wanglab/gogpt-training-data huggingface dataset:
Protein: Omega-amidase NIT3 (EC 3.5.1.3) (Nitrilase homolog 2) (P49954)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Possesses omega-amidase activity. The role of omega-amidase is to remove potentially toxic intermediates by converting 2-oxoglutaramate and 2-oxosuccinamate to biologically useful 2-oxoglutarate and oxaloacetate, respectively.
Interaction partners:
- NADP-specific glutamate dehydrogenase 1
- NADP-specific glutamate dehydrogenase 2
- NAD-specific glutamate dehydrogenase
- Aspartate aminotransferase, cytoplasmic
- Aspartate aminotransferase, mitochondrial
- Glutamate synthase
- Large ribosomal subunit protein eL31B
- Bis
- Malate dehydrogenase, peroxisomal
- Pyruvate carboxylase 1
Sequence:
MSASKILSQKIKVALVQLSGSSPDKMANLQRAATFIERAMKEQPDTKLVVLPECFNSPYSTDQFRKYSEVINPKEPSTSVQFLSNLANKFKIILVGGTIPELDPKTDKIYNTSIIFNEDGKLIDKHRKVHLFDVDIPNGISFHESETLSPGEKSTTIDTKYGKFGVGICYDMRFPELAMLSARKGAFAMIYPSAFNTVTGPLHWHLLARSRAVDNQVYVMLCSPARNLQSSYHAYGHSIVVDPRGKIVAEAGEGEEIIYAELDPEVIESFRQAVPLTKQRRFDVYSDVNAH
Protein: Serine peptidase inhibitor, Kazal type 4 (E9PU35)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Serine protease inhibitor Kazal-type 1
Sequence:
MAMHLWLVTLTLVPLLAMDRELPVSAARLVFSRMPICEHMAEFPNCPRSPNLICGTDGLTYENECHLCVTRMKTKKDIQIMKDGKC
Protein: DENN domain containing 1A (A0A0A0MS48)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000256|ARBA:ARBA00004132}.
Interaction partners:
Sequence:
MGSRIKQNPETTFEVYVEVAYPRTGGTLSDPEVQRQFPEDYSDQEVLQTLTKFCFPFYVDSLTVSQVGQNFTFVLTDIDSKQRFGFCRLSSGAKSCFCILSYLPWFEVFYKLLNILADYTTKRQENQWNELLETLHKLPIPDPGVSVHLSVHSYFTVPDTRELPSIPENRNLTEYFVAVDVNNMLHLYASMLYERRILIICSKLSTLTACIHGSAAMLYPMYWQHVYIPVLPPHLLDYCCAPMPYLIGIHLSLMEKVRNMALDDVVILNVDTNTLETPFDDLQSLPNDVISSLKNRLKKVSTTTGDGVARAFLKAQAAFFGSYRNALKIEPEEPITFCEEAFVSHYRSGAMRQFLQNATQLQLFKQFIDGRLDLLNSGEGFSDVFEEEINMGEYAGSDKLYHQWLSTVRKGSGAILNTVKTKANPAMKTVYKFAKDHAKMGIKEVKNRLKQKDIAENGCAPTPEEQLPKTAPSPLVEAKDPKLREDRRPITVHFGQLQRLRPTRPPPKIQRSRPVRPPRPHVVKRPKSNIAVEGRRTSVPSPEHLVKPLRHYAVFLSEDSSDDECQREEGPSSGFTESFFFSAPFEWPQPYRTLRESDSAEGDEAESPEQQVRKSTGPVPAPPDRAASIDLLEDVFSNLDMEAALQPLGQAKSLEDLRAPKDLREQPGTFDYQRLDLGGSERSRGVTVALKLTHPYNKLWSLGQDDMAIPSKPPAASPEKPSALLGNSLALPRRPQNRDSILNPSDKEEVPTPTLGSITIPRPQGRKTPELGIVPPPPIPRPAKLQAAGAALGDVSERLQTDRDRRAALSPGLLPGVVPQGPTELLQPLSPGPGAAGTSSDALLALLDPLSTAWSGSTLPSRPATPNVATPFTPQFSFPPAGTPTPFPQPPLNPFVPSMPAAPPTLPLVSTPAGPFGAPPASLGPAFASGLLLSSAGFCAPHRSQPNLSALSMPNLFGQMPMGTHTSPLQPLGPPAVAPSRIRTLPLARSSARAAETKQGLALRPGDPPLLPPRPPQGLEPTLQPSAPQQARDPFEDLLQKTKQDVSPSPALAPAPDSVEQLRKQWETFE
Protein: Kappa-conotoxin RIIIJ (Kappa-M-RIIIJ) (P0CG45)
Organism: Conus radiatus (Rayed cone)
Function: Kappa-conotoxins inhibits voltage-gated potassium channels. This toxin dose-dependently and reversibly inhibits the Kv1.2/KCNA2 channel in mammalia. Does not exert protective effect on cardiac tissue when administered after an ischemic event.
Subcellular location: Secreted.
Interaction partners:
Sequence:
LPPCCTPPKKHCPAPACKYKPCCKS
Protein: SWR1-complex protein 5 (P38326)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the SWR1 complex which mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling. Involved in chromosome stability.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- SWR1-complex protein 4
- Vacuolar protein sorting-associated protein 72
- Protein AF-9 homolog
- SWR1-complex protein 7
- Vacuolar protein sorting-associated protein 71
- RuvB-like protein 1
- RuvB-like protein 2
- Actin-like protein ARP6
- Bromodomain-containing factor 1
- Helicase SWR1
Sequence:
MPEVETKIIPNEKEDEDEDGYIEEEDEDFQPEKDKLGGGSDDSDASDGGDDYDDGVNRDKGRNKVDYSRIESESGGLIKTRRARQAEEEYAKTHKYESLTVESIPAKVNSIWEELQEASKNRLLSSSGKVGSVLDGSKEARSTTAAQQEDKILIERNYKFAGETVHEKKWVSRSSAEGQEYLNSLKFKQQAPAAPVQLEKAVRTKSNESRQHLRRPLKRPPLLEQIISGGLRPKLTTLEKSQLDWASYVDRAGLNDELVLHNKDGFLARQEFLQRVGSAEDERYKELRRQQLAQQLQQDSEAS
Protein: Vacuolar fusion protein MON1 homolog (Q9BI89)
Organism: Caenorhabditis elegans
Interaction partners:
- Vacuolar fusion protein CCZ1 homolog
- small monomeric GTPase
- Ras-related protein Rab-7a
- Vacuolar protein sorting-associated protein 39 homolog
- Vacuolar protein sorting-associated protein 41 homolog
- Vacuolar protein sorting-associated protein 11 homolog
- Rab5 GDP/GTP exchange factor
- Vacuolar protein sorting-associated protein 18 homolog
- PH domain-containing protein
- Vps8 domain-containing protein
Sequence:
MEVEVPGGSEAADTGSEASYKVSQVEIEDVEENLKNADVIFEHLEQLPFQVFILSEFGKPIFVNNDRNEGEIVSLVALICAFVSRCQSWGDSLMTMTSQDNHIQFLHKSPLIFCVVSKYPEQLDQQLEVLFEQICSILSKSQLENVYKKKGDNYDLRKLLRGTDRLIDSSISSWRASPINLVDSSISAIPMNPSDREFLSTTMASCLGAAKLDGALFGIMIARRQIAAMVRFKKYMIHPRDLNIVINLVSDNTLQTDSQNWVPICLPRFNDTGFFYAYISYPWCNKEQDIPVCIVLLSVKRDHFDGLKEVRQQIVTKLENNQKFFVNFAQAMKTPNLYQISQIGSNSESLWSFLYLNHSSKQVCMSASKIPLITRDERWIARSEMRRSSSLSSLHPHLRTLFVRGTKHCLFVWVTDLFSLYCIFGPFVTATIAFQVVEKLLKSLKSHEQRYFIINSTSF
Protein: Heme oxygenase 1, chloroplastic (AtHO1) (EC 1.14.14.18) (Protein GENOMES UNCOUPLED 2) (Protein REVERSAL OF THE DET PHENOTYPE 4) (O48782)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Key enzyme in the synthesis of the chromophore of the phytochrome family of plant photoreceptors. Catalyzes the opening of the heme ring to form the open-chain tetrapyrrole biliverdin IX with the release of iron and carbon monoxide (CO). Produces specifically the biliverdin IX-alpha isomer. Can form complex with heme, is ferredoxin-dependent and its activity is increased in the presence of ascorbate. Plays a role in salt acclimation signaling. May affect the plastid-to-nucleus signaling pathway by perturbing tetrapyrrole synthesis. The plastid-to-nucleus signal plays an important role in the coordinated expression of both nuclear- and chloroplast-localized genes that encode photosynthesis-related proteins.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:10072395, ECO:0000269|PubMed:19860740}.
Interaction partners:
- Phytochromobilin:ferredoxin oxidoreductase, chloroplastic
- Ferrochelatase-1, chloroplastic/mitochondrial
- Ferrochelatase-2, chloroplastic
- Frataxin, mitochondrial
- Protoheme IX farnesyltransferase, mitochondrial
- Tetrapyrrole-binding protein, chloroplastic
- Heme oxygenase 4, chloroplastic
- Heme oxygenase 3, chloroplastic
- Pentatricopeptide repeat-containing protein GUN1, chloroplastic
- SOUL heme-binding family protein
Sequence:
MAYLAPISSSLSIFKNPQLSRFQFSSSSPNPLFLRPRIQILSMTMNKSPSLVVVAATTAAEKQKKRYPGESKGFVEEMRFVAMRLHTKDQAKEGEKETKSIEERPVAKWEPTVEGYLRFLVDSKLVYDTLELIIQDSNFPTYAEFKNTGLERAEKLSTDLEWFKEQGYEIPEPTAPGKTYSQYLKELAEKDPQAFICHFYNIYFAHSAGGRMIGRKVAERILDNKELEFYKWDGELSQLLQNVREKLNKVAEEWTREEKNHCLEETEKSFKYSGEILRLILS
Protein: Protein S100 (S100 calcium-binding protein) (W5UM31)
Organism: Ictalurus punctatus (Channel catfish) (Silurus punctatus)
Interaction partners:
Sequence:
MSDLQKGMALLISTFHKYSGKEGDKCTLTKGELKDLLTKELEGAFGNCSDQATLDKIFKDLDTNADGVVDFQEYATMVACTTMLCNKSLSKK
Protein: Major vault protein beta (MVP-beta) (P54659)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Unknown, though MVP-beta is required for normal vault structure.
Subcellular location: Cytoplasm. Nucleus {ECO:0000250}.
Interaction partners:
- Poly [ADP-ribose] polymerase
- Poly [ADP-ribose] polymerase
- Poly [ADP-ribose] polymerase
Sequence:
MATPVQASTVIRVKPHHYIHVLDNNTNVTRVEVGPQTFTRQDHERVLNPTPLPMILIPPRQYCIIENPIIRDKEGKLVVDKFNQPKLRHGDQEIRFSQDPFPLYPGEVVIAQPVPLQVIQTNSALRLKCLRDFVEVKADKTTVSHIAGDEWLFEGPGTYYPRVEVQVVEPVRAVIIKENQALKLRARLSFVDRRDVVRQVGEEWLVRESGAYLPGVSEEIVGFIQALVLTDRIAYQLLATRSFTDSFGKVRKAGEEWIITQKDCDTYIPDVNEKVIRDIKAITLTNRQYCIVENPIDPKTGKNKLGHKELLQGDRTFFLMPGESLVKGIQNVNVLSEDEALLLSAKEEFVEKKGTTTIVHKPGDLWMIYGPCDYIPPIQVDVVERRKRIPLDVNEGIYVRDIKTGKVRSVHGSSYMLLPNEERWAKPLAPIVEELLKKSASRDQNEEHNESDRDSTKVITYRVPHNAAVQIFDYRKKEARVVFGPELVMLEPDEEFTVLSLSGKIPKRPNHIRSLALFLGPDFMTDLITVETADHARLSLKLSYNWHFKVEQDNPSKLFATSDFTGDLCKATGSLVRAAVAASTFDNFHKHSSDIIQQAVFGSTDGSSNDCLYFETNGLVITNIDVQSVEPVDQRTLDSLQKSVQLAIEITTKSQEATARQEAERLEQMARGELERQKIIDEAKNEESRSKLVQLQAQSAAVESTGQAVAEARARAEAAIIEAESEIKQARLSTRAIEIEALSEIENLKAKHIVEIQHIKSLNNLELIKAKESATIETTKFENYVEALGSDTIKSIAQAPEETKAKLLAGLGLKSFMITDGKSPLNLFDTANGLIADAQRSEVDEE
Protein: Protein ECM19 (Extracellular mutant protein 19) (Q06011)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May be involved in cell wall organization and biogenesis.
Subcellular location: Mitochondrion membrane {ECO:0000269|PubMed:16823961}; Single-pass membrane protein {ECO:0000269|PubMed:16823961}.
Interaction partners:
- mRNA-binding protein PUF3
Sequence:
MDWLKNTTIVVLFSHSTDKSNKHKKRQVQCNMRKNTLDMVTIGIACLVGVYTGTRFFEPIVIDRLRKDGNLRTDIPIPEYDEDGNLLKVTPSLSSTPAAPPTPPTPPTPPQQ
Protein: Ubiquitin associated and SH3 domain containing, B (A0A8I5YC04)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MLTRRQKALASTGGRSVQAACDWLFSHVGDPFLDDPLPREYVLYLRPTGPLAQKLSDFWQQSKQICGKNKAHNIFPHITLCQFFMCEDSKVDALGEALQTTVSRWRCKFSAPLPLELYTSSNFIGLFVKEDSAEVLKKFAADFAAEAASKTEVHVEPHKKQLHVTLAYHFQASHLPTLEKLAQNIDVKLGCDWVATIFSRDIRFANHETLQVIYPYSPQNDDELELVPGDFIFMSPMEQTSTSEGWIYGTSLTTGCSGLLPENYITKADECSTWIFHGSCSILNTVSSSALAFGDGALERRQYEDQGLGETTPLTIICQPMQPLRVNSQPGPQKRCLFVCRHGERMDVVFGKYWLSQCFDAKGRYIRTNLNMPHSLPQRSGSFRDYEKDAPITVFGCMQARLVGEALLESNTVIDHVYCSPSLRCVQTAHNILKGLQQDNHLKIRVEPGLFEWTKWVAGSTLPAWMPPSELAAANLSVDTTYRPHIPVSKLVISESYDTYINRSFQVTKEIISECKSKGNNILIVAHASSLEACTCQLQGLSPQNSKDFVQMVRKIPYLGFCSCEELGETGIWQLTDPPILPLTHGPTGGFNWRETLLQE
Protein: Collagen alpha-1(III) chain (P13941)
Organism: Rattus norvegicus (Rat)
Function: Collagen type III occurs in most soft connective tissues along with type I collagen. Involved in regulation of cortical development. Is the major ligand of ADGRG1 in the developing brain and binding to ADGRG1 inhibits neuronal migration and activates the RhoA pathway by coupling ADGRG1 to GNA13 and possibly GNA12 (By similarity).
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
Interaction partners:
- Collagen alpha-1
- Collagen alpha-2
- Collagen type V alpha 2 chain
- Lumican
- Collagen alpha-1
- Integrin alpha-2
- Integrin beta-1
- Procollagen C-endopeptidase enhancer 1
- Decorin
- Fibrillin-1
Sequence:
MMSFVQCGTWFLLTLLHPSLILAQQSNVDELGCNYLGQSYESRDVWKPEPCQICVCDSGSVLCDDIMCDDEPLDCPNPEIPFGECCAICPQPSTPAPVIPDGNRPQGPKGDPGPPGIPGRNGDPGLPGQPGLPGPPGSPGICESCPTGGQNYSPQFDSYDVKSGVGGMGGYPGPAGPPGPPGPPGSSGHPGSPGSPGYQGPPGEPGQAGPAGPPGPPGAIGPSGPAGKDGESGRPGRPGERGLPGPPGIKGPAGIPGFPGMKGHRGFDGRNGEKGETGAPGLKGENGLPGDNGAPGPMGPRGAPGERGRPGLPGAAGARGNDGARGSDGQPGPPGPPGTAGFPGSPGAKGEVGPAGSPGSNGSPGQRGEPGPQGHAGAQGPPGPPGNNGSPGGKGEMGPAGIPGAPGLLGARGPPGPAGANGAPGQRGPSGEPGKNGAKGEPGARGERGEAGSPGIPGPKGEDGKDGSPGEPGANGVPGNPGERGAPGFRGPAGPNGAPGEKGPAGERGGPGPAGPRGVAGEPGRDGTPGGPGIRGMPGSPGGPGNDGKPGPPGSQGESGRPGPPGPSGPRGQPGVMGFPGPKGNDGAPGKNGERGGPGGPGLPGPAGKNGETGPQGPPGPTGAPGDKGDAGPPGPQGLQGIPGTSGPPGENGKPGEPGPKGEAGAPGVPGGKGDSGAPGERGPPGTAGTPGLRGGAGPPGPEGGKGPAGPPGPPGTSGPPGLQGMPGERGGPGSPGPKGEKGEPGGAGADGVPGKDGPRGPAGPIGPPGPAGQPGDKGEGGAPGLPGIAGPRGGPGERGEHGPPGPAGFPGAPGQNGEPGAKGERGAPGEKGEGGPPGAAGPPGGSGPAGPPGPQGVKGERGSPGGPGAAGFPGGRGLPGPPGNNGNPGPPGPSGAPGKDGPPGPAGNSGSPGNPGVAGPKGDAGQPGEKGPPGAQGPPGSPGPLGIAGLTGARGLAGPPGMPGPRGSPGPQGIKGESGKPGASGHNGERGPPGPQGLPGQPGTAGEPGRDGNPGSDGQPGRDGSPGGKGDRGENGSPGAPGAPGHPGPPGPVGPSGKNGDRGETGPAGPSGAPGPAGARGAPGPQGPRGDKGETGERGSNGIKGHRGFPGNPGPPGSPGAAGHQGAVGSPGPAGPRGPVGPHGPPGKDGSSGHPGPIGPPGPRGNRGERGSEGSPGHPGQPGPPGPPGAPGPCCGGGAAIAGVGGEKSGGFSPYYGDDPMDFKINTEEIMSSLKSVNGQIESLISPDGSRKNPARNCRDLKFCHPELKSGEYWVDPNQGCKMDAIKVFCNMETGETCINASPMTVPRKHWWTDAGAEKKHVWFGESMNGGFQFSYGNPDLPEDVLDVQLAFLRLLSSRASQNITYHCKNSIAYMDQANGNVKKSLKLMGSNEGEFKAEGNSKFTYTVLEDGCTKHTGEWSKTVFEYQTRKAMRLPIIDIAPYDIGGPDQEFGVDIGPVCFL
Protein: Low molecular weight neuronal intermediate filament (XNIF) (P35617)
Organism: Xenopus laevis (African clawed frog)
Interaction partners:
Sequence:
MTSRELYTSSYKKIFGDWGRSSSLLYTTNSSSSTRSQSYRPREAYTSNISSYRKVSRSPGHLSSAQDHFDLSQSTALSNELKIVRTNEKEQLQGLNDRFVTYIEKVHHLEQQNKLLESEVTLLRQKHSEPSRLSHIYEQEIRELRSKLEEQEQDKDQAQLDYEHLGACLEQLKLKLEQESARREEAEDVMKNYRKDLDQATLNRLQLEKKVESLLDEIAFLRKVHEEEIAELQASVQEAQISVEMDVVSKPDLTAALKEIRMQYEVLSARNQQSSEEWYQAKIANVSLEASRNNDSVRQAKEEITEYRRQLQARTLEIDALRSANESLERQLQEAEDRSNEEMSHLQDTIGQLDNALRTTKEEMARHLREYQDLLNVKMALDIEIAAYRKLLEGEETRLTSVGGGSMFGIGYPFSSGSYSGGRSSTTSTISIRKEEKKESPEGGKGGSSGQPKTSKPGDQEKISQKAAAN
Protein: Replication factor A protein 1 (RF-A protein 1) (DNA-binding protein BUF2) (Replication protein A 69 kDa DNA-binding subunit) (Single-stranded DNA-binding protein) (P22336)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: As part of the replication protein A (RPA/RP-A), a single-stranded DNA-binding heterotrimeric complex, may play an essential role in DNA replication, recombination and repair. Binds and stabilizes single-stranded DNA intermediates, preventing complementary DNA reannealing and recruiting different proteins involved in DNA metabolism. Binds to single-stranded sequences participating in DNA replication in addition to those mediating transcriptional repression (URS1) and activation (CAR1). Stimulates the activity of a cognate strand exchange protein (SEP1). It cooperates with T-AG and DNA topoisomerase I to unwind template DNA containing the simian virus 40 origin of DNA replication.
Subcellular location: Nucleus.
Interaction partners:
- Replication factor A protein 3
- ATP-dependent helicase SGS1
- Replication factor A protein 2
- DNA repair and recombination protein RAD52
- DNA replication ATP-dependent helicase/nuclease DNA2
- Serine/threonine-protein kinase MEC1
- DNA repair protein RAD51
- DNA repair protein RAD1
- Topoisomerase 1-associated factor 1
- DNA repair protein RAD59
Sequence:
MSSVQLSRGDFHSIFTNKQRYDNPTGGVYQVYNTRKSDGANSNRKNLIMISDGIYHMKALLRNQAASKFQSMELQRGDIIRVIIAEPAIVRERKKYVLLVDDFELVQSRADMVNQTSTFLDNYFSEHPNETLKDEDITDSGNVANQTNASNAGVPDMLHSNSNLNANERKFANENPNSQKTRPIFAIEQLSPYQNVWTIKARVSYKGEIKTWHNQRGDGKLFNVNFLDTSGEIRATAFNDFATKFNEILQEGKVYYVSKAKLQPAKPQFTNLTHPYELNLDRDTVIEECFDESNVPKTHFNFIKLDAIQNQEVNSNVDVLGIIQTINPHFELTSRAGKKFDRRDITIVDDSGFSISVGLWNQQALDFNLPEGSVAAIKGVRVTDFGGKSLSMGFSSTLIPNPEIPEAYALKGWYDSKGRNANFITLKQEPGMGGQSAASLTKFIAQRITIARAQAENLGRSEKGDFFSVKAAISFLKVDNFAYPACSNENCNKKVLEQPDGTWRCEKCDTNNARPNWRYILTISIIDETNQLWLTLFDDQAKQLLGVDANTLMSLKEEDPNEFTKITQSIQMNEYDFRIRAREDTYNDQSRIRYTVANLHSLNYRAEADYLADELSKALLA
Protein: Collagen alpha-1(VI) chain (P12109)
Organism: Homo sapiens (Human)
Function: Collagen VI acts as a cell-binding protein.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
Interaction partners:
- Collagen alpha-2
- Collagen alpha-3
- Collagen alpha-1
- Platelet glycoprotein VI
- Collagen alpha-1
- CD44 antigen
- Integrin alpha-5
- Collagen alpha-2
- Integrin alpha-V
- Collagen alpha-1
Sequence:
MRAARALLPLLLQACWTAAQDEPETPRAVAFQDCPVDLFFVLDTSESVALRLKPYGALVDKVKSFTKRFIDNLRDRYYRCDRNLVWNAGALHYSDEVEIIQGLTRMPGGRDALKSSVDAVKYFGKGTYTDCAIKKGLEQLLVGGSHLKENKYLIVVTDGHPLEGYKEPCGGLEDAVNEAKHLGVKVFSVAITPDHLEPRLSIIATDHTYRRNFTAADWGQSRDAEEAISQTIDTIVDMIKNNVEQVCCSFECQPARGPPGLRGDPGFEGERGKPGLPGEKGEAGDPGRPGDLGPVGYQGMKGEKGSRGEKGSRGPKGYKGEKGKRGIDGVDGVKGEMGYPGLPGCKGSPGFDGIQGPPGPKGDPGAFGLKGEKGEPGADGEAGRPGSSGPSGDEGQPGEPGPPGEKGEAGDEGNPGPDGAPGERGGPGERGPRGTPGTRGPRGDPGEAGPQGDQGREGPVGVPGDPGEAGPIGPKGYRGDEGPPGSEGARGAPGPAGPPGDPGLMGERGEDGPAGNGTEGFPGFPGYPGNRGAPGINGTKGYPGLKGDEGEAGDPGDDNNDIAPRGVKGAKGYRGPEGPQGPPGHQGPPGPDECEILDIIMKMCSCCECKCGPIDLLFVLDSSESIGLQNFEIAKDFVVKVIDRLSRDELVKFEPGQSYAGVVQYSHSQMQEHVSLRSPSIRNVQELKEAIKSLQWMAGGTFTGEALQYTRDQLLPPSPNNRIALVITDGRSDTQRDTTPLNVLCSPGIQVVSVGIKDVFDFIPGSDQLNVISCQGLAPSQGRPGLSLVKENYAELLEDAFLKNVTAQICIDKKCPDYTCPITFSSPADITILLDGSASVGSHNFDTTKRFAKRLAERFLTAGRTDPAHDVRVAVVQYSGTGQQRPERASLQFLQNYTALASAVDAMDFINDATDVNDALGYVTRFYREASSGAAKKRLLLFSDGNSQGATPAAIEKAVQEAQRAGIEIFVVVVGRQVNEPHIRVLVTGKTAEYDVAYGESHLFRVPSYQALLRGVFHQTVSRKVALG
Protein: SD02553p (Q8T9G0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKITPWLKKDCYAVRIKKKGMTFPTPNAAGKITHPTSSAKKAIRKEARPNGLAQIQEEGPTATNSPIESTYLPVAHMKSVSIDGSSGTSATFESPAKKAPKRGIRETSPLNGNELQQLISTIPIADEKASSLMEKVDNCIGRESFDDRNKDFMHMENSSTKTAVEKSTKQKRVSGKKSEIPKSIITNNEILEKNSTETLSEKQVAAKAKKQSVRKTGATGKPSTSRLKKSEKTKTTSSVTSTSKLEQVREEESDVSSEVLAKPKPQCSTTASILKQGGDGASNSEDDLQIALAMSKATYKEEQQKRKKTKREPSNKQPQSPAEKSMTVFNNQSVACNSTALANDTACYRVLPKRRGVKRAAAVSTTEEKTATNSSSSPTSSLEEMGSPTGGDPDCTVVTSTTGCEPPASERQEIPATIKITKRGILLHSPSAPEGASFTLTEQGLGKIIGERWARKYLKYHIGSRSFDSRHSVYYQPTPQLAAALSAPQDAQNIGNISGSSASDDDIFEQINRYGTVYSILENNSGDK
Protein: Conserved oligomeric Golgi complex subunit 1 (COG complex subunit 1) (Component of oligomeric Golgi complex 1) (Q9VGC3)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for normal Golgi function.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
Interaction partners:
- Conserved oligomeric Golgi complex subunit 8
- Conserved oligomeric Golgi complex subunit 7
- Conserved oligomeric Golgi complex subunit 6
- Conserved oligomeric Golgi complex subunit 4
- Conserved oligomeric Golgi complex subunit 2
- Conserved oligomeric Golgi complex subunit 3
- Conserved oligomeric Golgi complex subunit 5
- Vacuolar protein sorting-associated protein 51 homolog
- Vacuolar protein sorting-associated protein 52 homolog
- Vacuolar protein sorting-associated protein 53 homolog
Sequence:
MTANLLNLNVDTLFEQHSVSEIDEVHKKIQSVVENKREELRTHVGERYRDLLQAADTIAAMQTSAGTLMEQVRHVQANCRSLNEQQLLGFQSTANASAKDAALKERNAGKKLQTYYGTMAQIKLLTALPELIWTHLDNDRFYAATELFIFSRHISTGLQLDGQSALMQKLPVARKQWEILRPFHVTIKQAILTALEREELLQEMTVDCLQSLLLLDKSDLSTVLKSFLNLRSSAFLNCLQSGPSEPRRVKDRILASLNVLNSTVELLDKCLLGYSLLFSRLEECASSTCPPSINRMESSERQLVHLLPEIIAGFKPQFDVPQLTPEQLGSSLQQWLDKMNALAAAHLQQVFALVTNMQTIQDIKSAARTNGRPDFVRLEQQLHLKRSQLDFYARKYVPLINARVREIIRSSWASAMKLTYEQVLLLIEAGQSQPPLQIWREQSDDLPLSLAAALSDQPKRLANRTKGYDGATIELCKRFDSHLADIVQELNVMLQEQTTRAEDKVSLIEFLRETAEEQLTEYLSNLKGLELRERPALLLALRNSLALVELCPNLKLCFCQPSSWRQWTDNSAGLGIEHWQRICGLIEKEMLSFWLVIVDDVLAGHNCEEKLPKVINHEVVLSDFALWQTLTLEQRDEDQEQSVQSTIRIPSQPRLSLQTYLHQLIQALNSVVPQTLPPKVLQAFIQRLIGKLLCHYEGLAHAECTKASQNIALQLYFDLKFLERVFAISREERTLYDQIHAQQNQLRDYIDPFDFELFAEHITAHVSRAASRLQGELGVLTPSAAAPSQGAAAASSLAHEADPNVLCLSSSGSTSLWFPLLPIVMPQAAGRVTSAERKSPIQEPVEKTATTTPTRKSGGNGARKGDSSKSKSSAASFFGMSQEWFR
Protein: Uncharacterized protein, isoform B (B7Z087)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGGGFAAPPITLASNQRPVALDQVEIPIPATDMHEKLLEKEGKTERTNLLGRSKDKPPKDKPPKQSKFAERLRRSFRRGDHRSLEIKRQEPTPEELKAKSRATPPPPSTLRSDNNNRLPFALSHLNLPGLGLGVGVGVGGHINPALLLDSPDECTPPEYAYQHLSSVATTNSSTSLESSCELGELSGSQNSVYYWASMGGEVSTSAGAAGADGTAGTGAGTGAGAGAAVPIEGQDRRRLETQNSSRSDQQPITTNASSAPGNSSRSCSLTSDSSSIRLTRLQNFLFKSSNESSRSCQGHSNEGFTVSSHNSSSGEWEQLGAYLSSSSGVGGGHDFQGGSFPEESTPDETDGTLPVETSSSGGGGGYYQYTLTSPNNPFLPEITARTYHSTYGEDGAVEGGEPTTDDLQLDGKYGCAGSRSAQLPTPSYSRAGSQESTHSEGGGPPGPTPSPASSSSSTPGRHRRKLFSLNSPTRLLHHQQQQPPPSGATSASPPSGGSSNDGGGGKFNSASLVRSLNPFLPSVTSPKKAPHKQSAVTSPGCLTPDLSTKREEFLRATMKICLVVSPPNSKLQLKSKSLTHLDGLDSGVVACQQGPPGMATSTASTTATTAGGTGATTGLFATTGAPGSLGRQANVVSSSEFFSVSFCLDSSQQPDEEFIPATKGVTLLNALSHALRRRNLSFTQITITDNNPTPSFLDAGPSLLPVSVDEQTDVESLAGHHLCITERGSNRKPLQKAASFGSRQPPPRLLPSVSTEETSESGVAPGKQIKQRWSSIFGIKNPQQSQLCELLNSYAKNGVPQRPDSMSFDHPDLVNSLAYLQYMHKSWRDFVNSDSMSESEVKIQTAIWELVTTEVYYIHALQTVTDLFLACLEAVQEEGLLIDVDQARLFSNVRAVCEANIKFWTLWLYPMVAHSAITHEPLRCAFFQEGFLSFASIFAPYKIYCAEQSTCQFYCKELNHNNALFTSYLAWCESQKMCNRLRLADIVVRPMQRLTKYSLLLAAIKKHMSDVEEIEAIDVMMHSVENFVGSVNNHLTMRQENERLKGVMVRIESYDVVDTNNEVLDKMIKQNSQMFDLCAPMRGCPAYHVRHLFMEGDHKFKDNLGKSDVHCFLLTDLLLVCKTIAKRGLGALKVIRQPYLTDQLIVQLAPNNTLNCVYLNEFQVATTAFTLQCTEAKNWYDALWRAKTIYQRLKRGGGGGGSGSGTVGGGDSFRFGGSATSGGTADSLGVRKSPMNSSICSHVSSANNSHSGSVEWNDSRNISVDFEKTNSVSSDEGSSIMTGNHGVNLKGKQQLISGLHKTKMGIIGQMGSKSANTLSVQPMNHLGQSLPNLNMHHSHTNNTLLVPGSTTSHSGNMLLSPSHRGISYPPPSPTRVPLRRGMAFSTSTKNPPLRKTRNITSQNSINWHQIPATPTPPSPRSQYQSPGVVCMQKSLPLLLPTNTDEGQGPTQPPPPLQKQLSHQAPLPTTIHNQSSTETDV
Protein: DnaJ homolog subfamily B member 11 (APOBEC1-binding protein 2) (ABBP-2) (ER-associated DNAJ) (ER-associated Hsp40 co-chaperone) (Endoplasmic reticulum DNA J domain-containing protein 3) (ER-resident protein ERdj3) (ERdj3) (ERj3p) (Q99KV1)
Organism: Mus musculus (Mouse)
Function: As a co-chaperone for HSPA5 it is required for proper folding, trafficking or degradation of proteins. Binds directly to both unfolded proteins that are substrates for ERAD and nascent unfolded peptide chains, but dissociates from the HSPA5-unfolded protein complex before folding is completed. May help recruiting HSPA5 and other chaperones to the substrate. Stimulates HSPA5 ATPase activity. It is necessary for maturation and correct trafficking of PKD1.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000269|PubMed:15525676}.
Interaction partners:
- Endoplasmin
- Endoplasmic reticulum chaperone BiP
- Protein disulfide-isomerase A6
- Protein disulfide-isomerase A4
- Stromal cell-derived factor 2-like protein 1
- Stromal cell-derived factor 2
- Hypoxia up-regulated protein 1
- Endoplasmic reticulum resident protein 44
- Peptidyl-prolyl cis-trans isomerase B
- Heat shock cognate 71 kDa protein
Sequence:
MAPQNLSTFCLLLLYLIGTVIAGRDFYKILGVPRSASIKDIKKAYRKLALQLHPDRNPDDPQAQEKFQDLGAAYEVLSDSEKRKQYDTYGEEGLKDGHQSSHGDIFSHFFGDFGFMFGGTPRQQDRNIPRGSDIIVDLEVTLEEVYAGNFVEVVRNKPVARQAPGKRKCNCRQEMRTTQLGPGRFQMTQEVVCDECPNVKLVNEERTLEVEIEPGVRDGMEYPFIGEGEPHVDGEPGDLRFRIKVVKHRIFERRGDDLYTNVTVSLVEALVGFEMDITHLDGHKVHISRDKITRPGAKLWKKGEGLPNFDNNNIKGSLIITFDVDFPKEQLTEEAKEGIKQLLKQGPVQKVYNGLQGY
Protein: 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase (EC 4.1.1.45) (Picolinate carboxylase) (Q8TDX5)
Organism: Homo sapiens (Human)
Function: Converts alpha-amino-beta-carboxymuconate-epsilon-semialdehyde (ACMS) to alpha-aminomuconate semialdehyde (AMS). ACMS can be converted non-enzymatically to quinolate (QA), a key precursor of NAD, and a potent endogenous excitotoxin of neuronal cells which is implicated in the pathogenesis of various neurodegenerative disorders. In the presence of ACMSD, ACMS is converted to AMS, a benign catabolite. ACMSD ultimately controls the metabolic fate of tryptophan catabolism along the kynurenine pathway.
Interaction partners:
- 3-hydroxyanthranilate 3,4-dioxygenase
- 2-aminomuconic semialdehyde dehydrogenase
- Sentrin-specific protease 8
- Kynureninase
- Kynurenine 3-monooxygenase
- Nicotinate-nucleotide pyrophosphorylase [carboxylating]
- Malonyl-CoA decarboxylase, mitochondrial
- Tryptophan 2,3-dioxygenase
- Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial
- Coiled-coil domain-containing protein 62
Sequence:
MKIDIHSHILPKEWPDLKKRFGYGGWVQLQHHSKGEAKLLKDGKVFRVVRENCWDPEVRIREMDQKGVTVQALSTVPVMFSYWAKPEDTLNLCQLLNNDLASTVVSYPRRFVGLGTLPMQAPELAVKEMERCVKELGFPGVQIGTHVNEWDLNAQELFPVYAAAERLKCSLFVHPWDMQMDGRMAKYWLPWLVGMPAETTIAICSMIMGGVFEKFPKLKVCFAHGGGAFPFTVGRISHGFSMRPDLCAQDNPMNPKKYLGSFYTDALVHDPLSLKLLTDVIGKDKVILGTDYPFPLGELEPGKLIESMEEFDEETKNKLKAGNALAFLGLERKQFE
Protein: Beta-glucosidase 40 (AtBGLU40) (EC 3.2.1.21) (Q9FZE0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Endoglucanase 17
Sequence:
MAHRRLIMTMTKMMMMVTMMMMMDKTCICADISRGSFPKGFVFGTASSAFQHEGAVKAEGRGPTIWDTFSHTFGKITDFSNADVAVDQYHRYEEDVQLMKNMGMDAYRFSISWTRIFPNGVGHINEAGIDHYNKLINALLAKGIEPYVTLYHWDLPQALHDRYLGWLNPQIINDFAAYAEVCFQRFGDRVKHWITFNEPHTFAIQGYDVGLQAPGRCTILFKLTCREGNSSTEPYIVGHNVILTHATVSDIYRKKYKAKQGGSLGIAFDVMWFEPESNKTEDIEAAQRAQDFQLGWFLDPLMFGDYPSSMRSRVGSRLPVFTGSQSSLVKGSLDFVGINHYTTYYARNNATNLIGTLLHDAVSDSGTVTLPFKGLSTIGDRASSIWLYIVPRGMRSLMNYIKHRYGNPPVFITENGMDDPNSILISRKDALKDAKRIKYHHDYLSSLQASIKEDGCNVKGYFVWSLLDNWEWAAGYSSRFGLYFVDYRDNLKRYPKDSVHWFTSFLNSTS