wanglab/gogpt-training-data huggingface dataset:
Protein: NADH:ubiquinone reductase (non-electrogenic) (EC 1.6.5.9) (Q8I302)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Cytochrome b-c1 complex subunit Rieske, putative
- Cytochrome b
- Cytochrome c oxidase subunit 3
- Cytochrome c oxidase subunit 1
- Cytochrome c oxidase subunit 2, putative
- Cytochrome c oxidase polypeptide II
- Lysine--tRNA ligase
- Phosphoglycerate mutase
Sequence:
MLVKFRKCGQANIFRSISNVRKIYNVAKNNLKNNKDIERKEKIIILGSGWGGFNFLLNIDFKKYDVTLISPRNYFTFTPLLPCLCSGTLSVNVCTESIRNFLRKKNGYCGNYLQLECTDVFYEDKYINCIDIENNKVKLFYDYLIIAVGAKTNTFNINGVDKYAYFVKDIDDALKIRKKFLDILEKCTLPNISNEEKKKMLHVAVVGGGPTGVEVTAEFADFINKEVKINYKDIFNFISISIIEGGNNLLPTFTQNISDFTKENFHNLNINVLTNYYVIDVDKHSFHIQSSLNKNEKKKLSYGLLIWASGLAQTTLIQKFLKTIPVQANNAILKVDEKLRVIGIPSNNIYAIGDCKKIQPKLLHEHTNEIIKILTGNKLTSEALKLKQSELTKTFPQLSISKWDYEKNKKGEMTPQQFHDYLFEIDKNYKSPTPTAQNAKQEAYYLSNVFNNFIHTNQKFNIPSFIEKWKGSLAYIGNHQVVADLPYYELKGGRFSSTFWKVVYIQLLLSWKSRFHFFIDFIKTKWYGRPFIK
Protein: Melanopsin opn4m3 (Opsin 4b) (G8Z411)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU004951}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU004951}.
Interaction partners:
Sequence:
MNASRSLSMGIPTQVANSTAVSDSLAPWNYSAVSAHKLMELPARATTVAMVQDVRHPFPTVDVPDHAHYTIGSVILAVGITGMVGNLLVMYAFCKSRSLRTPANMFIINLAVTDFLMCVTQTPIFFTTSLHKRWIFGEKGCELYAFCGALFGICSMITLMIIAVDRYFVITRPLASIGVMSRKRALLILSAAWAYSMGWSLPPFFGWSAYVPEGLLTSCSWDYMTFSPSVRAYTMLLFTFVFFIPLFVIIYCYFFIFKAIRETNRAVGKINGEGGPRDSIKKIHRMKNEWKMAKIALIVILLYVISWSPYSCVALTAFAGYADMLTPYMNSVPAVIAKASAIHNPIIYAITHPKYRSAIAKYIPCLGVLLCVPRRDRFSSSSFISTRRSTLTSQSSETSSNLHRAGKARLSSVSDSESGWTDTEADLSTASSRPASRQVSSEIRKDLCDIKHSSSLRLKVKSRDSGIFDRTSAQSLADPSTNRPCAYISTVGDKDEISMAEVSLSSCPSSSQNDVSEKADEKRPLVRIPSIIVTSETCPAVLPAGHSSRLIPGAPAVTDSVTVTD
Protein: Golgi reassembly stacking protein 1 (cDNA FLJ32481 fis, clone SKNMC2001113, moderately similar to Golgi reassembly-stacking protein 1) (B3KPY8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGLGVSAEQPAGGAEGFHLHGDVEPSSPAALAGLRPYTDYVVGSDQILQEPPSYHKKPPGTPPPSALPLGAPPPDALPPGPTPEDSPSLETGSRQSDYMEALLQAPGSSMEDPLPGPGSPSHSAPDPDGLPHFMETPLQPPPPVQRVMDPGFLDVSGISLLDNSNASVWPSLPSSTELTTTAVSTSGPEDICSSSSSHERGGEATWSGSEFEVSFLDSPGAQAQADHLPQLTLPDSLTSAASPEDGLSAELLEAQAEEEPASTEGLDTGTEAEGLDSQAQISTTE
Protein: Anaphase-promoting complex subunit 1 (APC1) (Cyclosome subunit 1) (Mitotic checkpoint regulator) (Testis-specific gene 24 protein) (Q9H1A4)
Organism: Homo sapiens (Human)
Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains.
Interaction partners:
- Anaphase-promoting complex subunit 10
- Anaphase-promoting complex subunit 7
- Cell division cycle protein 27 homolog
- Anaphase-promoting complex subunit CDC26
- Mitotic checkpoint serine/threonine-protein kinase BUB1 beta
- Cell division cycle protein 23 homolog
- Anaphase-promoting complex subunit 16
- Anaphase-promoting complex subunit 2
- Anaphase-promoting complex subunit 5
- Cell division cycle protein 20 homolog
Sequence:
MSNFYEERTTMIAARDLQEFVPFGRDHCKHHPNALNLQLRQLQPASELWSSDGAAGLVGSLQEVTIHEKQKESWQLRKGVSEIGEDVDYDEELYVAGNMVIWSKGSKSQALAVYKAFTVDSPVQQALWCDFIISQDKSEKAYSSNEVEKCICILQSSCINMHSIEGKDYIASLPFQVANVWPTKYGLLFERSASSHEVPPGSPREPLPTMFSMLHPLDEITPLVCKSGSLFGSSRVQYVVDHAMKIVFLNTDPSIVMTYDAVQNVHSVWTLRRVKSEEENVVLKFSEQGGTPQNVATSSSLTAHLRSLSKGDSPVTSPFQNYSSIHSQSRSTSSPSLHSRSPSISNMAALSRAHSPALGVHSFSGVQRFNISSHNQSPKRHSISHSPNSNSNGSFLAPETEPIVPELCIDHLWTETITNIREKNSQASKVFITSDLCGQKFLCFLVESQLQLRCVKFQESNDKTQLIFGSVTNIPAKDAAPVEKIDTMLVLEGSGNLVLYTGVVRVGKVFIPGLPAPSLTMSNTMPRPSTPLDGVSTPKPLSKLLGSLDEVVLLSPVPELRDSSKLHDSLYNEDCTFQQLGTYIHSIRDPVHNRVTLELSNGSMVRITIPEIATSELVQTCLQAIKFILPKEIAVQMLVKWYNVHSAPGGPSYHSEWNLFVTCLMNMMGYNTDRLAWTRNFDFEGSLSPVIAPKKARPSETGSDDDWEYLLNSDYHQNVESHLLNRSLCLSPSEASQMKDEDFSQNLSLDSSTLLFTHIPAIFFVLHLVYEELKLNTLMGEGICSLVELLVQLARDLKLGPYVDHYYRDYPTLVRTTGQVCTIDPGQTGFMHHPSFFTSEPPSIYQWVSSCLKGEGMPPYPYLPGICERSRLVVLSIALYILGDESLVSDESSQYLTRITIAPQKLQVEQEENRFSFRHSTSVSSLAERLVVWMTNVGFTLRDLETLPFGIALPIRDAIYHCREQPASDWPEAVCLLIGRQDLSKQACEGNLPKGKSVLSSDVPSGTETEEEDDGMNDMNHEVMSLIWSEDLRVQDVRRLLQSAHPVRVNVVQYPELSDHEFIEEKENRLLQLCQRTMALPVGRGMFTLFSYHPVPTEPLPIPKLNLTGRAPPRNTTVDLNSGNIDVPPNMTSWASFHNGVAAGLKIAPASQIDSAWIVYNKPKHAELANEYAGFLMALGLNGHLTKLATLNIHDYLTKGHEMTSIGLLLGVSAAKLGTMDMSITRLLSIHIPALLPPTSTELDVPHNVQVAAVVGIGLVYQGTAHRHTAEVLLAEIGRPPGPEMEYCTDRESYSLAAGLALGMVCLGHGSNLIGMSDLNVPEQLYQYMVGGHRRFQTGMHREKHKSPSYQIKEGDTINVDVTCPGATLALAMIYLKTNNRSIADWLRAPDTMYLLDFVKPEFLLLRTLARCLILWDDILPNSKWVDSNVPQIIRENSISLSEIELPCSEDLNLETLSQAHVYIIAGACLSLGFRFAGSENLSAFNCLHKFAKDFMTYLSAPNASVTGPHNLETCLSVVLLSLAMVMAGSGNLKVLQLCRFLHMKTGGEMNYGFHLAHHMALGLLFLGGGRYSLSTSNSSIAALLCALYPHFPAHSTDNRYHLQALRHLYVLAAEPRLLVPVDVDTNTPCYALLEVTYKGTQWYEQTKEELMAPTLLPELHLLKQIKVKGPRYWELLIDLSKGTQHLKSILSKDGVLYVKLRAGQLSYKEDPMGWQSLLAQTVANRNSEARAFKPETISAFTSDPALLSFAEYFCKPTVNMGQKQEILDLFSSVLYECVTQETPEMLPAYIAMDQAIRRLGRREMSETSELWQIKLVLEFFSSRSHQERLQNHPKRGLFMNSEFLPVVKCTIDNTLDQWLQVGGDMCVHAYLSGQPLEESQLSMLACFLVYHSVPAPQHLPPIGLEGSTSFAELLFKFKQLKMPVRALLRLAPLLLGNPQPMVM
Protein: Diacylglycerol O-acyltransferase 2 (EC 2.3.1.20) (Acyl-CoA retinol O-fatty-acyltransferase) (ARAT) (Retinol O-fatty-acyltransferase) (EC 2.3.1.76) (Diglyceride acyltransferase 2) (Q5FVP8)
Organism: Rattus norvegicus (Rat)
Function: Essential acyltransferase that catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. Required for synthesis and storage of intracellular triglycerides (By similarity). Probably plays a central role in cytosolic lipid accumulation. In liver, is primarily responsible for incorporating endogenously synthesized fatty acids into triglycerides (By similarity). Functions also as an acyl-CoA retinol acyltransferase (ARAT) (By similarity). Also able to use 1-monoalkylglycerol (1-MAkG) as an acyl acceptor for the synthesis of monoalkyl-monoacylglycerol (MAMAG) (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q96PD7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q96PD7}. Lipid droplet {ECO:0000250|UniProtKB:Q96PD7}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q96PD7}.
Interaction partners:
- Diacylglycerol O-acyltransferase 1
- Patatin-like phospholipase domain-containing protein 2
- Long-chain fatty acid transport protein 1
- phosphatidate phosphatase
- Phospholipid phosphatase 2
- phosphatidate phosphatase
- Acylglycerol transacylase
- Phospholipid phosphatase 3
- phosphatidate phosphatase
- Pancreatic triacylglycerol lipase
Sequence:
MKTLIAAYSGVLRGERRAEAARSENKNKGSALSREGSGRWGTGSSILSALQDIFSVTWLNRSKVEKHLQVISVLQWVLSFLVLGVACSVILMYTFCTDCWLIAALYFTWLAFDWNTPKKGGRRSQWVRNWAVWRYFRDYFPIQLVKTHNLLTTRNYIFGYHPHGIMGLGAFCNFSTEATEVSKKFPGIRPYLATLAGNFRMPVLREYLMSGGICPVNRDTIDYLLSKNGSGNAIVIVVGGAAESLSSMPGKNAVTLRNRKGFVKLALRHGADLVPTYSFGENEVYKQVIFEEGSWGRWVQKKFQKYIGFAPCIFHGRGLFSSDTWGLVPYSKPITTVVGEPITVPKLEHPTQKDIDLYHTMYMEALVKLFDNHKTKFGLPETEVLEVN
Protein: Uncharacterized protein (G8BJX3)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Subcellular location: Secreted, cell wall {ECO:0000256|ARBA:ARBA00004191}.
Interaction partners:
- protein-tyrosine-phosphatase
- protein-tyrosine-phosphatase
- SH3 domain-containing protein
- glucan endo-1,3-beta-D-glucosidase
- Vacuolar membrane protein
Sequence:
MLYKTIISTALLAQALAAPLAINQQQHQHHKHNEEKRAVHVVTQTNVVVVTLGNGDATTTFSPVSAETHASEASQVTDAPQVQPTTTADASSNDDDSTSSSSSASDSTSSSSSNVGSGGAKGVTYTPYADNGNCKTSSQIASEVAELSGFDVIRLYGVDCDQVAQVLQAKASGQKIFAGIYDVSAISDGVQTIADAVKAHGSWDDIHTVSVGNELVNSGQANPSQIKSYVNQAKSALKSAGYNGSVVSVDTFIAVINNPELCDYSDYIAVNAHCFFDGYYTADQAGEWVLSQIQRVSTACGNSKNVLITETGWPSRGDSNNKAVPSKENQEAAIQSIKDTCGSASILFTAFNDLWKADGPYNAEKYWGFLSN
Protein: Sister chromatid cohesion protein DCC1 (Defective in sister chromatid cohesion protein 1) (P25559)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the RFC-like complex CTF18-RFC which is required for efficient establishment of chromosome cohesion during S-phase and may load or unload POL30/PCNA. During a clamp loading circle, the RFC:clamp complex binds to DNA and the recognition of the double-stranded/single-stranded junction stimulates ATP hydrolysis by RFC. The complex presumably provides bipartite ATP sites in which one subunit supplies a catalytic site for hydrolysis of ATP bound to the neighboring subunit. Dissociation of RFC from the clamp leaves the clamp encircling DNA.
Interaction partners:
- Chromosome transmission fidelity protein 18
- Replication factor C subunit 5
- Chromosome transmission fidelity protein 8
- Replication factor C subunit 2
- Replication factor C subunit 3
- Replication factor C subunit 4
- DNA polymerase epsilon catalytic subunit A
- Chromosome segregation in meiosis protein 3
- DNA polymerase alpha-binding protein
- Checkpoint protein RAD24
Sequence:
MSINLHSAPEYDPSYKLIQLTPELLDIIQDPVQNHQLRFKSLDKDKSEVVLCSHDKTWVLKQRKHSNTVLLMREFVPEQPITFDETLLFGLSKPYMDVVGFAKTESEFETRETHGELNLNSVPIYNGELDFSDKIMKRSSTKVIGTLEELLENSPCSALEGISKWHKIGGSVKDGVLCILSQDFLFKALHVLLMSAMAESLDLQHLNVEDTHHAVGKDIEDEFNPYTREIIETVLNKFAVQEQEAENNTWRLRIPFIAQWYGIQALRKYVSGISMPIDEFLIKWKSLFPPFFPCDIDIDMLRGYHFKPTDKTVQYIAKSTLPMDPKERFKVLFRLQSQWDLEDIKPLIEELNSRGMKIDSFIMKYARRKRLGKKTVVTSR
Protein: Lysine-specific permease LysP (Lysine transporter LysP) (Trigger transporter LysP) (P25737)
Organism: Escherichia coli (strain K12)
Function: Permease involved in lysine uptake. In addition, functions as a lysine sensor that mediates the lysine-dependent regulation of the transcriptional activator CadC. In the absence of lysine, or at low lysine concentrations, LysP inhibits CadC by an interaction with the transmembrane domain of CadC. In the presence of lysine, LysP loses its ability to interact with and inhibit CadC, and acts as a lysine permease.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:7551055}; Multi-pass membrane protein {ECO:0000269|PubMed:7551055}.
Interaction partners:
- Transcriptional activator CadC
- Aspartate aminotransferase
- ATP-dependent Clp protease ATP-binding subunit ClpX
- Malate dehydrogenase
- HTH-type transcriptional regulator ZntR
- Beta-glucuronidase
- Long-chain-fatty-acid--CoA ligase
- Uncharacterized HTH-type transcriptional regulator YeiE
- Isocitrate dehydrogenase
Sequence:
MVSETKTTEAPGLRRELKARHLTMIAIGGSIGTGLFVASGATISQAGPGGALLSYMLIGLMVYFLMTSLGELAAYMPVSGSFATYGQNYVEEGFGFALGWNYWYNWAVTIAVDLVAAQLVMSWWFPDTPGWIWSALFLGVIFLLNYISVRGFGEAEYWFSLIKVTTVIVFIIVGVLMIIGIFKGAQPAGWSNWTIGEAPFAGGFAAMIGVAMIVGFSFQGTELIGIAAGESEDPAKNIPRAVRQVFWRILLFYVFAILIISLIIPYTDPSLLRNDVKDISVSPFTLVFQHAGLLSAAAVMNAVILTAVLSAGNSGMYASTRMLYTLACDGKAPRIFAKLSRGGVPRNALYATTVIAGLCFLTSMFGNQTVYLWLLNTSGMTGFIAWLGIAISHYRFRRGYVLQGHDINDLPYRSGFFPLGPIFAFILCLIITLGQNYEAFLKDTIDWGGVAATYIGIPLFLIIWFGYKLIKGTHFVRYSEMKFPQNDKK
Protein: Chromatin assembly factor 1 subunit A (CAF-1 subunit A) (CAF-1 90 kDa subunit) (Chromatin assembly factor 1 subunit p90) (RAP1 localization factor 2) (Q12495)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acts as a component of chromatin assembly factor 1 (CAF-1), which assembles histone octamers onto replicating DNA in vitro. It performs the first step of the nucleosome assembly process, bringing newly synthesized histones H3 and H4 to replicating DNA; histones H2A/H2B can bind to this chromatin precursor subsequent to DNA replication to complete the histone octamer. p90 may facilitate the efficient and timely assembly of histones into telomeric chromatin.
Subcellular location: Nucleus.
Interaction partners:
- Histone-binding protein MSI1
- Chromatin assembly factor 1 subunit B
- Origin recognition complex subunit 3
- Histone chaperone ASF1
- Origin recognition complex subunit 6
- Origin recognition complex subunit 5
- Histone chaperone RTT106
- Protein HIR1
- Histone H3
- Proliferating cell nuclear antigen
Sequence:
MEQHLKSIPLQDDTKKKGILSFFQNTTTVKSNKFLTKEKDVITLDDPKEDVSGPMIETVKQETMKSINKECADEMKTTPKKANAEDKLLCYKNSPIQSTKYDRNTNKQVPNGNIIAIETKSRSSSPCSKRELSSSKKEEAKREKELKKQQRAEEKHRKELLRQEEKKKKELKVEEERQRRAELKKQKEEEKRRKEEARLEAKRRKEEERLKKEEEIRLKEEAKERAQSRIGNFFKKLSDSNTPVVEKSDYEKFFLPFYAKDGVRVSNKWKLTKVELEGSKRKIDDELLNSKDKTSSDDLLNWLQSRRLPRGHKIKRKAVDVLQQMPLKEKTDDELQSLLAQVPHKYIKFYENVRPPFIGTYSMDFTLPPNDPFSTKGTGFNYDYDSDVEWVNEEEEGEVDNLESGEEEEEEEDDEDVPSEGEFDGFLDSEENSDLDGLPCAKRKFVGPLIPTICLKSNFENLSEENKRYLQQLKAEVIIETDGPIDPFKEPKTSSLPSKRSNSDLQAQTASQSQSPEKKQKAMITDPMDLLRLFDGVQDSTFSLGTVTEIAQKNLPQYNKQTIKNTIKEYAIRSSGKGDLPRKWVIKDAQNWENLRANANMPTPSL
Protein: Dehydration-responsive element-binding protein 1C (Protein DREB1C) (C-repeat/dehydration-responsive element-binding factor 2) (C-repeat-binding factor 2) (CRT/DRE-binding factor 2) (Q9SYS6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional activator that binds specifically to the DNA sequence 5'-[AG]CCGAC-3'. Binding to the C-repeat/DRE element mediates cold-inducible transcription. CBF/DREB1 factors play a key role in freezing tolerance and cold acclimation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Transcription factor ICE1
- Protein COLD-REGULATED 15A, chloroplastic
- Low-temperature-induced 78 kDa protein
- Calmodulin-binding transcription activator 3
- Dehydrin COR47
- Zinc finger protein ZAT12
- Zinc finger protein ZAT10
- Floral homeotic protein APETALA 2
- E3 ubiquitin-protein ligase HOS1
- Transcription factor MYB15
Sequence:
MNSFSAFSEMFGSDYESPVSSGGDYSPKLATSCPKKPAGRKKFRETRHPIYRGVRQRNSGKWVCELREPNKKTRIWLGTFQTAEMAARAHDVAAIALRGRSACLNFADSAWRLRIPESTCAKEIQKAAAEAALNFQDEMCHMTTDAHGLDMEETLVEAIYTPEQSQDAFYMDEEAMLGMSSLLDNMAEGMLLPSPSVQWNYNFDVEGDDDVSLWSY
Protein: Large ribosomal subunit protein uL2C (60S ribosomal protein L2-C) (K37) (K5) (KD4) (P0CT72)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Elongation factor 3
- Large ribosomal subunit protein eL18A
- Large ribosomal subunit protein uL24
- Large ribosomal subunit protein eL6
- mRNA export factor elf1
- Large ribosomal subunit protein eL13
- Large ribosomal subunit protein eL14
- Large ribosomal subunit protein eL31
- Large ribosomal subunit protein eL29
- Large ribosomal subunit protein eL8
Sequence:
MGRVIRAQRKSGGIFQAHTRLRKGAAQLRTLDFAERHGYIRGVVQKIIHDPGRGAPLAKVAFRNPYHYRTDVETFVATEGMYTGQFVYCGKNAALTVGNVLPVGEMPEGTIISNVEEKAGDRGALGRSSGNYVIIVGHDVDTGKTRVKLPSGAKKVVPSSARGVVGIVAGGGRIDKPLLKAGRAFHKYRVKRNCWPRTRGVAMNPVDHPHGGGNHQHVGHSTTVPRQSAPGQKVGLIAARRTGLLRGAAAVEN
Protein: SNARE-complex protein Syntaxin-18 N-terminal domain-containing protein (Q54TZ2)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004211}; Single-pass type IV membrane protein {ECO:0000256|ARBA:ARBA00004211}.
Interaction partners:
- Centrosomal protein 103 kDa
- Vesicle-trafficking protein SEC22b
- t-SNARE coiled-coil homology domain-containing protein
- t-SNARE family protein
- Uncharacterized protein
- Uncharacterized protein
- Sec1 family domain-containing protein 1 homolog
- Alpha-soluble NSF attachment protein
- Sec20 family protein
- V-SNARE family protein
Sequence:
MVMIDDTNRFLECVKRKCNDPSMKNKISNQTLLKKNQTKKEHQTDIIIKASISIYNTINTLELFLNEHKEAYVNTTTHIKSMSSKMTDEEREEIDKLSTNQIEVCKSSIKSIEELIRKHYTDLSKSYKKELSKWYGNKSISSSSIAILDIIRDDPADFLNLSETGRLSLRESLENYGPRVVLYSNIVDQLKHYLNNVSNSFKKLRSFRLNLKLKESEKLGNKATQDNTTLLRLRNKPSSSSSTKDPNSYNYEEEEENEKKVTTKDLYGGDGDGDDDEFDEEEMQIYEQQNSELKAELETLADQIEVINRQVEELSQLFDEITPHILQHKEVITNIHTTTIEATNYVTRGNNQIYEATKKSFDFRVMVLIFLIISSLSLLVLNWYQD
Protein: DNA cross-link repair protein pso2/snm1 (EC 3.1.-.-) (Q10264)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for DNA interstrand cross-link repair. This requires cleavage of cross-linked DNA to generate DNA double strand breaks (DSBs). This protein may have 5' exonuclease activity on single-stranded and double-stranded DNA, which could be necessary for the processing of DNA double strand breaks prior to religation.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Ribonuclease MRP protein subunit rmp1
- Probable ribonucleases P protein subunit pop8
- Ribonuclease P protein subunit rpr2
- ATP-dependent DNA helicase II subunit 2
- ATP-dependent DNA helicase II subunit 1
- Ribonucleases P/MRP protein subunit POP7
- DNA repair protein rad14
- Protein cft1
- LSM complex subunit lsm2
- Exodeoxyribonuclease 1
Sequence:
MSKRKSSSILDFFKKSNNGKNMWGNEAVSVEKTDSTTKPSTVKNAISSSQIKNEKFSQEVLLQFNDPSFTSEVGESPQWQSFGDANILEPLKNELVKNEESTMSELLLCPICGITLESLTVDANIHVNDCLDGRTTEAVSKKLKKDSVVKADPSNSSTFPISDSCKQALLPLPGKQINVRSVVPFYKLMPYNIPFAVDAFAYGAIDGVEAYFLSHFHSDHYGGLTPKWKHGPIYCSEVTGNLLINVMHVDEQYVKRLKLNQPYNIMGITVYVLDANHCPGSAMFVFETLQSNQTRRVLHCGDFRASKDHVMHPVLREKTIHKVYLDTTYLNPKYTFPPQADVVQACADKAISIKKSTDSRLLVVVSTYSIGKEKVAVAIAKSLSSRIYVVPRKMHIIKQLENQDLIDLLTDDPTQASVHMVTMMGIHPNSLLDYLEQYNSSFDKIIGYKVTGWTFQPLENRAQLSSSLDSIISRPPKFVEYDLRAIRGSTDKVAAFVAPYSEHSSFYDLTMFCLSMNIGHIIPTVNVGSQRSREKMNVWLDRWAWRRKKQGLLSLENVDW
Protein: Mitoregulin (Micropeptide in mitochondria) (Micropeptide regulator of beta-oxidation) (Small integral membrane protein 37) (lncRNA-encoded micropeptide) (Q8NCU8)
Organism: Homo sapiens (Human)
Function: Positively regulates mitochondrial complex assembly and/or stability (By similarity). Increases mitochondrial membrane potential while decreasing mitochondrial reactive oxygen species. Increases mitochondrial respiration rate. Increased mitochondrial respiratory activity promotes myogenic differentiation which facilitates muscle growth and regeneration (By similarity). Increases mitochondrial calcium retention capacity. Plays a role in maintenance of cellular lipid composition through its interaction with cytochrome b5 reductase CYB5R3 which is required for mitochondrial respiratory complex I activity (By similarity). Interacts with the mitochondrial trifunctional enzyme complex (MTE) and enhances fatty acid beta-oxidation. Not required for MTE formation or stability (By similarity). Modulates triglyceride clearance in adipocytes through its role in regulating fatty acid beta-oxidation and lipolysis.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q8BT35}; Single-pass membrane protein {ECO:0000305}. Note=Preferentially binds to cardiolipin relative to other common cell membrane lipids. {ECO:0000250|UniProtKB:Q8BT35}.
Interaction partners:
Sequence:
MADVSERTLQLSVLVAFASGVLLGWQANRLRRRYLDWRKRRLQDKLAATQKKLDLA
Protein: Glutamine repeat protein 1 (E9Q9S8)
Organism: Mus musculus (Mouse)
Interaction partners:
- Olfactory receptor
Sequence:
MSSICLFRDVAIIKSGKRRKRRAYSRLDGAKEQHQQHQQHQQDQHQQHQQQQQQQQQQQQHQQHQQHQQHQQHQQHQQHQQHQQHQQHQQHQQHQQHQQHQQHQQQQQHQQHQQHQQQQQQQQHQQHQQHQQHQHQQHQHQQHQQHQQQQQNQMDKIPGMMIFEIPETKNLERI
Protein: MIP1.1a (U5HUF9)
Organism: Nicotiana benthamiana
Interaction partners:
Sequence:
MFGRAPKKSDNTKYYEILGVPKTASPEDLKKAYRKAAIKNHPDKGGDPEKFKELAQAYEVLSDPEKREIYDQYGEDALKEGMGGGGGGHDPFDIFSSFFGGSPFGGGMGGGSSRGRRQKRGEDVVHPLKVSLDDLYNGTSKKLSLSRNVLCPKCKGKGSKSGASMKCSGCQGSGMKVTIRQLGPSMIQQMQHACNECKGTGETISDKDRCGQCKGEKVVQEKKVLEVVVEKGMQNGQKITFPGEADEAPDTISGDIVFVLQQKEHPKFKRKGDDLFVEHTLSLTEALCGFQFILTHLDNRQLLIKSQPGEVVKPDQFKAINDEGMPMYQRPFMRGKLYIHFSVDFPETLSPEQCKNLEAVLPPKPKTQMTDMELDECEETTLHDVNIEEEMRRKQQQAQEAYDEDEDMHGGAQRVQCAQQ
Protein: Ets DNA-binding protein pokkuri (Protein anterior open) (Protein yan) (Q01842)
Organism: Drosophila melanogaster (Fruit fly)
Function: Ets-related protein that functions as a negative regulator of photoreceptor development acting antagonistically to pnt and the proneural signal mediated by RAS. It acts upstream of SINA to inhibit R7 development.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00237, ECO:0000269|PubMed:1505027}. Note=In undifferentiated cells during the early stages of eye development.
Interaction partners:
- ETS-domain lacking
- Mitogen-activated protein kinase ERK-A
- Stress-activated protein kinase JNK
- Exportin-1
- Ras-like protein 1
- Protein tramtrack, alpha isoform
- ETS-like protein pointed
- Raf homolog serine/threonine-protein kinase Raf
- Protein lozenge
Sequence:
MSKMKMLPVQLSLNSLNPGIWSDVLWRCPPAPSSQLAELKTQLPPSLPSDPRLWSREDVLVFLRFCVREFDLPKLDFDLFQMNGKALCLLTRADFGHRCPGAGDVLHNVLQMLIIESHMMQWHLPNSPVTPTSRYPLSPHSHPPTPTWPPLNAPPENSPFHSSAHSLAGHHFMAPNSVTLSPPPSVDSQASSPPQAPYQNGGATGAAPGSAGGSAPAAGGATNTSNPTSSSASSTGSNGSQPNIMPMKGISSASSNHSDSEEEYSETSGGVSKMPPAPLSYSTASPPGTPILKDIKPNWTQQLTNSFVNSWSQQQQQQQQQQAAAVAAVAAQAQQHQLQQQQQQQQLPQKLTLDNTAGPVVTPAGGSISAPTTPSYMYKAKREFFPENSEPNTNGRLLWDFLQQLLNDRNQKYSDLIAWKCRDTGVFKIVDPAGLAKLWGIQKNHLSMNYDKMSRALRYYYRVNILRKVQGERHCYQFLRNPTELKNIKNISLLRQSTPANGNGGSPSMPQGSSQAPGSPAGQNWNPQQQSQQQQQSPQRPASRNGPMSLPAVAAVAAAAAAAYGPPPTSPLFMHAINGAFHYLSAAAAGPPPNSPALNTPSAVGGPDKFQFHPLKLENGSGSGSESAGEDLKPTDLSVSSKSTATSNEDCYPLIRNADGLTTIKLIRYNEHQVAASPAGQSPKHDDQQAGASNASSSPRPMDQASEQAQPVPMESDCNGGESEDSFRHMQQ
Protein: Sperm acrosome developmental regulator (Q8IZ16)
Organism: Homo sapiens (Human)
Function: May play a role in acrosome formation and nucleus shaping during spermiogenesis.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:31429579, ECO:0000269|PubMed:31985809}. Note=Detected in acrosome of round spermatids and spermatozoa. {ECO:0000269|PubMed:31985809}.
Interaction partners:
- TSC22 domain family protein 4
Sequence:
MVVVMKFFRWVRRAWQRIISWVFFWRQKIKPTISGHPDSKKHSLKKMEKTLQVVETLRLVELPKEAKPKLGESPELADPCVLAKTTEETEVELGQQGQSLLQLPRTAVKSVSTLMVSALQSGWQMCSWKSSVSSASVSSQVRTQSPLKTPEAELLWEVYLVLWAVRKHLRRLYRRQERHRRHHVRCHAAPRPNPAQSLKLDAQSPL
Protein: Amiloride-sensitive Na+ channel (Gonad-specific amiloride-sensitive sodium channel 1) (Ripped pocket, isoform A) (O46342)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MTISDSELDSSKGIDLTFRRRRKAGSVACEGFITTYHEYCRNTSIHGVQYLGEQERPFRERIFWLFVFLISIYGCSTLIQSAYTKWTETPVIVSFAEKSTPVWNIPFPAVTVCSETKRVLKQKGKETTYADLYSQFSEDMRASRVFRPENVSALEMEEFRTLLHVCNTQIIEEDIPLIAGDDLDYFDVLQRMLPQFDRYFFYCRWLSRFGECETFFRKTLTEEGICYTFNGLRATEIYRDDTYQYQHSGEPLEMENISSQHTAWTLETGYALDSDVETFPARVLSAGARSGIFLALQSFKQEVDYACRGPVQGFKVLLHAPDDVPQVSKQFVRIPMGKEVLIAVKPNMITMSSGIAEYHPVRRQCFLSHERSLRFFKVYTESNCQLECLANFTLTKCGCVKFSMPRNVDMPVCGEDKIHCYDRAERELLVREFKRVKALNAGRENSRSVESACNCMPACTSLVYNTEISQANFDLEEMLVAEGDTEFLKEYPGSQMSRLSIYFKQSQFITSKRSELYGMTEFLANCGGIFGLFMGFSILSLVEMIYHFTLRLFTNLKRLVKG
Protein: Defensin alpha 4 (Corticostatin HP-4) (HNP-4) (HP-4) (Neutrophil defensin 4) (P12838)
Organism: Homo sapiens (Human)
Function: Host-defense peptide that has antimicrobial activity against Gram-negative bacteria, and to a lesser extent also against Gram-positive bacteria and fungi. Exhibits antimicrobial activity against Gram-negative E.coli and E.aerogenes and Gram-positive S.faecalis, S.aureus and B.cereus and the yeast C.albicans (in vitro). Interacts with pathogenic surface proteins and toxins, such as HIV-1 surface protein gp120 and B.anthracis anthrax lethal factor lef. Protects blood cells against infection with HIV-1 (in vitro). Inhibits enzymatic activity of B.anthracis lef/anthrax lethal factor (in vitro). Inhibits corticotropin (ACTH)-stimulated corticosterone production (in vitro).
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q01523}. Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:2500436, ECO:0000269|PubMed:2501794}. Note=Stored as mature peptide in neutrophil granules. {ECO:0000269|PubMed:2500436}.
Interaction partners:
- Cell adhesion molecule CEACAM8
- Neutrophil elastase
- Cathepsin G
- Neutrophil defensin 3
- Neutrophil defensin 1
- Beta-defensin 1
- Neutrophil collagenase
- Myeloperoxidase
- Bactericidal permeability-increasing protein
- Defensin beta 4A
Sequence:
MRIIALLAAILLVALQVRAGPLQARGDEAPGQEQRGPEDQDISISFAWDKSSALQVSGSTRGMVCSCRLVFCRRTELRVGNCLIGGVSFTYCCTRVD