wanglab/gogpt-training-data huggingface dataset:
Protein: Cell wall alpha-1,3-glucan synthase mok11 (EC 2.4.1.183) (Q09854)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Alpha-amylase 2
Sequence:
MAYPLVVSFFLYIVILDKHAWCAPFNNLLTDWNLNTNVSALDPSDYWGEWENHEFFPSPEHWRFPIYTIAIDKWVDGDPTNNDFSGTRFEYDIYETEFRNGGDIIGVRQSLDYLQGMGVKAVYFAGTPFVNMPWGADQYSPLDFTLLDPHLGTINDWRGTIEEMHSKGMYVIVDLTVATLADLIGFEGFTNTTTPFTFIEHNALWKGEDRYADWNFTNSWDPDCELPRFWGESGEPVVVEWTGCYNSDFDQYGDTEAFGSHPDWQRQLSKFASVQDRLREWKPSVASKLKRLSCLVISMLDVDGFRIDKATQMTVDFLVDWAKSVRLCANRFNKSNFFIPGEVTGPSSFGAIYYNRGRQPNQRPANLIDALNATSSDNVYFLREEGENALDASAFHYSVYRIILRFLRMDGLMEIPYDLPVDLAEAWHQIVINEDSFNPKTEKYDPRHLYGVSNYDVFRWASVADGSRRLILGTMMTFFLFPGAPLIYYGDEQGLYVLDNSANNYLYGRQSMAAAPAWYIHGCYSGSSSTYPAIDLSPAKIGCLDIWNSLDHFDPSRIERQLFIEFQDIRSRYSALTHGWKSELLGNWTNIEYLPNSGINPSNVGTFSMVRGAINSLQNISSEYNFPGVKTSSSDVWILFTNSNVSVNLKSNCFSKEAIVSPFISGTKIKNLVYPYDEYQLEASSHFSQISNTEPMGCLPELGLDGYGYKLFVPINEYIPRRPFITKFSPSHDSRLVIPLEKLRIIVEFSEEMDCKSISKSLLITSKTLNGDSPVLDESSVTCQKINDKDRVRFSGQSSSLFRWSATFSNIADGIHRISFNNASTADGKDFTHSVDHFLLRVGSLNNPIVFSSANYSYDLLQKENNSVYIKHAAIGADMFRYSLDFGSTWTEWQTYDGNNTYCNLSGWSQSSRYGWKGHHIMVQYWSELTGSSNYMQESDLEYPYKRWFPHVFMDSDYTQWTHDSDIRNRMLPLENGSFLGYHIADVYPSALQFNVWGLNKDGKADKSFIYGSLQNNSFLSRVSPSSLEENVFYIQHPPPKSYLSWSVTFDPQRRRYYINPSGCVFVSLGIYLSSLIVPLLTGVLAVYIFKKKFYHVKFNAFGTSKQNLHFRQHDVLGMKNLFNFSCSNKIKGEEVLNDGDKGKRRTVLLATLEYDIPSLNICIKIGGLGVMAQLMARHLEHEDIIWVIPCVGDVSYSNVEEDDPIEVVIIDQTYFINVYKYVIGNIIYILLDAPIFRRQTSGKPYPSRADDLSSAIFYSAWNQCIASVISRNNIDLYHMNDYHGSLAPLYLLPKIIPVALSLHNAEFQGLWPLRNSSEKEEVCSVFNISKSVCSKYVQFGNVFNLLHAGASYIRIHQKGYGVVGVSSKYGKRSWARYPIFWGLRKIGKLPNPDPADNGTNFKDLDANSMNEFENIKAKHKRSAQEWANLNIDPEADLLIFVGRWTLQKGIDLIADITPTLLENFNSQIVVVGPVIDLYGKFAAEKFTALMKKYPGRIYSRPLFTQLPSYIFSGADFALIPSRDEPFGLVAVEFGRKGTLGIGAKVGGLGQMPGWWYTIESNTTAHLLCQFEEACRQALTSSKSVRTKLRAISTIQRFPVSEWVSKLDTHVRNCIKFSHKQNLEEDFIHEPVIDVDEFAISSSKDIDADEDLEIIGSSDNKAIDSNGEGFLIEKDNIGTGSYSNQQSFDFKSSESDSFPQKSPSVESFSIIDNDNPFHEGQNSSTGYKDIVQGLLAENGVSEAGVDVMTSIVSSTIPIVSNHQTEGSQMFNEISSVSSIHVYHDESQPPVEMPAESDTPLQNKLYHPGMWSSSDIRIPNNSSQLSIDSVRSGMRPFSLSKVPHQFDDEEGKALQIFREKLKDLNCKNSMNEMCIENFLMKCTRKYFDEVRKLRLGTLKPENLQFVKDPSSLALETNLLPASDTIEEKNDVGNKQVNSHILDPGFLKEEECVYEFEQLHGLRKALQVEIYGWPLYTILLAIGQVLAATSFQLNLFSDTPDQPEYQSYIVCSVYISASLFWYILHSLVPNIYALSTPFIIYATAFALAGLTTFSSLGDSRLWISRVATWIYSIASGSQALFFSLNFGNEGRYDILYWIVRACFIQGSQQVWSAALWYWGSYSTDKPNRMGVSGKLNPQPWMAAITWPIALVLLAIAFVVYRGLPNFYRQCPSKIPAFYRSLFRRRLIMWFFISVFLQNYWMSSVYGRSWAFMWSAHNVHKWAMFLLVILFYVAIWIALVALLASLSRYHSWILPILGLGFGAPRWLQTLWGTSNIGIYVPFLGKGAPYLSRMLWLYLGLLDTVQTVGIGIILLQTLTREHITVVLITGQIVGAIASMVGKASSPSKFGPGDVFIDFTHWSVKDGPQILASIPFWVCLICQLSVIIGYFLFFRRENLSRP
Protein: Lin-9 DREAM MuvB core complex component (C9J5J4)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MHRGGQPLKKRRGSFKMAELDQLPDESSSAKALVSLKEGSLSNTWNEKYSSLQKTPVWKGRNTSSAVEMKFTATMSTPDKKASQKIGFRLRNLLKLPKAHKWCIYEWFYSNIDKPLFEGDNDFCVCLKESFPNLKTRKLTRVEWGKIRRLMGKPRRCSSAFFEEERSALKQKRQKIRLLQQRKVADVSQFKDLPDEIPLPLVIGTKVTARLRGVHDGLFTGQIDAVDTLNATYRVTFDRTGLGTHTIPDYEVLSNEPHETMPIAAFGQKQRPSRFFMTPPRLHYTPPLQSPIIDNDPLLGQSPWRSKISGSDTETLGGFPVEFLIQVTRLSKILMIKKEHIKKLREMNTEAEKLKSYSMPISIEFQRRYATIVLELEQLNKDLNKVLHKVQQYCYELAPDQGLQPADQPTDMRRRCEEEAQEIVRHANSSTGQPCVENENLTDLISRLTAILLQIKCLAEGGDLNSFEFKSLTDSLNDIKSTIDASNIR
Protein: Interleukin-17F (IL-17F) (Q7TNI7)
Organism: Mus musculus (Mouse)
Function: Effector cytokine of innate and adaptive immune system involved in antimicrobial host defense and maintenance of tissue integrity. IL17A-IL17F signals via IL17RA-IL17RC heterodimeric receptor complex, triggering homotypic interaction of IL17RA and IL17RC chains with TRAF3IP2 adapter through SEFIR domains. This leads to downstream TRAF6-mediated activation of NF-kappa-B and MAPkinase pathways ultimately resulting in transcriptional activation of cytokines, chemokines, antimicrobial peptides and matrix metalloproteinases, with potential strong immune inflammation. IL17A-IL17F is primarily involved in host defense against extracellular bacteria and fungi by inducing neutrophilic inflammation. As signature effector cytokine of T-helper 17 cells (Th17), primarily induces neutrophil activation and recruitment at infection and inflammatory sites. Stimulates the production of antimicrobial beta-defensins DEFB1, DEFB103A, and DEFB104A by mucosal epithelial cells, limiting the entry of microbes through the epithelial barriers. IL17F homodimer can signal via IL17RC homodimeric receptor complex, triggering downstream activation of TRAF6 and NF-kappa-B signaling pathway. Via IL17RC induces transcriptional activation of IL33, a potent cytokine that stimulates group 2 innate lymphoid cells and adaptive T-helper 2 cells involved in pulmonary allergic response to fungi. Likely via IL17RC, promotes sympathetic innervation of peripheral organs by coordinating the communication between gamma-delta T cells and parenchymal cells. Stimulates sympathetic innervation of thermogenic adipose tissue by driving TGFB1 expression. Regulates the composition of intestinal microbiota and immune tolerance by inducing antimicrobial proteins that specifically control the growth of commensal Firmicutes and Bacteroidetes.
Subcellular location: Secreted {ECO:0000269|PubMed:18025225}.
Interaction partners:
- Interleukin-17 receptor A
- Interleukin-17 receptor C
- Interleukin-17 receptor E
- Interleukin-17A
- Interleukin-22
- Interleukin-25
- Signal transducer and activator of transcription 3
- Interleukin-17 receptor D
- Interferon gamma
- Interleukin-23 receptor
Sequence:
MKCTRETAMVKSLLLLMLGLAILREVAARKNPKAGVPALQKAGNCPPLEDNTVRVDIRIFNQNQGISVPREFQNRSSSPWDYNITRDPHRFPSEIAEAQCRHSGCINAQGQEDSTMNSVAIQQEILVLRREPQGCSNSFRLEKMLLKVGCTCVKPIVHQAA
Protein: TP53-target gene 5 protein (TP53-inducible gene 5 protein) (Q9Y2B4)
Organism: Homo sapiens (Human)
Function: May play a significant role in p53/TP53-mediating signaling pathway.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10719363}. Nucleus {ECO:0000269|PubMed:10719363}. Note=Cell cycle dependent intracellular localization.
Interaction partners:
Sequence:
MSPSAKKRPKNSRVSKMQDEKLRDETEQPVSKVIERNRLRTVLKNLSLLKLLKSSNRRIQELHKLAKRCWHSLLSVPKILRISSGENSACNKTKQNNEEFQEIGCSEKELKSKKLESTGDPKKKEYKEWKSQVQSGMRNKEKTSLAAMPRKEKHIEPEVPRTSRDDSLNPGVQGRQPLTEGPRVIFIKPYRNRTPMGHMKQLDVADQWIWFEGLPTRIHLPAPRVMCRSSTLRWVKRRCTRFCSASLEMPMWHPYKVDVTWTRARGASRGWRSRHQLKGRNGWRNSRVYK
Protein: Nuclear transcription factor Y subunit gamma (CAAT box DNA-binding protein subunit C) (Nuclear transcription factor Y subunit C) (NF-YC) (P70353)
Organism: Mus musculus (Mouse)
Function: Component of the sequence-specific heterotrimeric transcription factor (NF-Y) which specifically recognizes a 5'-CCAAT-3' box motif found in the promoters of its target genes. NF-Y can function as both an activator and a repressor, depending on its interacting cofactors.
Subcellular location: Nucleus.
Interaction partners:
- Nuclear transcription factor Y subunit alpha
- Nuclear transcription factor Y subunit beta
- MHC class II transactivator
- CCAAT/enhancer-binding protein zeta
- DNA polymerase epsilon subunit 3
- Cyclic AMP-dependent transcription factor ATF-2
- Inhibitor of growth protein 2
- Cellular tumor antigen p53
Sequence:
MSTEGGFGGTSSSDAQQSLQSFWPRVMEEIRNLTVKDFRVQELPLARIKKIMKLDEDVKMISAEAPVLFAKAAQIFITELTLRAWIHTEDNKRRTLQRNDIAMAITKFDQFDFLIDIVPRDELKPPKRQEEVRQSVTPAEPVQYYFTLAQQPTAVQVQGQQQGQQTTSSTTTIQPGQIIIAQPQQGQTTPVTMQVGEGQQVQIVQAQPQGQAQQTQSGTGQTMQVMQQIITNTGEIQQIPVQLNAGQLQYIRLAQPVSGTQVVQGQIQTLATNAQQITQTEVQQGQQQFSQFTDGQQLYQIQQVTMPAGQDLAQPMFIQSANQPSDGQTPQVTGD
Protein: Acyl carrier protein 2, chloroplastic (ACP-2) (P25701)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Carrier of the growing fatty acid chain in fatty acid biosynthesis.
Subcellular location: Plastid, chloroplast.
Interaction partners:
- EMBRYO DEFECTIVE 3147
- NADH dehydrogenase 1 beta subcomplex subunit 9
- Putative acyl-activating enzyme 19
- NADH dehydrogenase 1 alpha subcomplex subunit 6
- Probable NADH dehydrogenase 1 alpha subcomplex subunit 12
- NADH dehydrogenase iron-sulfur protein 6
- NADH dehydrogenase iron-sulfur protein 4, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 7
- NADH dehydrogenase 1 alpha subcomplex subunit 2
- NADH dehydrogenase 1 alpha subcomplex subunit 9
Sequence:
MASIAASASISLQARPRQLAIAASQVKSFSNGRRSSLSFNLRQLPTRLTVSCAAKPETVDKVCAVVRKQLSLKEADEITAATKFAALGADSLDTVEIVMGLEEEFGIEMAEEKAQSIATVEQAAALIEELLFEKAK
Protein: Transcription factor Pcc1 (Q585J0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRRMDPDAGGGDHDLLQCVLRLPLPNPEVASIMLQVLRVEPPVPGTSREVQLWADDSARSTVFARLCATQERALRAAVAALLEQTKLVLRTLDAFPVDAPANV
Protein: GTP-binding protein ryh1 (P17608)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in retrograde traffricking of proteins from the endosome to the Golgi. Involved in protein transport to the plasma membrane. Involved in the secretory pathway where it has a role in acid phosphatase secretion. Required also in normal glycosylation trafficking pathways.
Subcellular location: Endosome membrane {ECO:0000269|PubMed:16483310}; Lipid-anchor {ECO:0000305}. Golgi apparatus membrane {ECO:0000269|PubMed:16483310}; Lipid-anchor {ECO:0000305}. Nucleus {ECO:0000269|PubMed:16823372}. Cytoplasm, cytosol {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Probable secretory pathway GDP dissociation inhibitor 1
- Vacuolar protein sorting-associated protein 33
- Guanine nucleotide exchange factor subunit ric1
- Vacuolar morphogenesis protein 6
- Uncharacterized Rab geranylgeranyltransferase C15C4.03
- Protein sat1
- Vacuolar protein sorting-associated protein 9b
- Serine/threonine-protein kinase gad8
- Target of rapamycin complex 2 subunit sin1
- GTP-binding protein ypt3
Sequence:
MSENYSFSLRKFKLVFLGEQSVGKTSLITRFMYDQFDNTYQATIGIDFLSKTMYLEDRTVRLQLWDTAGQERFRSLIPSYIRDSSVAIIVYDITNHNSFVNTEKWIEDVRAERGDDVIIVLVGNKTDLADKRQVTQEEGEKKAKELKIMHMETSAKAGHNVKLLFRKIAQMLPGMENVETQSTQMIDVSIQPNENESSCNC
Protein: Signal peptidase complex catalytic subunit sec11 (EC 3.4.21.89) (O74323)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalytic component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum (By similarity). Specifically cleaves N-terminal signal peptides that contain a hydrophobic alpha-helix (h-region) shorter than 18-20 amino acids (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P15367}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P15367}.
Interaction partners:
- Signal peptidase complex subunit 2
- Signal peptidase complex subunit 1
- Signal peptidase complex subunit 3
- DNA-directed RNA polymerase II subunit rpb7
- Exosome complex component rrp40
- ADP-ribosylation factor guanine nucleotide-exchange factor sec71
- Protein transport protein sec1
Sequence:
MQKLSFRQGLAQILNLLLVLSSAYMGYKTLSFVTDCESPVVVVLSESMEPSFQRGDLLFLDNRNPSFDEAKVPSVFEKIIYGSPVGIGDIVVYSLPDRPIPIVHRVVKLYESENQTHLITKGDNNKIDDVAMFPKSINYLDRENHILGVVRGYFPYLGMITIWLTDYPILKYIMLGGLGLLTLIQKEEQ
Protein: Large ribosomal subunit protein eL21B (60S ribosomal protein L21-B) (Q12672)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}.
Interaction partners:
- Large ribosomal subunit protein eL32
- Large ribosomal subunit protein eL30
- Large ribosomal subunit protein eL38
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein eL20A
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein eL29
- Large ribosomal subunit protein uL3
Sequence:
MGKSHGYRSRTRYMFQRDFRKHGAVHMSTYLKIYKVGDIVDIKANGSIQKGMPHKFYQGKTGVVYNVTKSSVGVIINKMVGNRYLEKRLNLRVEHIKHSKCRQEFLERVKANAAKRAEAKAQGVAVQLKRQPAQPRESRIVSTEGNVPQTLAPVPYETFI
Protein: SCUBE1 protein (Q86TI6)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MGAAAVRWHLCVLLALGTRGRLAGGSGLPGSVDVDECSEGTDDCHIDAICQNTPKSYKCLCKPGYKGEGKQCEDIDECENDYYNGGCVHECINIPGNYRCTCFDGFMLAHDGHNCLDVDECQDNNGGCQQICVNAMGSYECQCHSGFFLSDNQHTCIHRSNEGMNCMNKDHGCAHICRETPKGGVACDCRPGFDLAQNQKDCTLTCNYGNGGCQHSCEDTDTGPTCGCHQKYALHSDGRTCIEKDEAAIERSQFNATSVADVDKRVKRRLLMETCAVNNGGCDRTCKDTATGVRCSCPVGFTLQPDGKTCKGQHVELCGCPCLYWPGQEPPCACIAGPRAGLSGGHV
Protein: histidinol-phosphate transaminase (EC 2.6.1.9) (Imidazole acetol-phosphate transaminase) (Q6FX16)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Histidine biosynthesis trifunctional protein
- Imidazoleglycerol-phosphate dehydratase
- Prephenate dehydrogenase [NADP
- Imidazole glycerol phosphate synthase hisHF
- Tryptophan synthase
- ATP phosphoribosyltransferase
- prephenate dehydratase
- Histidinol-phosphatase
- 1-
- Candida glabrata strain CBS138 chromosome M complete sequence
Sequence:
MTFDLQKIVRPKIFNLEPYRCARDDFTEGILLDANENPHGPRLVGHQDTNLHRYPDPHQLEFKRQMATYRNNSSSFKDLSLPPLTEDNLCLGVGSDESIDAVIRACCVPGKEKILTLPPTYSMYSVCANINDVEVLECPLIYEDNSFQPDSQKVISILSSDPLIKLVFLTSPGNPTGAKIDSNIIIKILESWDGGFVVVDEAYIDFCGGSTAPLVTKYPNLITLQTLSKSFGLAGIRLGMTFATADFAAILNAMKAPYNISSITSEFATKALTKENITLMEKTSREINKEKVRLLKELTALPLIDKHHVGGLDANFIMVRIHGGDNDMAKEVYYKLATQSGVVVRFRGNEIGCKGCLRITVGTVEENTTLISEFKKCLSSYNP
Protein: 2-oxoglutarate (2OG) and Fe(II)-dependent oxygenase superfamily protein (Gibberellin oxidase-like protein) (Q9LUZ1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Lysine-specific demethylase JMJ30
- Cysteine-rich receptor-like protein kinase 2
- Ethylene-responsive transcription factor ERF035
Sequence:
MSISESYPPAFRRVTNDENPPATPVIVQGKDINIPVIDLERLDKEILREACKEWGIFRLENHGVPLALTSRLQEISESLLSLPFEKKRELFAAVKSPLSYFWGTPALNRSGDALKRGAQASNLTMLEGFNVPLSSLSSLSKLPTSTCCDDDAQEEPKLESFRVLMEEYGKHITRIAVSLFEAIAQTLNLELSGNRRSEYLSESTGLIRVYRYPQSSEEAAREALGMEVHTDSSVISILREDESGGLEIMKGEEWFCVKPVANTLIVNLGDMMQAISDDEYKSVTHRVKKRNRKTERHSVCYFVFPKRDCVIKSSNYKLFTYSDFEAQVQADVQSLGTKIGLPRFNPNSPLFL
Protein: Protein L-Myc (Class E basic helix-loop-helix protein 38) (bHLHe38) (Protein L-Myc-1) (V-myc myelocytomatosis viral oncogene homolog) (P12524)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:2548855}.
Interaction partners:
- Protein max
- E1A-binding protein p400
- Zinc finger protein Rlf
- Protein lin-28 homolog A
- Enhancer of polycomb homolog 1
- Transformation/transcription domain-associated protein
- Vacuolar protein sorting-associated protein 72 homolog
- Peptidyl-prolyl cis-trans isomerase E
- Histone acetyltransferase KAT5
- Juxtaposed with another zinc finger protein 1
Sequence:
MDYDSYQHYFYDYDCGEDFYRSTAPSEDIWKKFELVPSPPTSPPWGLGPGAGDPAPGIGPPEPWPGGCTGDEAESRGHSKGWGRNYASIIRRDCMWSGFSARERLERAVSDRLAPGAPRGNPPKASAAPDCTPSLEAGNPAPAAPCPLGEPKTQACSGSESPSDSENEEIDVVTVEKRQSLGIRKPVTITVRADPLDPCMKHFHISIHQQQHNYAARFPPESCSQEEASERGPQEEVLERDAAGEKEDEEDEEIVSPPPVESEAAQSCHPKPVSSDTEDVTKRKNHNFLERKRRNDLRSRFLALRDQVPTLASCSKAPKVVILSKALEYLQALVGAEKRMATEKRQLRCRQQQLQKRIAYLTGY
Protein: Glycosylphosphatidylinositol anchor attachment 1 (E9PPZ9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGLLSDPVRRRALARLVLRLNAPLCVLSYVAGIAWFLALVFPPLTQRTYMSENAMGSTMVEEQFAGGDRARAFARDFAAHRKKSGALPVAWLERTMRSVGLEVYTQSFSRKLPFPDETHERYMVSGTNVYGILRAPRAASTESLVLTVPCGSDSTNSQAVGLLLALAAHFREHDLLGTEAWLEAYHDVNVTGMQSSPLQGRAGAIQAAVALELSSDVVTSLDVAVEGLNGQLPNLDLLNLFQTFCQKGGLLCTLQGKLQPEDWTSLDGPLQGLQTLLLMVLRQASGRPHGSHGLFLRYRVEALTLRGINSFRQYKYDLVAVGKALEGMFRKLNHLLERLHQSFFLYLLPGLSRFVSIGLYMPAVGFLLLVLGLKALELWMQLHEAGMGLEEPGGAPGPSVPLPPSQGVGLASLVAPLLISQAMGLALYVLPVLGQHVATQHFPVAEAEAVVLTLLAIYAAGLALPHNTHRVVSTQAPDRGWMALKLVALIYLALQLGCIALTNFSLGFLLATTMVPTAALAKPHGPRTLYAALLVLTSPAATLLGSLFLWRELQEAPLSLAEGWQLFLAALAQGVLEHHTYGALLFPLLSLGLYPCWLLFWNVLFWK
Protein: B-box type zinc finger family protein (F4JUJ1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MRILCDACENAAAIIFCAADEAALCRPCDEKALHMRLDISKCSESVKRVQIVETSSLIWWIKMGTFCLQSLHLVVHMCNKLASRHVRVGLAEPSNAPCCDICENAPAFFYCEIDGSSLCLQCDMVVHVGGKRTHGRFLLLRQRIEFPGDKPKENNTRDNLQNQRVSTNGNGEANGKIDDEMIDLNANPQRVHEPSSNNNGIDVNNENNHEPAGLVPVGPFKRESEK
Protein: Procathepsin L (EC 3.4.22.15) (Cathepsin L1) [Cleaved into: Cathepsin L; Cathepsin L heavy chain; Cathepsin L light chain] (P25975)
Organism: Bos taurus (Bovine)
Function: Thiol protease important for the overall degradation of proteins in lysosomes (By similarity). Plays a critical for normal cellular functions such as general protein turnover, antigen processing and bone remodeling. Involved in the solubilization of cross-linked TG/thyroglobulin and in the subsequent release of thyroid hormone thyroxine (T4) by limited proteolysis of TG/thyroglobulin in the thyroid follicle lumen (By similarity). In neuroendocrine chromaffin cells secretory vesicles, catalyzes the prohormone proenkephalin processing to the active enkephalin peptide neurotransmitter. In thymus, regulates CD4(+) T cell positive selection by generating the major histocompatibility complex class II (MHCII) bound peptide ligands presented by cortical thymic epithelial cells. Also mediates invariant chain processing in cortical thymic epithelial cells. Major elastin-degrading enzyme at neutral pH. Accumulates as a mature and active enzyme in the extracellular space of antigen presenting cells (APCs) to regulate degradation of the extracellular matrix in the course of inflammation (By similarity). Secreted form generates endostatin from COL18A1 (By similarity). Critical for cardiac morphology and function. Plays an important role in hair follicle morphogenesis and cycling, as well as epidermal differentiation (By similarity). Required for maximal stimulation of steroidogenesis by TIMP1 (By similarity).
Subcellular location: Lysosome {ECO:0000250|UniProtKB:P06797}. Apical cell membrane {ECO:0000250|UniProtKB:P06797}; Peripheral membrane protein {ECO:0000250|UniProtKB:P06797}; Extracellular side {ECO:0000250|UniProtKB:P06797}. Cytoplasmic vesicle, secretory vesicle, chromaffin granule {ECO:0000269|PubMed:12869695}. Secreted, extracellular space {ECO:0000250|UniProtKB:P06797}. Secreted {ECO:0000250|UniProtKB:P06797}. Note=Localizes to the apical membrane of thyroid epithelial cells. Released at extracellular space by activated dendritic cells and macrophages. {ECO:0000250|UniProtKB:P06797}.
Interaction partners:
- Ia antigen-associated invariant chain
- Cathepsin S
- Serpin family B member 13
- Cystatin-A
- Apoptosis regulator Bcl-2
- BH3-interacting domain death agonist
- Cathepsin L
- Bcl-2-like protein 1
- Transmembrane protease serine 2
- Cathepsin D
Sequence:
MNPSFFLTVLCLGVASAAPKLDPNLDAHWHQWKATHRRLYGMNEEEWRRAVWEKNKKIIDLHNQEYSEGKHGFRMAMNAFGDMTNEEFRQVMNGFQNQKHKKGKLFHEPLLVDVPKSVDWTKKGYVTPVKNQGQCGSCWAFSATGALEGQMFRKTGKLVSLSEQNLVDCSRAQGNQGCNGGLMDNAFQYIKDNGGLDSEESYPYLATDTNSCNYKPECSAANDTGFVDIPQREKALMKAVATVGPISVAIDAGHTSFQFYKSGIYYDPDCSSKDLDHGVLVVGYGFEGTDSNNNKFWIVKNSWGPEWGWNGYVKMAKDQNNHCGIATAASYPTV
Protein: Kallikrein related-peptidase 6 (A0A0B6VLS7)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MKMLALCLVLAKSAWSEEQEKVVHGGPCLKDSHPFQAALYTSGHLLCGGVLIDSQWVLTAAHCKKPNMEVFLGKHNLRQTETFQRQISVDRTIVHPRYNPETHDNDIMMVHLKNPVKFSKKIQPLPLRNDCSEENPNCQILGWGKMENGDFPDTIQCADVHLVPREQCEHAYPGKITQSMVCAGDMKEGNDSCQGDSGGPLVCGGRLRGLVSWGDMPCGSKEKPGVYTDVCTHIRWIQNILRNKWL
Protein: Secretory carrier-associated membrane protein 4 (SCAMP-4) (Secretory carrier membrane protein 4) (Q9ET20)
Organism: Rattus norvegicus (Rat)
Function: Probably involved in membrane protein trafficking.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- tRNA-dihydrouridine
Sequence:
MAGKENNFPPLPHFLPLKPCFYQDFSDEIPVEHQVLVKRIYRLWMFYCTTLGVNLVACLAWWIAGGAGANFGLAMLWLVLFTPCSYVCWFRPAYKAFRADSSFNFMAFFFIFGAQFVLTVIQAIGFSGWGACGWLATIGFFGTSVGAAVVMLIPAIMFSLSAVVMAITIVKVHRIYRGAGGSLQKAQTEWSAGTWRNPPSREAQFNSFSGNSLPEYPTVPSYSTSGSQWP
Protein: Glutamate dehydrogenase, putative (EC 1.4.1.2) (Q8IAM0)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- glutamate synthase
- Glutamine synthetase, putative
- Aspartate aminotransferase
- Isocitrate dehydrogenase
- 2-oxoglutarate dehydrogenase E1 component
- Glutamate dehydrogenase
- Glutamate dehydrogenase
- Citrate synthase
- Dihydrolipoyl dehydrogenase, apicoplast
- Dihydrolipoyl dehydrogenase
Sequence:
MDIDRRSALSCSPNNMECGFGSGHFSNNSITWKEKYEQTKELLKSYNLFSDHLINYSIDFYFNKLGFNKFHFEETSPELISKVVVCIITAKINEQYSSDKYFPTFEETHDNVIFIITRVFADDNKTRLNYKMEKKIEEKYFNFSDMSKDCYRLKSFRSVHSVFDKEHTYQEPLRTYILELPTYNDDIIKENETDLKKLMDVNFYNYIKGTRSEQIYYELNKAVLYDLTGQFLQTHYYETSSSTFTLTIAVKRSNVISSIFSLIGDCLNMHRCFSYSKYVEPLKNGVLLIILNVKVIVNNEMEREKQKLDLKDKIYKVVKSLKTLCLFNDSKFIQLSVKRTFTAQESAYLFMIIKFITFFSTNTLSSYKNVEHALNLRNYNNNIMDTTTNSSSSPSSVLNDVYIIKEKLKSSKYTKEEILRCAQSNVRTIKMLFANFEKKLNHQRNKCNQMKYGENNMKNSGDLLKEYSTNNRNVDHPTLSSLASSSSSCSSSFSLHSYLSGSYESPYYHHNKDSKDIIDEIEDNHDKKILQYFYMFEKYALKTNFFLTHKISLAVAFDGALLKDSIYEAQPYSIIMILGLHFVGFHIRFSKISRGGVRIVISNNVNSYMHNSDNLFDEAYNLAYTQNFKNKDIPEGGSKGIILLDADVCNVANTKYIKNLSFYSYVNSILDLLINEDLNEESASSISVHSTKGANNTTITFDNVMSSVENMVDRGGVEGEHLNITLPYDANMACNNNTTNDNLSNMHDTYNLNNSGEATLDHHSVDNRIVSNSSGTNNMNAQKGEGEDEKAKDKEMSNNRKNEENERKRCDNVSNSNYNYVNGTTEDAVQKIMGSKCKGGRNNNGEEKDGDMNGHNNNNNDNNNIDDDEHIEECYKGAGCVINGENKTRKMILQEKMNEEEDLIFLGPDENTGSDQLMDWACIIAKKRKYPYWKTFSTGKLRKNGGVPHDMYGMTTLGIETYISKLCEKLNIKEESISRSLVGGPDGDLGSNAILQSKTKIISIIDGSGILYDKQGLNKEELIRLAKRRNNKDKSKAITCCTLYDEKYFSKDGFKISIEDHNVDIFGNKIRNGLDFRNTFFLNPLNKCELFNPCGGRPHSINIFNVNNIIKNGECIYKYIVEGANVFISDDARNILESKNVILFKDAATNKGGVISSSLEVLAGLVLDDKQYIDYMCSPDSDILQVDENEINFVHQNQKMNHSLSFKRGSINNLEEDEKKDTSNNEKNKNIIKTVNKNDTQDNSHHHNNSNKCNEDQQDVSDFYKAYVKEIQKKITHYCELEFESLWKETRRTKTPISKAINILSNKISELKKDILSSDTLCRDYKLLKKVLERVIPPTLLKIVTFEQILERVPYVYIKSLFASSLASNYYYSQQFLNDLSAFNFFEYITKLQSESA
Protein: Cell division topological specificity factor (P58152)
Organism: Neisseria gonorrhoeae
Function: Prevents the cell division inhibition by proteins MinC and MinD at internal division sites while permitting inhibition at polar sites. This ensures cell division at the proper site by restricting the formation of a division septum at the midpoint of the long axis of the cell (By similarity).
Interaction partners:
Sequence:
MSLIELLFGRKQKTATVARDRLQIIIAQERAQEGQTPDYLPTLRKELMEVLSKYVNVSLDNIRISQEKQDGMDVLELNITLPEQKKV
Protein: Caprin family member 2 (F5H142)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MKSAKPQVNHSQHGESQRALSPLQSTLSSAASPSQAYETYIENGLICLKHKIRNIEKKKLKLEDYKDRLKSGEHLNPDQLEAVEKYEEVLHNLEFAKELQKTFSGLSLDLLKAQKKAQRREHMLKLEAEKKKLRTILQVQYVLQNLTQEHVQKDFKGGLNGAVYLPSKELDYLIKFSKLTCPERNESLSVEDQMEQSSLYFWDLLEGSEKAVVGTTYKHLKDLLSKLLNSGYFESIPVPKNAKEKEVPLEEEMLIQSEKKTQLSKTESVKESESLMEFAQPEIQPQEFLNRRYMTEVDYSNKQGEEQPWEADYARKPNLPKRWDMLTEPDGQEKKQESFKSWEASGKHQEVSKPAVSLEQRKQDTSKLRSTLPEEQKKQEISKSKPSPSQWKQDTPKSKAGYVQEEQKKQETPKLWPVQLQKEQDPKKQTPKSWTPSMQSEQNTTKSWTTPMCEEQDSKQPETPKSWENNVESQKHSLTSQSQISPKSWGVATASLIPNDQLLPRKLNTEPKDVPKPVHQPVGSSSTLPKDPVLRKEKLQDLMTQIQGTCNFMQESVLDFDKPSSAIPTSQPPSATPGSPVASKEQNLSSQSDFLQEPLQATSSPVTCSSNACLVTTDQASSGSETEFMTSETPEAAIPPGKQPSSLASPNPPMAKGSEQGFQSPPASSSSVTINTAPFQAMQTVFNVNAPLPPRKEQEIKE
Protein: Family with sequence similarity 114 member A1 (D6R9C9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSDDAGDTLATGDKAEVTEMPNSDSLPEDAEVHCDSAAVSHEPTPADPRGEGHENAAVQGAGAAAIGPPVQPQDANALEPPLNGDVTEDTLAECIDSVSLEAEPRSEIPLQEQNYLAVDSPPSGGGWAGWGSW