEVVDRVAVLSGSSCGTPVSRAWITECGQSSGDKLEDTERALSGERALHTMPGKEVLDILSPRY
Protein: Glycerol-3-phosphate acyltransferase 4, isoform B (EC 2.3.1.15) (LD39624p) (Q960R0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MIAVLLDIFWIPIGGFLSFLIFISAINKSIGVRKAYVNLLLRIFEYGRVSIETASKENQHIQNPKTDDKQGVQLVDDADSKEGTNGATLITRDAVLLPQPQEPAPEKPVSSTKDEINFDFEKCLDYVKSGVEAIIEDDVTSRFEAEELKSWNMLTRTNRHYEFISWKITSIWVFGFFIRYVILMPLRVLVCFVGVVWLTVCTAAVGYLKDGPFKRDLVHKVLGMCFGVLSSAISAVITYHNEDNRPSSGICVANHTSPIDVLVLMCDSTYSLIGQRHGGFLGVLQRALARASPHIWFERGEAKDRHLVAERLKQHVSDPNNPPILIFPEGTCINNTSVMQFKKGSFEVGGVIYPVAIKYDPRFGDAFWNSAKYSMMQYLYMMMTSWAIVCDVWYLPPMYRQEGESAIDFANRVKSVIAKQGGLIDLVWDGQLKRMKPKKEWREIQQVEFANRLKSDST
Protein: Uncharacterized protein C1orf21 (Cell proliferation-inducing gene 13 protein) (Q9H246)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGCASAKHVATVQNEEEAQKGKNYQNGDVFGDEYRIKPVEEVKYMKNGAEEEQKIAARNQENLEKSASSNVRLKTNKEVPGLVHQPRANMHISESQQEFFRMLDEKIEKGRDYCSEEEDIT
Protein: BcDNA.LD23181 (Egg-derived tyrosine phosphatase (EC 3.1.3.48, EC 3.1.3.64)) (Q9NDR1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MCSLTPNHMVNVTQQHLHDLLETFEKKSFEAAAFEEGTAEYDISKKCEYLFKLDYSLIELDNTNGLLSPRYPGRILIPEYEHGHMAKTLVPGNGLFGQVGGGVGGGGSSGTTATATPLNSSAGSTGSEGVGIQAFVTFANPLQTQQQHPLQQQYPSQQMHPLHAQYPSQQPHPLQQQQQQPSQQQPQNTIYEDQYDIQRMRELVTMAKYARCRQRFAVPVIMYRGKYICRSATLSVMPETYGRKVVDYAYDCLSGGNYTAPNGEENDADSTDESLITHMHDQAQSQFSYDEVIKSDIQLLHTLNVSTIVDLMVENRKIKYFMAVSSSEKADPNKHYKSFNLLSLPYPGCEFFKKFRDNNYMARNLHYNWKQTFNDANINIPNMGPAADIDVAWSEYRDWDLVAITQNYLRATLKYVQEENSGLLIHCISGWDRTPLFVSLVRLSLWADGLIHQSLNAMQMAYFTLAYDWYLFGHQLPDRLKRGEDIMFFCFHVLKFITDEEFSIVEHRKRTKTSSSSGSSVIVIKSDCCDDEPLKEDYILSFDQDSNDSYSNCSNCDMSITDNFYATTPAQVNPLTSRSPNPKRSRTSPISVPGSNARQRQESTSSNGSWQVVTDTGSIDSMMNGSYMMRFVAQQAADGGGSSNIPLCNGGNGYHCSINAASSGSGSGSGSSISNGSSTHGFANGSSKDVGGSTMASKQCINLRKQRLNAVRAIFIQAYGKTIGLKFKEGSSMNLATFIGNLADQLF
Protein: Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2 (Oligosaccharyl transferase delta subunit) (Ribophorin II) (RPN-II) (Ribophorin-2) (P91390)
Organism: Caenorhabditis elegans
Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit stt-3
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit dad-1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
- Probable dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 3
- Translocon Sec61/SecY plug domain-containing protein
- Protein transport protein Sec61 subunit gamma
- Dol-P-Glc:Glc
- Malectin domain-containing protein
- Mannosyl-oligosaccharide glucosidase
Sequence:
MKLLLVLLTIASVALAAVDDVAVNNFKVGILAKDQQPSDENLKTVALFSKLPNELKADASQRLYVSFTVAKKSDNAKVKPHQVFLRFVAQNGEDVVVVVNPDANGNYVYDNVLRTAAKSFRNLSGQFKISLLVGDVTIKNPINWQFANIDAALPVAYEPTPKSQQVHFEPLNEISHIFRQPEKRPSALISDLFTIICLSPLLILVVLWSQVGINFQNAPASPWVPIFHVGLIGIFGIYFMFWVQFDMFVTLKYLAVLGFLTFVAGNRVLRAISESKQKSE
Protein: Nitrite reductase (NADH) large subunit (EC 1.7.1.15) (P08201)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Nitrite reductase small subunit
- Respiratory nitrate reductase 1 alpha chain
- Nitrate/nitrite antiporter NarK
- Cytochrome c-552
- Periplasmic nitrate reductase
- Respiratory nitrate reductase 1 beta chain
- Hydroxylamine reductase
- Glutamine synthetase
- Siroheme synthase
- Respiratory nitrate reductase 1 gamma chain
Sequence:
MSKVRLAIIGNGMVGHRFIEDLLDKSDAANFDITVFCEEPRIAYDRVHLSSYFSHHTAEELSLVREGFYEKHGIKVLVGERAITINRQEKVIHSSAGRTVFYDKLIMATGSYPWIPPIKGSDTQDCFVYRTIEDLNAIESCARRSKRGAVVGGGLLGLEAAGALKNLGIETHVIEFAPMLMAEQLDQMGGEQLRRKIESMGVRVHTSKNTLEIVQEGVEARKTMRFADGSELEVDFIVFSTGIRPRDKLATQCGLDVAPRGGIVINDSCQTSDPDIYAIGECASWNNRVFGLVAPGYKMAQVAVDHILGSENAFEGADLSAKLKLLGVDVGGIGDAHGRTPGARSYVYLDESKEIYKRLIVSEDNKTLLGAVLVGDTSDYGNLLQLVLNAIELPENPDSLILPAHSGSGKPSIGVDKLPDSAQICSCFDVTKGDLIAAINKGCHTVAALKAETKAGTGCGGCIPLVTQVLNAELAKQGIEVNNNLCEHFAYSRQELFHLIRVEGIKTFEELLAKHGKGYGCEVCKPTVGSLLASCWNEYILKPEHTPLQDSNDNFLANIQKDGTYSVIPRSPGGEITPEGLMAVGRIAREFNLYTKITGSQRLAMFGAQKDDLPEIWRQLIEAGFETGHAYAKALRMAKTCVGSTWCRYGVGDSVGLGVELENRYKGIRTPHKMKFGVSGCTRECSEAQGKDVGIIATEKGWNLYVCGNGGMKPRHADLLAADIDRETLIKYLDRFMMFYIRTADKLTRTAPWLENLEGGIDYLKAVIIDDKLGLNAHLEEEMARLREAVLCEWTETVNTPSAQTRFKHFINSDKRDPNVQMVPEREQHRPATPYERIPVTLVEDNA
Protein: Pannexin-1 [Cleaved into: Caspase-activated pannexin-1 (Caspase-activated PANX1)] (Q9JIP4)
Organism: Mus musculus (Mouse)
Function: Structural component of the gap junctions and the hemichannels. May play a role as a Ca(2+)-leak channel to regulate ER Ca(2+) homeostasis (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:22311122, ECO:0000269|PubMed:30814251}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00351}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q96RD7}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00351}.
Interaction partners:
- P2X purinoceptor 7
- Caspase-1
- Pannexin-2
- NACHT, LRR and PYD domains-containing protein 3
- P2X purinoceptor 4
- P2X purinoceptor 1
- Calcium homeostasis modulator protein 1
- Voltage-gated potassium channel subunit beta-3
- Gap junction beta-2 protein
- NACHT, LRR and PYD domains-containing protein 1a
Sequence:
MAIAHLATEYVFSDFLLKEPTEPKFKGLRLELAVDKMVTCIAVGLPLLLISLAFAQEISIGTQISCFSPSSFSWRQAAFVDSYCWAAVQQKSSLQSESGNLPLWLHKFFPYILLLFAILLYLPALFWRFSAAPHLCSDLKFIMEELDKVYNRAIKAAKSARDLDLRDGPGPPGVTENVGQSLWEISESHFKYPIVEQYLKTKKNSSHLIMKYISCRLVTFVVILLACIYLSYYFSLSSLSDEFLCSIKSGVLKNDSTIPDRFQCKLIAVGIFQLLSLINLIVYALLIPVVVYTFFIPFRQKTDILKVYEILPTFDVLHFKSEGYNDLSLYNLFLEENISELKSYKCLKVLENIKSNGQGIDPMLLLTNLGMIKMDIIDGKIPTSLQTKGEDQGSQRVEFKDLDLSSEAAANNGEKNSRQRLLNPSC
Protein: Protein YIF1 (Q8MTA2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU368073}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU368073}. Golgi apparatus membrane {ECO:0000256|RuleBase:RU368073}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU368073}.
Interaction partners:
Sequence:
MNYNPNPASAAGRPRPPKRVSDVNAMGSSAPMMGGGATFMAPPTGPGILDPNMYGAPAPAPVNSYGFDPNLGQPSQHIQQPPQQQPGYGYGAPPPQQAAGPPTYGIGAPQPVAPPTGQYPQFAMFQQPIVQDMAMQYGQKLADQGKQIMENQFEKWVPVAKLKYYFAVDNAYVGRKLRLLFFPYMHKDWSLRYDQEHPVQPRYDVNAPDLYLPTMGYITYVIVAGLLLGMQKRFSPEQLGIQASSAMAYSIFELVIYSLALYVMNVKTSLKTLDLLAFTGYKYVNIVVCLMVSTLFFKSGYYIALAYTSFSFGFFMLRTLRTKLLQDNSPAAPSGAINYDPYGNPQQFDYSGGKKRKLYFLFMIVAGQALFAFLLSKHLYLPEAEVLTVPKTF
Protein: Cell differentiation family, Rcd1-like protein (Q553Y8)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- NOT2/NOT3/NOT5 family protein
- Uncharacterized protein
- NOT2/NOT3/NOT5 family protein
- Endonuclease/exonuclease/phosphatase domain-containing protein
- poly
- poly
- RING zinc finger-containing protein
- CCR4-NOT transcription complex subunit 11
- DEAD/DEAH box helicase
- Uncharacterized protein
Sequence:
MINNLRNNSSVDKDCEIYFKNEYKINNNNNNNNNNNNNNKIHNNTISLNSNPSQSPSHAISESKFFKPTPSSNSVLNPYFSSNYFVGNSFFNSSRLNNTGGDNSINNNNNNININNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNSSISSIINSHSNNNYKNNFLNIVEEKSQIKNNQISKEFPQTLTLDFNSFCSNIDFNSNDVLSNSFLNNLVINKTNNNNNENNNNHNNNHNNNHNKYNNNNNNINNNNNIINNYNNNNNNNSNINNNNNSIKFNNNINSNKNNTSNNLFFKQNQHDDFDEEEDDRALSSMVSKIVDGESDTLELYYDKNGFGSNSQNKIEKVNNTTTTTTTTTSITALNNTLSTNNKINNNSSPFKSNNTKFNHQKNKHKNGGINNYNLNISNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNTDTNTNNHNHNHNIIINNSINNNNNNNLFNNGNSNISQNGSHSITSKLQIKIEDKTDHQLISDLLEPQKREEALCEIVKRKDSIPSLASLVWFTPCVISVLLQEIMNLYNFISPPNPKLKARASNKVCNILNIFQVIASDPETRSLFIQAKVISYIYPYLSTNSKSKPFEYLRLTTLGVINTVIKQESQDIINYLIEIDISTPCLKIMENGNDLSKTASAFILQKILNWDDGLNYFVQSPKRLSDLTNCLKYMVEAMIPDHMSSRLLKHIVRCYLRLSENLKIRDQLIGWMPTCFSNGQLNDFIQKEGDVIVKRWFTQLLGNLYPTQHSNNKRHQSSSSSQQQQQQQQQQQQQQQQQQQQQQQHHHHHHHQQHIKPSTISSQQKTTVPSSTQSQSLIPFSSVISNNSNNENSNINNSNSNNNNNNNNNNNNNNNNNNNNNNNNNNIFSHSRSNGRTKNNNESSENNNNNNNIYRLPSRGSPFQ