wanglab/gogpt-training-data huggingface dataset:
Protein: Putative viral protein-binding protein C1 (Q6Q795)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEEVIQAGLAQWSRQKGLALPWDRTRGHPDVPWRNLTSSPTRPLAQPAGSCMPAEPSPAAHYHQLHVHLQLLPSDLSERPGLRLAPLALVEVGMTLPVPQTPLPHVTQQQKLAPGRQLCPW
Protein: Immunoglobulin heavy constant mu (Ig mu chain C region) (Ig mu chain C region BOT) (Ig mu chain C region GAL) (Ig mu chain C region OU) (P01871)
Organism: Homo sapiens (Human)
Function: Constant region of immunoglobulin heavy chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen. IgM antibodies play an important role in primary defense mechanisms. They have been shown to be involved in early recognition of external invaders like bacteria and viruses, cellular waste and modified self, as well as in recognition and elimination of precancerous and cancerous lesions. The membrane-bound form is found in the majority of normal B-cells alongside with IgD. Membrane-bound IgM induces the phosphorylation of CD79A and CD79B by the Src family of protein tyrosine kinases. It may cause death of cells by apoptosis. It is also found in soluble form, which represents about 30% of the total serum immunoglobulins where it is found almost exclusively as a homopentamer. After the antigen binds to the B-cell receptor, the secreted form is secreted in large amounts.
Subcellular location: [Isoform 1]: Secreted. Note=During differentiation, B-lymphocytes switch from expression of membrane-bound IgM to secretion of IgM. {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
GSASAPTLFPLVSCENSPSDTSSVAVGCLAQDFLPDSITFSWKYKNNSDISSTRGFPSVLRGGKYAATSQVLLPSKDVMQGTDEHVVCKVQHPNGNKEKNVPLPVIAELPPKVSVFVPPRDGFFGNPRKSKLICQATGFSPRQIQVSWLREGKQVGSGVTTDQVQAEAKESGPTTYKVTSTLTIKESDWLGQSMFTCRVDHRGLTFQQNASSMCVPDQDTAIRVFAIPPSFASIFLTKSTKLTCLVTDLTTYDSVTISWTRQNGEAVKTHTNISESHPNATFSAVGEASICEDDWNSGERFTCTVTHTDLPSPLKQTISRPKGVALHRPDVYLLPPAREQLNLRESATITCLVTGFSPADVFVQWMQRGQPLSPEKYVTSAPMPEPQAPGRYFAHSILTVSEEEWNTGETYTCVVAHEALPNRVTERTVDKSTEGEVSADEEGFENLWATASTFIVLFLLSLFYSTTVTLFKVK
Protein: Magnesium-protoporphyrin IX monomethyl ester [oxidative] cyclase, chloroplastic (Mg-protoporphyrin IX monomethyl ester oxidative cyclase) (EC 1.14.13.81) (Copper response defect 1 protein) (AtCrd1) (Dicarboxylate diiron protein) (AtZIP) (MPE-cyclase) (Q9M591)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the formation of the isocyclic ring in chlorophyll biosynthesis. Mediates the cyclase reaction, which results in the formation of divinylprotochlorophyllide (Pchlide) characteristic of all chlorophylls from magnesium-protoporphyrin IX 13-monomethyl ester (MgPMME).
Subcellular location: Plastid, chloroplast inner membrane; Peripheral membrane protein. Plastid, chloroplast thylakoid membrane; Peripheral membrane protein.
Interaction partners:
- Magnesium protoporphyrin IX methyltransferase, chloroplastic
- Protochlorophyllide reductase B, chloroplastic
- Protochlorophyllide reductase C, chloroplastic
- Divinyl chlorophyllide a 8-vinyl-reductase, chloroplastic
- Geranylgeranyl diphosphate reductase, chloroplastic
- Protochlorophyllide reductase A, chloroplastic
- Protein YCF54, chloroplastic
- Magnesium-chelatase subunit ChlH, chloroplastic
- Glutamyl-tRNA reductase 1, chloroplastic
- Magnesium-chelatase subunit ChlD, chloroplastic
Sequence:
MAAEMALVKPISKFSSPKLSNPSKFLSGRRFSTVIRMSASSSPPPPTTATSKSKKGTKKEIQESLLTPRFYTTDFEEMEQLFNTEINKNLNEAEFEALLQEFKTDYNQTHFVRNKEFKEAADKLQGPLRQIFVEFLERSCTAEFSGFLLYKELGRRLKKTNPVVAEIFSLMSRDEARHAGFLNKGLSDFNLALDLGFLTKARKYTFFKPKFIFYATYLSEKIGYWRYITIYRHLKENPEFQCYPIFKYFENWCQDENRHGDFFSALMKAQPQFLNDWQAKLWSRFFCLSVYVTMYLNDCQRTNFYEGIGLNTKEFDMHVIIETNRTTARIFPAVLDVENPEFKRKLDRMVVSYEKLLAIGETDDASFIKTLKRIPLVTSLASEILAAYLMPPVESGSVDFAEFEPNLVY
Protein: Photosystem II protein D1 (PSII D1 protein) (EC 1.10.3.9) (Photosystem II Q(B) protein) (P83755)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbA) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01379}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01379}.
Interaction partners:
- Photosystem II reaction center protein Z
- Photosystem II reaction center protein I
- Photosystem II reaction center protein L
- Photosystem II reaction center protein J
- Photosystem II reaction center protein H
- Cytochrome b559 subunit alpha
- Photosystem II reaction center protein K
- Photosystem II D2 protein
- Photosystem II CP47 reaction center protein
- Cytochrome b559 subunit beta
Sequence:
MTAILERRESESLWGRFCNWITSTENRLYIGWFGVLMIPTLLTATSVFIIAFIAAPPVDIDGIREPVSGSLLYGNNIISGAIIPTSAAIGLHFYPIWEAASVDEWLYNGGPYELIVLHFLLGVACYMGREWELSFRLGMRPWIAVAYSAPVAAATAVFLIYPIGQGSFSDGMPLGISGTFNFMIVFQAEHNILMHPFHMLGVAGVFGGSLFSAMHGSLVTSSLIRETTENESANEGYRFGQEEETYNIVAAHGYFGRLIFQYASFNNSRSLHFFLAAWPVVGIWFTALGISTMAFNLNGFNFNQSVVDSQGRVINTWADIINRANLGMEVMHERNAHNFPLDLAAVEAPSTNG
Protein: Protoheme IX farnesyltransferase, mitochondrial (EC 2.5.1.141) (Heme O synthase) (HOS) (P21592)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Converts protoheme IX and farnesyl diphosphate to heme O.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:16823961}. Mitochondrion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Heme A synthase COX15
- Cytochrome c oxidase assembly protein COX11
- Holocytochrome-c1 synthase
- Cytochrome oxidase assembly protein SHY1
- Holocytochrome-c synthase
- Cytochrome c oxidase subunit 3
- Probable NADPH:adrenodoxin oxidoreductase, mitochondrial
- Adrenodoxin homolog, mitochondrial
- Ferrochelatase, mitochondrial
- Protein SCO2
Sequence:
MSYFPRTYAHLMRNVLAHNKGNIYLQIGTQLHDTQIKIRFNGVRYISRNHGGKQQHINTAPIEFTPNFGYGDRTSNCNKKVESTAMKTLRCTDDISTSSGSEATTDASTQLPFNVKLVDPMVRKSKRPSHAISEGLNMKTLKKKVIMPYLQLTKPRLTILVMLSAICSYALSPYPASVNELLCLTVGTTLCSGSANAINMGREPEFDRQMVRTQARPVVRGDVTPTQAFEFAALIGTLGVSILYFGVNPTVAILGASNIALYGWAYTSMKRKHIINTWLGALVGMVPPLMGWAAASPLSHPGSWCLAGLLFAWQFPHFNTLSHNIRNEYKNAGYVMTAWKNPLLNARVSLRYSILMFPLCFGLSYFNITDWYYQIDSGLINAWLTFWAFKFYWQQRINYSAKTLKDNVKFNKGLSVANIYARKTFMASVLHLPAILILAIIHKKGRWDWIYPGEAKRPQERF
Protein: Monomeric G-protein (Ras-related small GTP-binding family protein) (Q9LSZ4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Serine/threonine protein phosphatase 2A 55 kDa regulatory subunit B beta isoform
- Serine/threonine protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform
- non-specific serine/threonine protein kinase
- At3g17740
- Protein NRDE2 homolog
- Kinesin-like protein KIN-14E
- At3g07890
- Ypt/Rab-GAP domain of gyp1p superfamily protein
- Ypt/Rab-GAP domain of gyp1p superfamily protein
- Ypt/Rab-GAP domain of gyp1p superfamily protein
Sequence:
MAQSCLKIVRINNLRNRVNRRILILRRFTRLLWSRIVACTPGKSRRYLLLSRALPSPTVSRPSPSPIPAVDVVVGGGGGGGEFVRRSSVVYDNDNSHRRSDSDLVSLKISLLGDPEIGKTSFLAKYVGEEKEVEMRELEKGINCTDKTLYMGGARISYSIWELEGAERSRDQIPVACKDSVAILFMFDLTSRCTLNSVISWYQQARKSNQTAIPVMVGTKFDEFIQLPIDLQWTIASQARTYAKALNATLFFSSASYNINVNKIFKFVTAKLFDLPWTVERNLTIGEPIIDF
Protein: BTB domain-containing protein (Q95XV8)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MIQQIASGSTSMAACERENSVDNQPDRASIDDRSSNKNYDEDVESRMIPVDRPSHKGSIRDNTPDSILRLNIGGSSYRIRTRSIIKFGPKTLLGRFVRMNHEHRRQWADWYFEEQDEYFFERVPRYFDPIYDFYATGKLHVPKDLCFDKFMAELRFWAVSKSRMDECCSPFTQYCVTMGGDPKCTEKDHFIGVRCANIRRRLWLILEGHSQSKWWKAFEIISTAFVVLSISALILGSIPEFQVPQKSEDGQLVYATATYPTYPNGGGMTIESRTVVREGSDNSTGDLMAEETVPTPRNTGKIEMTEHPVFTWVENVCVIYFSIEYAMRFIVAPRKLAFARQILNVIDLLSIAPFYFELLLWICGISGENVRKVRWAFLTVRLLRVLRVIRIAKLGRFSPGLANFALTIRKSKKQMQMVGVVMMTVIIFFSTLIYFLERDEPGTKFTSIPATFWWCVVTMATVGYGDLVPVTVAGKLVGSGAIVCGVMVLALPITIMVNNFMQVVKLREEEIVKKYAQGDQV
Protein: Cytochrome P450 3A18 (EC 1.14.14.1) (CYPIIIA18) (Cytochrome P450(6)beta-2) (Q64581)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes 16-beta- and 6-alpha-hydroxylations of testosterone.
Subcellular location: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.
Interaction partners:
- Cytochrome P450 1A2
- Cytochrome P450 2E1
- Estrogen sulfotransferase Ste2
- Cytochrome P450 1A1
- Cytochrome P450, family 2, subfamily j, polypeptide 4
- Cytochrome P450 4A10
- Aromatase
- Cytochrome P450 4A12
- Cytochrome P450 26A1
- Cytochrome P450 4A2
Sequence:
MEIIPNLSIETWVLLATSLMLFYIYGTYSHGLFKKLGIPGPKPVPLFGTIFNYGDGMWKFDDDCYKKYGKIWGFYEGPQPFLAIMDPEIIKMVLVKECYSVFTNRRCFGPMGFMKKAITMSEDEEWKRLRTILSPTFTSGKLKEMFPLMRQYGDTLLKNLRREEAKGEPINMKDIFGAYSMDVITGTSFGVNVDSLNNPQDPFVQKAKKILKFQIFDPFLLSVVLFPFLTPIYEMLNFSIFPRQSMNFFKKFVKTMKKNRLDSNQKNRVDFLQLMMNTQNSKGQESQKALSDLEMAAQAIIFIFGGYDATSTSISFIMYELATRPNVQKKLQNEIDRALPNKAPVTYDALMEMEYLDMVVNESLRLYPIATRLDRVSKKDVEINGVFIPKGTVVTIPIYPLHRNPEYWLEPEEFNPERFSKENKGSIDPYVYLPFGNGPRNCIGMRFALISMKLAVIGVLQNFNIQPCEKTQIPLKISRQPIFQPEGPIILKLVSRD
Protein: GTP cyclohydrolase-2 (EC 3.5.4.25) (GTP cyclohydrolase II) (F9UNI1)
Organism: Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1) (Lactobacillus plantarum)
Interaction partners:
- Riboflavin synthase
- 6,7-dimethyl-8-ribityllumazine synthase
- GTP cyclohydrolase 1
- GTP 3',8-cyclase
- Nucleoside diphosphate kinase
- 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase
- Dihydropteroate synthase
- Transcription antitermination protein NusB
- 16S rRNA
- GTP diphosphokinase
Sequence:
MDTMKKVAAALAALKRGELIIVADDETREAEGDMVGLAAKATTATVNRMITSARGLLCVPMAPSIATRLHLTPMTSEHDAFGTAFTVSTDHHTTSTGISAADRATTIQALANPNSQAADFYHPGHVFPLIARTGGLLARRGHTEAAVTLAQLAGVTPAAYICEVIKKNGLMARRRDLKALAEGLQLPLITIEDITTYVIQTGAAQLTTTPSVNLPTKDGQFTMTGFEVPGHTALPVALQAGDISGDEPVLVRLHSECFTGDVLGSRRCDCGDQLHAALQKISQAQRGVFVYLRQEGRGIGLANKLAAYALQEHGVDTYDANVQLGFQPDERRYDIAALVLRQMGITRVRLLTNNPDKVEQLRAAGIDVVERVPLEIPANQYDQAYLKTKRDRFHHQLTLTEGHE
Protein: Natural cytotoxicity triggering receptor 3 (Activating natural killer receptor p30) (Natural killer cell p30-related protein) (NK-p30) (NKp30) (CD antigen CD337) (O14931)
Organism: Homo sapiens (Human)
Function: Cell membrane receptor of natural killer/NK cells that is activated by binding of extracellular ligands including BAG6 and NCR3LG1. Stimulates NK cells cytotoxicity toward neighboring cells producing these ligands. It controls, for instance, NK cells cytotoxicity against tumor cells. Engagement of NCR3 by BAG6 also promotes myeloid dendritic cells (DC) maturation, both through killing DCs that did not acquire a mature phenotype, and inducing the release by NK cells of TNFA and IFNG which promote DC maturation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10562324}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Natural cytotoxicity triggering receptor 3 ligand 1
- T-cell surface glycoprotein CD3 zeta chain
- High affinity immunoglobulin epsilon receptor subunit gamma
- Natural cytotoxicity triggering receptor 2
- Large proline-rich protein BAG6
- Natural cytotoxicity triggering receptor 1
- NKG2-D type II integral membrane protein
- Nectin-2
- CD226 antigen
- MHC class I polypeptide-related sequence B
Sequence:
MAWMLLLILIMVHPGSCALWVSQPPEIRTLEGSSAFLPCSFNASQGRLAIGSVTWFRDEVVPGKEVRNGTPEFRGRLAPLASSRFLHDHQAELHIRDVRGHDASIYVCRVEVLGLGVGTGNGTRLVVEKEHPQLGAGTVLLLRAGFYAVSFLSVAVGSTVYYQGKCLTWKGPRRQLPAVVPAPLPPPCGSSAHLLPPVPGG
Protein: ATP-dependent RNA helicase SUB2 (EC 3.6.4.13) (Suppressor of BRR1 protein 2) (Q07478)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: ATP-binding RNA helicase component of the TREX complex involved in transcription elongation and required for the export of mRNA out of the nucleus. SUB2 also plays a role in pre-mRNA splicing and spliceosome assembly. May be involved in rDNA and telomeric silencing, and maintenance of genome integrity.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP22
- THO complex subunit THP2
- THO complex subunit HPR1
- THO complex subunit 2
- RNA annealing protein YRA1
- THO complex subunit MFT1
- Protein TEX1
- Protein THO1
- Splicing factor MUD2
- mRNA export factor MEX67
Sequence:
MSHEGEEDLLEYSDNEQEIQIDASKAAEAGETGAATSATEGDNNNNTAAGDKKGSYVGIHSTGFKDFLLKPELSRAIIDCGFEHPSEVQQHTIPQSIHGTDVLCQAKSGLGKTAVFVLSTLQQLDPVPGEVAVVVICNARELAYQIRNEYLRFSKYMPDVKTAVFYGGTPISKDAELLKNKDTAPHIVVATPGRLKALVREKYIDLSHVKNFVIDECDKVLEELDMRRDVQEIFRATPRDKQVMMFSATLSQEIRPICRRFLQNPLEIFVDDEAKLTLHGLQQYYIKLEEREKNRKLAQLLDDLEFNQVIIFVKSTTRANELTKLLNASNFPAITVHGHMKQEERIARYKAFKDFEKRICVSTDVFGRGIDIERINLAINYDLTNEADQYLHRVGRAGRFGTKGLAISFVSSKEDEEVLAKIQERFDVKIAEFPEEGIDPSTYLNN
Protein: Cardio acceleratory peptide 2b (Capability protein) (Myotropin-CAP2b-like protein) [Cleaved into: CAP-1 (CAP2b-1) (Capa-1); CAP-2 (CAP2b-2) (Capa-2); CAP-3 (CAP2b-3) (Capa-3) (Myotropin) (Pyrokinin-1)] (Q9NIP6)
Organism: Drosophila melanogaster (Fruit fly)
Function: CAP-1 and CAP-2, but not CAP-3 are ligands for the Capa receptor. CAP-1 and CAP-2 are probably components of the signal transduction pathway that leads to Malpighian tubule fluid secretion via the second messenger nitric oxide. CAP-3 is a ligand for the PK1-R G-protein coupled receptor.
Subcellular location: Secreted {ECO:0000269|PubMed:11959669}. Note=Released from the neuroendocrine cells into the hemolymph.
Interaction partners:
- Neuropeptides capa receptor
- Protein hugin
- Pyrokinin-1 receptor
- Leucokinin
- Pyrokinin 2 receptor 2, isoform A
- Ecdysis triggering hormone
Sequence:
MKSMLVHIVLVIFIIAEFSTAETDHDKNRRGANMGLYAFPRVGRSDPSLANSLRDGLEAGVLDGIYGDASQEDYNEADFQKKASGLVAFPRVGRGDAELRKWAHLLALQQVLDKRTGPSASSGLWFGPRLGKRSVDAKSFADISKGQKELN
Protein: Peptidoglycan hydrolase gp181 (Gene product 181) (Gp181) (Q8SCY1)
Organism: Pseudomonas phage phiKZ
Function: Exolysin that catalyzes the cleavage of the host peptidoglycans during virus entry.
Subcellular location: Virion {ECO:0000269|PubMed:18671939}.
Interaction partners:
Sequence:
MAKKVTLPKGQTGATGTTLGQAGNILDLSDVDDIFGDTPKAKKGSPVTEFFNGIKQGLFDSVKPQQALKAFMRSAAPDGFSRMFGVYEDTMSTIRDVKDSVERTSASDLLFLTREAQDLAVKLKDKVPASVFDRLNNRLESQIENYKYAEDSNRNYKEIRRRMEAERDEDELKSAIDQVTLVQRDLAIKAEQGEVKRFAIGQAERGIRDKVSADRFDWMAKAMGQTVDNLSKLASYNEQVNYSIQKKGLEIQFRSMLHLRKIAQQTEATMELLNNGFAALVRNTGIPDHKKSSMKDLVGFNAAQRVSSSFVDNAIQTLPNFLGNFGSAVTNNATRFANENIRNFADAVRAGNMFGADAWENRYNIAGQFAGSYLGDWTRNSVIPVLGRMARPGIERFSNNYLGGRHNQASYLLDNFPAWTQEYMNNYQNTYGARGILRDIMAPFIPQFTLQDRLKTGSYQTIGQDSGFNQLTQRTIVEAIPGYLSRLLQETRMIRTGRDDITREVFDLSTGSFMSVEDSAANTERRLVSRSTVRGVSGALTDVLEAFDPNKELSIDARKALTERLIRDANMNKRFDPEAYARAGGYDRSKVSGETIKELTEYIKRQYNIGADGRMASTNENFARRQEISTLFLDVRNFSRDPIKEIERLTNAGKTDQLREMGIIITEQGIDRINYPRIWELMSSEVKYEGWGNDNPFDRYSDTPPSDNGGPEQLSPLGDQNNPHFIGPMYQSQTERKMRQAQEQVIRASKLAQEQANKGYDYAQQKVSLATDYVRDNVPNQFSELRRNVNIPASMNFGDLRDQLYGQAGDMYSRAVNYSNQLNGYSDIINQSIADLYTKANTFTPVIKGMDFLNGNLIDINTGMIVEKISDITGEIKNQAGITVVTAQEVATGLYNQRGDLLTKATDIASQLRDKAAQIAGDARERLTQGLDNVSDMAKDWYIPGREEAVILGRDLLAGEYIDTATNQIITNLKDAKGTIINRAGDVVVTAQELAKGLIRSDGFNLRRNIADTSNWIQRNVLGGGSTTQKIFNAMGTVANKAKDFTIGLGKDILSNRDAYLPGMLKPVLQKVKLKAGEYYTTAGNLLKSFDEINGPVLDRDGNIVVDEEQISELINSDGSKHTAAKSKGLFRTGLGNLARGYANMSMRYWKWLGKKSVDTAKGMAGLGYKLLGSPFKKRFSAFTGKVETQIDKKALDTTTDQLLAGIWEELRNQKPDANKPRRGSWQDLTSRVSDTLNGKNNGDEETTESKGLFGKLGDTLKNIFGKKKGDEEDEGLLEDLGLGGKKGGKWAAARQILGRGALAIGGGALSTAAAYASFGGTGASTNDKLAGAAIVTSNPIMWALKDFLIKPVLGWRGSQKFKDDLISYRMMQYGATTTDQMNKVTELEQLVSSVATRGGDASFDVRALNARDIIKIFGYGADDGPAIMRLANWIDFRFKPIFEAWLKGLSKINRSDVDISEVDSKVPNELKGQLIRSVSFPYEGNTPYLVLNNPFGEEDLSIDVASIQMKEKELLNKYSATEKTSVAPKATSSSFKESTTDVINDTITTIKSKSTDITNWFRDSTIGKAIKAVSPVESIRKMVTTTVDTIIPKANASDSLTSLQALRVHAYGMQGLDLAAVNGLLSIESLVNDKMRVANGKATYTGDIEELIKWTGQAFGMVTTSDGPDRVKVVDWLYRRFLPVFKAFIVTARSVSTSITLSQIETLTATQRVQIANAIMGATDDEGISIWKAPSIFNIVGDMDSVEDLAKISLDEIKKEAETEVAEAPGKSKSAQIAGKNDAASGRSFASRIIDNVKSTFNSATTKVTNWMENTSARVSQVIGRAREGVTDTYYTAKYKLGAGGELTPTGQTYGQLATGNGGVWENIPMPQSNKSRDAAQATFKAVSEMTGVPVELLNIFCGIESSFNYNAKAPTSSAAGWFQFIKSTWKGMLAKYGAKFGIPADDENGSLRFDPRINALMGAMFLRDNYEYLENALGRAPTDVDLYLAHFMGPAGARKFLTRDQNSIGAEIFPDQARANRSIFFKTDGSARTLGEIYQVMENKVAKFRTGGGKNANSQSLGKPKSTEELMNDAATAKQKDMATDKELIGGAADTSITDSSNNKIGLGKIMSGMASPLRTNAPSMMLPGAPSSATDVSSGQQPVVDTGAATQATVRASQIEEQRKVVTSQDKAMLDIASEQLSVLKQFHADILNYIKNKAANPSAQTGQEQANTIAPSQRPGRVVDNRPLPIRLR
Protein: Glucans biosynthesis protein D (P40120)
Organism: Escherichia coli (strain K12)
Function: Probably involved in the control of the structural glucose backbone of osmoregulated periplasmic glucans (OPGs).
Subcellular location: Periplasm.
Interaction partners:
- Glucans biosynthesis glucosyltransferase H
Sequence:
MDRRRFIKGSMAMAAVCGTSGIASLFSQAAFAADSDIADGQTQRFDFSILQSMAHDLAQTAWRGAPRPLPDTLATMTPQAYNSIQYDAEKSLWHNVENRQLDAQFFHMGMGFRRRVRMFSVDPATHLAREIHFRPELFKYNDAGVDTKQLEGQSDLGFAGFRVFKAPELARRDVVSFLGASYFRAVDDTYQYGLSARGLAIDTYTDSKEEFPDFTAFWFDTVKPGATTFTVYALLDSASITGAYKFTIHCEKSQVIMDVENHLYARKDIKQLGIAPMTSMFSCGTNERRMCDTIHPQIHDSDRLSMWRGNGEWICRPLNNPQKLQFNAYTDNNPKGFGLLQLDRDFSHYQDIMGWYNKRPSLWVEPRNKWGKGTIGLMEIPTTGETLDNIVCFWQPEKAVKAGDEFAFQYRLYWSAQPPVHCPLARVMATRTGMGGFSEGWAPGEHYPEKWARRFAVDFVGGDLKAAAPKGIEPVITLSSGEAKQIEILYIEPIDGYRIQFDWYPTSDSTDPVDMRMYLRCQGDAISETWLYQYFPPAPDKRQYVDDRVMS
Protein: Spectrin repeat containing nuclear envelope protein 1 (H0Y326)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus membrane {ECO:0000256|ARBA:ARBA00004126}.
Interaction partners:
Sequence:
ETFAKSLEALEAWIVEAEEILQGQDPSHSSDLSTIQERMEELKGQMLKFSSMAPDLDRLNELGYRLPLNDKEIKRMQNLNRHWSLISSQTTERFSKLQSFLLQHQTFLEKCETWMEFLVQTEQKLAVEISGNYQHLLEQQRAHELFQAEMFSRQQILHSIIIDGQRLLEQGQVDDRDEFNLKLTLLSNQWQGVIRRAQQRRGIIDSQIRQWQRYREMAEKLRKWLVEVSYLPMSGLGSVPIPLQQARTLFDEVQFKEKVFLRQQGSYILTVEAGKQLLLSADSGAEAALQAELAEIQEKWKSASMRLEEQKKKLAFLLKDWEKCEKGIADSLEKLRTFKKKLSQSLPDHHEELHAEQMRCKELENAVGSWTDDLTQLSLLKDTLSAYISADDISILNERVELLQRQWEELCHQLSLRRQQIGERLNEWAVFSEKNKELCEWLTQMESKVSQNGDILIEEMIEKLKKDYQEEIAIAQENKIQLQQMGERLAKASHESKASEIEYKLGKVNDRWQHLLDLIAARVKKLKETLVAVQQLDKNMSSLRTWLAHIESELAKPIVYDSCNSEEIQRKLNEQQELQRDIEKHSTGVASVLNLCEVLLHDCDACATDAECDSIQQATRNLDRRWRNICAMSMERRLKIEETWRLWQKFLDDYSRFEDWLKSSERTAAFPSSSGVIYTVAKEELKKFEAFQRQVHECLTQLELINKQYRRLARENRTDSACSLKQMVHEGNQRWDNLQKRVTSILRRLKHFIGQREEFETARDSILVWLTEMDLQLTNIEHFSECDVQAKIKQLKAFQQEISLNHNKIEQIIAQGEQLIEKSEPLDAAIIEEELDELRRYCQEVFGRVERYHKKLIRLPLPDDEHDLSDRELELEDSAALSDLHWHDRSADSLLSPQPSSNLSLSLAQPLRSERSGRDTPASVDSIPLEWDHDYDLSRDLESAMSRALPSEDEEGQDDKDFYLRGAVGLSGDHSALESQIRQLGKALDDSRFQIQQTENIIRSKTPTGPELDTSYKGYMKLLGECSSSIDSVKRLEHKLKEEEESLPGFVNLHSTETQTAGVIDRWELLQAQALSKELRMKQNLQKWQQFNSDLNSIWAWLGDTEEELEQLQRLELSTDIQTIELQIKKLKELQKAVDHRKAIILSINLCSPEFTQADSKESRDLQDRLSQMNGRWDRVCSLLEEWRGLLQDALMQCQGFHEMSHGLLLMLENIDRRKNEIVPIDSNLDAEILQDHHKQLMQIKHELLESQLRVASLQDMSCQLLVNAEGTDCLEAKEKVHVIGNRLKLLLKEVSRHIKELEKLLDVSSSQQDLSSWSSADELDTSGSVSPTSGRSTPNRQKTVHKRWLRFLPF
Protein: Tyrosine-protein phosphatase non-receptor type 1 (EC 3.1.3.48) (Protein-tyrosine phosphatase 1B) (PTP-1B) (P20417)
Organism: Rattus norvegicus (Rat)
Function: Tyrosine-protein phosphatase which acts as a regulator of endoplasmic reticulum unfolded protein response. Mediates dephosphorylation of EIF2AK3/PERK; inactivating the protein kinase activity of EIF2AK3/PERK. May play an important role in CKII- and p60c-src-induced signal transduction cascades. May regulate the EFNA5-EPHA3 signaling pathway which modulates cell reorganization and cell-cell repulsion. May also regulate the hepatocyte growth factor receptor signaling pathway through dephosphorylation of MET (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Interacts with EPHA3 at the cell membrane. {ECO:0000250}.
Interaction partners:
- Insulin receptor
- Insulin receptor substrate 1
- Insulin receptor substrate 2
- Receptor protein-tyrosine kinase
- Tyrosine-protein kinase JAK2
- Catenin beta-1
- Receptor-type tyrosine-protein phosphatase F
- Tyrosine-protein phosphatase non-receptor type 11
- Tyrosine-protein kinase
- Insulin receptor substrate 3
Sequence:
MEMEKEFEQIDKAGNWAAIYQDIRHEASDFPCRIAKLPKNKNRNRYRDVSPFDHSRIKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRIMEKGSLKCAQYWPQKEEKEMVFDDTNLKLTLISEDVKSYYTVRQLELENLATQEAREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPIVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLEMRRFRMGLIQTADQLRFSYLAVIEGAKFIMGDSSVQDQWKELSHEDLEPPPEHVPPPPRPPKRTLEPHNGKCKELFSNHQWVSEESCEDEDILAREESRAPSIAVHSMSSMSQDTEVRKRMVGGGLQSAQASVPTEEELSPTEEEQKAHRPVHWKPFLVNVCMATALATGAYLCYRVCFH
Protein: Gamma-aminobutyric acid receptor-associated protein-like 2 (GABA(A) receptor-associated protein-like 2) (Ganglioside expression factor 2) (GEF-2) (General protein transport factor p16) (Golgi-associated ATPase enhancer of 16 kDa) (GATE-16) (MAP1 light chain 3-related protein) (P60520)
Organism: Homo sapiens (Human)
Function: Ubiquitin-like modifier involved in intra-Golgi traffic (By similarity). Modulates intra-Golgi transport through coupling between NSF activity and SNAREs activation (By similarity). It first stimulates the ATPase activity of NSF which in turn stimulates the association with GOSR1 (By similarity). Involved in autophagy. Plays a role in mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Whereas LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation.
Subcellular location: Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:12507496, ECO:0000269|PubMed:15169837, ECO:0000269|PubMed:17580304, ECO:0000269|PubMed:19056683, ECO:0000269|PubMed:22311637, ECO:0000269|PubMed:31709703}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:30990354}. Golgi apparatus {ECO:0000250|UniProtKB:P60519}.
Interaction partners:
- Ubiquitin-like protein ATG12
- Sequestosome-1
- Next to BRCA1 gene 1 protein
- Ubiquitin-like modifier-activating enzyme ATG7
- Autophagy protein 5
- Ubiquitin-like-conjugating enzyme ATG3
- BCL2/adenovirus E1B 19 kDa protein-interacting protein 3-like
- Cysteine protease ATG4B
- Optineurin
- BCL2/adenovirus E1B 19 kDa protein-interacting protein 3
Sequence:
MKWMFKEDHSLEHRCVESAKIRAKYPDRVPVIVEKVSGSQIVDIDKRKYLVPSDITVAQFMWIIRKRIQLPSEKAIFLFVDKTVPQSSLTMGQLYEKEKDEDGFLYVAYSGENTFGF