wanglab/gogpt-training-data huggingface dataset:
Protein: Leucine-rich repeat and calponin homology domain-containing protein 1 (Calponin homology domain-containing protein 1) (Neuronal protein 81) (NP81) (Q9Y2L9)
Organism: Homo sapiens (Human)
Function: Acts as a negative regulator of GTPase CDC42 by sequestering CDC42-guanine exchange factor DOCK8. Probably by preventing CDC42 activation, negatively regulates CD4(+) T-cell migration.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:28028151}.
Interaction partners:
- Dedicator of cytokinesis protein 8
- Dedicator of cytokinesis protein 7
- DISP complex protein LRCH3
- Dedicator of cytokinesis protein 6
- Leucine-rich repeat and calponin homology domain-containing protein 4
- Thioredoxin domain-containing protein 3
Sequence:
MATPGSEPQPFVPALSVATLHPLHHPHHHHHHHQHHGGTGAPGGAGGGGGGSGGFNLPLNRGLERALEEAANSGGLNLSARKLKEFPRTAAPGHDLSDTVQADLSKNRLVEVPMELCHFVSLEILNLYHNCIRVIPEAIVNLQMLTYLNLSRNQLSALPACLCGLPLKVLIASNNKLGSLPEEIGQLKQLMELDVSCNEITALPQQIGQLKSLRELNVRRNYLKVLPQELVDLSLVKFDFSCNKVLVIPICFREMKQLQVLLLENNPLQSPPAQICTKGKVHIFKYLSIQACQIKTADSLYLHTMERPHLHQHVEDGKKDSDSGVGSDNGDKRLSATEPSDEDTVSLNVPMSNIMEEEQIIKEDSCHRLSPVKGEFHQEFQPEPSLLGDSTNSGEERDQFTDRADGLHSEFMNYKARAEDCEELLRIEEDVHWQTEGIISSSKDQDMDIAMIEQLREAVDLLQDPNGLSTDITERSVLNLYPMGSAEALELQDSALNGQIQLETSPVCEVQSDLTLQSNGSQYSPNEIRENSPAVSPTTNSTAPFGLKPRSVFLRPQRNLESIDPQFTIRRKMEQMREEKELVEQLRESIEMRLKVSLHEDLGAALMDGVVLCHLVNHIRPRSVASIHVPSPAVPKLSMAKCRRNVENFLEACRKLGVPEADLCSPCDILQLDFRHIRKTVDTLLALGEKAPPPTSALRSRDLIGFCLVHILFIVLVYITYHWNALSA
Protein: Aldo-keto reductase family 1, member B10 (D3Z494)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MAAFVTLLTGAKMPIVGLGTWKNESEVGEAIQEKIQEKAVKREDLFIVSKLWSTFFEKSLVKKAFQNTLSDLKLDYLDLYLIHWPQGFQSGNVFLPTDDKGSILSSKYTFLDAWEAMEELVDQGLVKALGVSNFNHFQIERLLNKPGLKHKPVTNQVECHPYLTQEKLIQYCHSKGITITAYSPLGSPDRPSAKPEDPLLLEIPKIKEIAAKHKRTAAQVLIRFHIERNVVVIPKSVTPSRIQENIQVFDFQLSEEDMAAILSFNRNWRACGLFAASHNEDFPFHAEY
Protein: Arabinogalactan peptide 1 (OsAGPEP1) (A9UGV5)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Proteoglycan that seems to be implicated in diverse developmental roles such as differentiation, cell-cell recognition, embryogenesis and programmed cell death.
Subcellular location: Vacuole, aleurone grain membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
Interaction partners:
Sequence:
MAGQLKSKIVAVAVAAVVVVASSLVGTASAADAPAPAPTSGATATAAAAPAFAAVSVAAAALGGYLFC
Protein: Potassium channel toxin kappa-KTx 2.9 (Potassium channel-blocking toxin 6) (Pi6) (C0HKB3)
Organism: Pandinus imperator (Emperor scorpion)
Function: Reversibly blocks voltage-gated potassium channels Kv1.2/KCNA2 and Kv1.3/KCNA3.
Subcellular location: Secreted {ECO:0000269|PubMed:28502745}.
Interaction partners:
Sequence:
VDACYEACMHHHMNSDDCIEACKNPVPP
Protein: D-galactonate dehydratase family member RspA (EC 4.2.1.-) (D-mannonate dehydratase) (EC 4.2.1.8) (Starvation sensing protein RspA homolog) (B3PDB1)
Organism: Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa)
Function: Has low D-mannonate dehydratase activity (in vitro), suggesting that this is not a physiological substrate and that it has no significant role in D-mannonate degradation in vivo. Has no detectable activity with a panel of 70 other acid sugars (in vitro).
Interaction partners:
- D-mannonate oxidoreductase
- Dehydratase
- Hydrolase, UxaA family
- Mannonate dehydratase
- 2-dehydro-3-deoxygluconokinase
- 6-phosphogluconate dehydrogenase, decarboxylating
- Ribose-5-phosphate isomerase A
- Ribulose-phosphate 3-epimerase
Sequence:
MKIVDAKVIVTCPGRNFVTLKIVTDQGIYGIGDATLNGREKSVVSYLEDYLIPVLIGRDPQQIEDIWQFFYRGAYWRRGPVGMTALAAIDVALWDIKAKLANMPLYQLLGGKSRERILSYTHANGKDLDSTLEAVRKAKDKGYKAIRVQCGIPGIAKTYGVSTNTKSYEPADADLPSVEVWSTEKYLNYIPDVFAAVRKEFGPDIHLLHDVHHRLTPIEAARLGKALEPYHLFWMEDAVPAENQESFKLIRQHTTTPLAVGEVFNSIHDCRELIQNQWIDYIRTTIVHAGGISQMRRIADFASLFHVRTGFHGATDLSPVCMGAALHFDYWVPNFGIQEHMAHSEQMNAVFPHAYTFNDGYFTPGEKPGHGVDIDEKLAAQYPYKRACLPVNRLEDGTLWHW
Protein: Agamous-like MADS-box protein AGL66 (Q1PFC2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor that forms a heterodimer with the MADS-box protein AGL30 and is involved in the regulation of pollen maturation at the late stages of pollen development and pollen tube growth.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251}.
Interaction partners:
- Agamous-like MADS-box protein AGL82
- AGAMOUS-like 50
- Probable WRKY transcription factor 34
- At1g01310 superfamily protein)
- CAP superfamily protein
- CAP superfamily protein
- Agamous-like MADS-box protein AGL65
Sequence:
MGRVKLEIKRIENTTNRQVTFSKRRNGLIKKAYELSILCDIDIALLMFSPSDRLSLFSGKTRIEDVFSRYINLSDQERENALVFPDQSRRPDFQSKEYLLRTLQQLKAENDIALQLTNPTAINSDVEELEHEVYKLQQQLLMAEEELRKYEPDPIRFTTMEEYETCEKQLMDTLTRVNQRREHILSQDQLSSYEASALQQQQSMGGPFGNDVVGGWLTENGPNEAHLFDASAHSAMYETLLQGSSSSSNQNNIMGESNVSNHNGDMFQEWAQAYNSTTAHNPSTLFPPMQHQHGLVVDPNIEEIEIPVMKKDAQADHEVSDYDIRMPQLSSQ
Protein: Basic helix-loop-helix protein SPATULA-like (Q5VRS4)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDEQRGRGGFDELVLLHQQQEQRRRREQQQEEEEEEEVRRQMFGAVVGGLAAFPAAAAALGQQQVDCGGELGGFCDSEAGGSSEPEAAAGARPRGGSGSKRSRAAEVHNLSEKRRRSKINEKMKALQSLIPNSNKTDKASMLDEAIEYLKQLQLQVQMLSMRNGVYLNPSYLSGALEPAQASQMFAALGGNNVTVVHPGTVMPPVNQSSGAHHLFDPLNSPPQNQPQSLILPSVPSTAIPEPPFHLESSQSHLRQFQLPGSSEFHKILFLHVLLSVKDGVSWRDNAKAPPIITSRKSARKRDELHQERIIHVEHQ
Protein: HTH-type transcriptional regulator SutR (Sulfur utilization regulator) (P77626)
Organism: Escherichia coli (strain K12)
Function: Regulates the expression of 12-16 transcription units involved in various steps of sulfur utilization. Represses expression of pfkB, fliZ, cysE, ydcO and its own expression. Activates expression of ypfN. Acts by binding to SutR boxes.
Interaction partners:
- 23S rRNA 5-hydroxycytidine C2501 synthase
- Inner membrane protein YdcO
Sequence:
MENLARFLSTTLKQLRQQRGWSLSRLAEATGVSKAMLGQIERNESSPTVATLWKIATGLNVPFSTFISPPQSATPSVYDPQQQAMVITSLFPYDPQLCFEHFSIQMASGAISESTPHEKGVIEHVVVIDGQLDLCVDGEWQTLNCGEGVRFAADVTHIYRNGGEQTVHFHSLIHYPRS
Protein: Intraflagellar transport protein 56 (Tetratricopeptide repeat protein 26) (TPR repeat protein 26) (Q5PR66)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Component of the intraflagellar transport (IFT) complex B required for transport of proteins in the motile cilium. Required for transport of specific ciliary cargo proteins related to motility, while it is neither required for IFT complex B assembly or motion nor for cilium assembly. Plays a key role in maintaining the integrity of the IFT complex B and the proper ciliary localization of the IFT complex B components. Essential for maintaining proper microtubule organization within the ciliary axoneme (By similarity).
Subcellular location: Cell projection, cilium {ECO:0000250|UniProtKB:Q8BS45}.
Interaction partners:
- Intraflagellar transport protein 46 homolog
- Intraflagellar transport protein 70A
- Intraflagellar transport 88 homolog.
- Intraflagellar transport 52 homolog
- Intraflagellar transport protein 57 homolog
- Intraflagellar transport 81 homolog.
- Intraflagellar transport 80 homolog
- Intraflagellar transport protein 172 homolog
- Clusterin-associated protein 1 homolog
- Intraflagellar transport protein 22 homolog
Sequence:
MLLSRMKPAVGGEASTSSNEKKRKNKSKKIPRLEDYLNQRDYLGALTLLEFQRNSGVSVEHADLWTGFCAFHVGDHKRAMEEYKALTLRPDCPVDVWVYLGCALFFLGLYKEAEEAALKGSKTQLQNRLLFHLAHKFNDEKKLMGFHQNLEDVTEDQLSLASIHYMRSHYQEAIDIYKRILLQNREFLALNVYVALCYYKLDYYDVSQEVLAVYLQSIPDSTIALNLKACNHFRLYNGKAAETELKNLIDISSSSFQFAKELIQHNLVVFRGGEGALQVLPPLIDVISEARLNLVIYYLRQDDIQEAYKLIKDLEPTTPQEYILKGVVNAALGQEIGSRDHLKIAQQFFQLVGGSASECDTIPGRQCMASCFFLLKQFEDVLIYLNSVKSYFYNDDTFSFNYAQAKAALGNYREAEELFLLIQNEKIKSDYVFQSWLARCYIMNQKPRQAWELYLRMETSSDPFSLLQLIANDCYKMGQFYYAAKAFDALERLDPNPEYWEGKRGACVGIFQLILAGRESREILKEVLPMLRSTGNPQVEYIIRIMKKWAKDNRVAL
Protein: Polynucleotide 5'-hydroxyl-kinase NOL9 (EC 2.7.1.78) (Nucleolar protein 9) (Q5SY16)
Organism: Homo sapiens (Human)
Function: Polynucleotide 5'-kinase involved in rRNA processing. The kinase activity is required for the processing of the 32S precursor into 5.8S and 28S rRNAs, more specifically for the generation of the major 5.8S(S) form. In vitro, has both DNA and RNA 5'-kinase activities. Probably binds RNA.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q3TZX8}. Nucleus, nucleolus {ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:21063389, ECO:0000269|PubMed:31288032}. Note=Colocalizes with pre-60S rRNP particles.
Interaction partners:
- Ribosomal biogenesis protein LAS1L
- WD repeat-containing protein 18
- Testis-expressed protein 10
- Proline-, glutamic acid- and leucine-rich protein 1
- Sentrin-specific protease 3
- CREB/ATF bZIP transcription factor
- WD repeat-containing protein 36
- HEAT repeat-containing protein 1
- Nuclear cap-binding protein subunit 1
- Protein RRP5 homolog
Sequence:
MADSGLLLKRGSCRSTWLRVRKARPQLILSRRPRRRLGSLRWCGRRRLRWRLLQAQASGVDWREGARQVSRAAAARRPNTATPSPIPSPTPASEPESEPELESASSCHRPLLIPPVRPVGPGRALLLLPVEQGFTFSGICRVTCLYGQVQVFGFTISQGQPAQDIFSVYTHSCLSIHALHYSQPEKSKKELKREARNLLKSHLNLDDRRWSMQNFSPQCSIVLLEHLKTATVNFITSYPGSSYIFVQESPTPQIKPEYLALRSVGIRREKKRKGLQLTESTLSALEELVNVSCEEVDGCPVILVCGSQDVGKSTFNRYLINHLLNSLPCVDYLECDLGQTEFTPPGCISLLNITEPVLGPPFTHLRTPQKMVYYGKPSCKNNYENYIDIVKYVFSAYKRESPLIVNTMGWVSDQGLLLLIDLIRLLSPSHVVQFRSDHSKYMPDLTPQYVDDMDGLYTKSKTKMRNRRFRLAAFADALEFADEEKESPVEFTGHKLIGVYTDFAFRITPRNRESHNKILRDLSILSYLSQLQPPMPKPLSPLHSLTPYQVPFNAVALRITHSDVAPTHILYAVNASWVGLCKIQDDVRGYTNGPILLAQTPICDCLGFGICRGIDMEKRLYHILTPVPPEELRTVNCLLVGAIAIPHCVLKCQRGIEGTVPYVTTDYNFKLPGASEKIGAREPEEAHKEKPYRRPKFCRKMK
Protein: PGR5-like protein 1A, chloroplastic (Ferredoxin-plastoquinone reductase 1) (Q8H112)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Ferredoxin-plastoquinone reductase involved in cyclic electron flow (CEF) around photosystem I. The homodimer is probably not involved in CEF.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:18243102}; Multi-pass membrane protein {ECO:0000269|PubMed:18243102}. Note=Predominantly located in the appressed regions of the thylakoids and less abundant in the stroma lamellae.
Interaction partners:
- Protein PROTON GRADIENT REGULATION 5
- Serine/threonine-protein kinase STN7, chloroplastic
- Ferredoxin/thioredoxin reductase subunit A
- Photosystem I reaction center subunit IV A, chloroplastic
- NAD
- Chlorophyll a-b binding protein 3, chloroplastic
- Protein CURVATURE THYLAKOID 1A
- Photosystem I reaction center subunit IV B, chloroplastic
- Photosystem II 22 kDa protein, chloroplastic
- NAD
Sequence:
MGSKMLFSLTSPRLFSAVSRKPSSSFSPSPPSPSSRTQWTQLSPGKSISLRRRVFLLPAKATTEQSGPVGGDNVDSNVLPYCSINKAEKKTIGEMEQEFLQALQSFYYDGKAIMSNEEFDNLKEELMWEGSSVVMLSSDEQRFLEASMAYVSGNPILNDEEYDKLKLKLKIDGSDIVSEGPRCSLRSKKVYSDLAVDYFKMLLLNVPATVVALGLFFFLDDITGFEITYIMELPEPYSFIFTWFAAVPVIVYLALSITKLIIKDFLILKGPCPNCGTENTSFFGTILSISSGGKTNTVKCTNCGTAMVYDSGSRLITLPEGSQA
Protein: Nicastrin (A5Z2T7)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MKKWLVIVLIIAGIRCDGFSDQVFRTLFIGEGNACYRTFNKTHEFGCQANRENENGLIVRIDKQEDFKNLDSCWNSFYPKYSGKYWALLPVNLIRRDTISQLKSSKCLSGIVLYNSGESIHPGDESTAASHDAECPNAASDYYLQDKNEEYCERKINSRGAITRDGLMKIDWRIQMVFIDNSTDLEIIEKCYSMFNKPKEDGSSGYPYCGMSFRLANMAAGNSEICYRRGKNDAKLFQMNIDSGDAPQLCGAMHSDNIFAFPTPIPTSPTNETIITSKYMMVTARMDSFGMIPEISVGEVSVLTSIISVLAAARSMGTQIEKWQKASNTSNRNVFFAFFNGESLDYIGSGAAAYQMENGKFPQMIRSDRTHIHPIRPNELDYILEVQQIGVAKGRKYYVHVDGERYQQNKTQTDRVIDRIERGLRSHAFDLEKPSGSGDRVPPASWHSFAKADAHVQSVLLAPYGKEYEYQRVNSILDKNEWTEDEREKAIQEIEAVSTAILAAAADYVGVETDEVVAKVDKKLITTIFDCLITSNFWFDCDFMQKLDGGRYHKLFNSYGFNQKSTYISMESHTAFPTVLHWLTIFALGSDKETLNVKSEKSCSHLGQFQAMYTYTWQPNPYTGNFSCLKSAIVKKVMVSPAVDSQTPEEEMNTRYSTWMESVYIIESVNLYLMEDASFEYTMILIAVISALLSIFAVGRCSETTFIVDEGEPAAEGGEPL
Protein: Alkyl hydroperoxide reductase C (EC 1.11.1.26) (Alkyl hydroperoxide reductase protein C22) (Peroxiredoxin) (SCRP-23) (Sulfate starvation-induced protein 8) (SSI8) (Thioredoxin peroxidase) (P0AE08)
Organism: Escherichia coli (strain K12)
Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. Is the primary scavenger for endogenously generated hydrogen peroxides.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:7499381}.
Interaction partners:
- Alkyl hydroperoxide reductase subunit F
- Thioredoxin reductase
- Catalase HPII
- Thiol:disulfide interchange protein DsbE
- Superoxide dismutase
- Superoxide dismutase
- Catalase-peroxidase
- DNA-binding transcriptional dual regulator OxyR
- Peroxiredoxin Bcp
- Superoxide dismutase
Sequence:
MSLINTKIKPFKNQAFKNGEFIEITEKDTEGRWSVFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYAVSTDTHFTHKAWHSSSETIAKIKYAMIGDPTGALTRNFDNMREDEGLADRATFVVDPQGIIQAIEVTAEGIGRDASDLLRKIKAAQYVASHPGEVCPAKWKEGEATLAPSLDLVGKI
Protein: GH17513p (Q8MT02)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGAI
Protein: LisH domain-containing protein (O01796)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MHSTNPILRQLADQLSELPQYAPLRTYIRATISATLGETPKKTSRDLTYRERVTHSMIADWLEQNGYPISSQVLKTEMSGNYMESAEKHVENGEKIDNLLRSQLKIDIRDGTGDDFERKSIKSIGAGRPFAKINMVDKQRAPLKITPLSDEEFRKTMRKRMEMERERLARLSNQAEDDSDDSSSSSDSSTSSASSSSEEKLTFSDILGKPTAAGAEKMIELSQIPNAWGPSKSALVTDDVASTSDPLPAIFNAHLPPLSMGRPPLTKSAKSREIDAIFGSDNVDYDLEDFEQDGVAKKKSILPMEKKKEEAKPKEQELVEPLVLSEGESIDELEDFDTGLLSSGGSDYSF
Protein: DNA replication complex GINS protein PSF3 (A0A0S2Z5L0)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU367161}.
Interaction partners:
Sequence:
MSEAYFRVESGALGPEENFLSLDDILMSHEKLPVRTETAMPRLGAFFLERSAGAETDNAVPQGSKLELPLWLAKGLFDNKRRILSVELPKIYQEGWRTVFSADPNVVDLHKMGPHFYGFGSQLLHFDSPENADISQSLLQTFIGRFRRIMDSSQNAYNEDTSALVARLDEMERGLFQTGQKGLNDFQCWEKGQASQITASNLVQNYKKRKFTDMED
Protein: Histone deacetylase 2 (Q99PA1)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
YETAVALDCEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTPEYMEKIKQRLFENLRMLPHAPGVQMQAIPEDAVHEDSGDEDGEDPDKRISIRASDKRIACDEEFSDSEDEGEGGRRNVADHKKGAKKARIEEDKKEAEDKKTDVKEEDKSKDNSGEKTDTKGAKSEQLNNP
Protein: Probable secreted beta-glucosidase SUN4 (EC 3.2.1.-) (Septation protein SUN4) (Soluble cell wall protein 3) (P53616)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the remodeling of the cell wall during the various phases of yeast culture development and under various environmental conditions and plays a role in septation.
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:24040106, ECO:0000269|PubMed:9748433}.
Interaction partners:
- Protein DSE2
- Protein EGT2
- Endochitinase
- Probable family 17 glucosidase SCW11
- Glucan endo-1,3-beta-D-glucosidase 1
- Antagonist of mitotic exit network protein 1
- Probable family 17 glucosidase SCW4
- Protein DSE1
- Probable family 17 glucosidase SCW10
- Probable circularly permuted 1,3-beta-glucanase TOS1
Sequence:
MKLSATTLTAASLIGYSTIVSALPYAADIDTGCTTTAHGSHQHKRAVAVTYVYETVTVDKNGQTVTPTSTEASSTVASTTTLISESSVTKSSSKVASSSESTEQIATTSSSAQTTLTSSETSTSESSVPISTSGSASTSSAASSATGSIYGDLADFSGPYEKFEDGTIPCGQFPSGQGVIPISWLDEGGWSGVENTDTSTGGSCKEGSYCSYACQPGMSKTQWPSDQPSDGRSIGGLLCKDGYLYRSNTDTDYLCEWGVDAAYVVSELSNDVAICRTDYPGTENMVIPTYVQAGDSLPLTVVDQDTYYTWQGLKTSAQYYVNNAGISVEDACVWGSSSSGVGNWAPLNFGAGSSDGVAYLSLIPNPNNGNALNFNVKIVAADDSSTVNGECIYENGSFSGGSDGCTVSVTAGKAKFVLYN
Protein: Signal peptidase complex subunit 2 (Microsomal signal peptidase 25 kDa subunit) (SPase 25 kDa subunit) (Q28250)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: 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. Enhances the enzymatic activity of SPC and facilitates the interactions between different components of the translocation site (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:3511473, ECO:0000269|PubMed:8632014}; Multi-pass membrane protein {ECO:0000269|PubMed:8632014}.
Interaction partners:
- Signal peptidase complex subunit 3
- Signal peptidase complex catalytic subunit SEC11C
- Signal peptidase complex catalytic subunit SEC11A
- Signal peptidase complex subunit 1.
- Actin-related protein 2/3 complex subunit 5
- SRP receptor subunit beta.
- Gastrin-releasing peptide
- Uncharacterized protein.
Sequence:
MAAASAQGGRTGGGGGSSGPGGGPTCGSGSGRSGLLDKWKIDDKPVKIDKWDGSAVKNSLDDSAKKVLLEKYKYVENFGLIDGRLTICTISCFFAIVALIWDYMHPFPESKPVLALCVISYFVMMGILTIYTSYKEKSIFLVAHRKDPTGMDPDDIWQLSSSLKRFDDKYTLKLTFISGRTKQQREAEFTKSIAKFFDHSGTLVMDAYEPEISRLHDSLATERKIK
Protein: Versicolorin reductase stcU (EC 1.3.1.-) (Sterigmatocystin biosynthesis cluster protein U) (Q00791)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Versicolorin reductase; part of the gene cluster that mediates the biosynthesis of sterigmatocystin (ST), a polyketide-derived furanocoumarin which is part of the most toxic and carcinogenic compounds among the known mycotoxins. The first step in the biosynthesis of sterigmatocystin is the production of hexanoate by the fatty acid synthase (FAS) units stcJ and stcK. The polyketide backbone is assembled by the non-reducing polyketide synthase stcA by condensation of the starter hexanoyl-CoA and 7 malonyl-CoA extender units followed by cyclization and release of norsolorinic acid (By similarity). Norsolorinic acid is the first stable intermediate in the biosynthesis of sterigmatocystin and is converted into averantin (AVN) by the ketoreductase stcE which reduces the hexanoate ketone to an alcohol (Probable). Averantin is then oxidized into 5'-hydroxyaverantin (HAVN) by the cytochrome P450 monooxygenase stcF. 5'-hydroxyaverantin is further converted to 5'-oxyaverantin (OAVN) by the 5'-hydroxyaverantin dehydrogenase stcG. The next step is the conversion of OAVN into averufin (AVF) which is catalyzed by a yet to be identified enzyme. The cytochrome P450 monoxygenase stcB and the flavin-binding monooxygenase stcW are both required for the conversion of averufin to 1-hydroxyversicolorone. The esterase stcI probably catalyzes the formation of versiconal hemiacetal acetate from 1-hydroxyversicolorone. The oxydoreductase stcN then probably catalyzes the biosynthetic step from versiconal to versicolorin B (VERB). The next step is performed by the versicolorin B desaturase stcL to produce versicolorin A (VERA). The ketoreductase stcU and the cytochrome P450 monooxygenase stcS are involved in the conversion of versicolorin A to demethylsterigmatocystin. The Baeyer-Villiger oxidas stcQ and the reductase stcR might be involved in the biosynthetic step from versicolorin A to demethylsterigmatocystin. The final step in the biosynthesis of sterigmatocystin is the methylation of demethylsterigmatocystin catalyzed by the methyltransferase stcP.
Interaction partners:
- Versicolorin B desaturase stcL
- Sterigmatocystin biosynthesis regulatory protein
- Norsolorinic acid synthase stcA
- Norsolorinic acid ketoreductase stcE
Sequence:
MSSSDNYRLDGKVALVTGAGRGIGAAIAVALGQRGAKVVVNYANSREAAEKVVDEIKSNGSDAISIQADVGDPDAVTKLMDQAVEHFGYLDIVSSNAGIVSFGHVKDVTPDEFDRVFRVNTRGQFFVAREAYRHLREGGRIILTSSNTASVKGVPRHAVYSGSKGAIDTFVRCLAIDCGDKKITVNAVAPGAIKTDMFLSVSREYIPNGETFTDEQVDECAAWLSPLNRVGLPVDVARVVSFLASDAAEWISGKIIGVDGGAFR
Protein: Polycomb complex protein BMI-1 (Polycomb group RING finger protein 4) (P25916)
Organism: Mus musculus (Mouse)
Function: Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. The complex composed of RNF2, UB2D3 and BMI1 binds nucleosomes, and has activity only with nucleosomal histone H2A. In the PRC1-like complex, regulates the E3 ubiquitin-protein ligase activity of RNF2/RING2 (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P35226}. Cytoplasm {ECO:0000250|UniProtKB:P35226}.
Interaction partners:
- E3 ubiquitin-protein ligase RING2
- E3 ubiquitin-protein ligase RING1
- Chromobox protein homolog 2
- Chromobox protein homolog 7
- Chromobox protein homolog 8
- Polycomb group RING finger protein 2
- Polyhomeotic-like protein 1
- E3 SUMO-protein ligase CBX4
- Histone-lysine N-methyltransferase EZH2
- Polycomb protein Suz12
Sequence:
MHRTTRIKITELNPHLMCVLCGGYFIDATTIIECLHSFCKTCIVRYLETSKYCPICDVQVHKTRPLLNIRSDKTLQDIVYKLVPGLFKNEMKRRRDFYAAHPSADAANGSNEDRGEVADEEKRIITDDEIISLSIEFFDQSRLDRKVNKEKPKEEVNDKRYLRCPAAMTVMHLRKFLRSKMDIPNTFQIDVMYEEEPLKDYYTLMDIAYIYTWRRNGPLPLKYRVRPTCKRMKMSHQRDGLTNAGELESDSGSDKANSPAGGVPSTSSCLPSPSTPVQSPHPQFPHISSTMNGTSNSPSANHQSSFASRPRKSSLNGSSATSSG
Protein: Oxidoreductase-like domain-containing protein 1 (Q9CR10)
Organism: Mus musculus (Mouse)
Interaction partners:
- Gene model 561
Sequence:
MGSPLQTLSRGGRVRAALWCWTQARGLSGRQCPNRVARSLSCSRGFPVRGGRPALGGTMVSVLTESFLQGTQHFSSWDCCQSLHRHRAPVQVTDSRRNLGMDHREEGFQVGTEDDREPKASLPRGNPTGPPCSLPPELEPPTNCCMSGCPNCVWVDYAEALLRLYQDGGEKALAILEEHVTDENLKAFLRMEIRLRMQSGA
Protein: RB transcriptional corepressor 1 (A0A0D9RYS3)
Organism: Chlorocebus sabaeus (Green monkey) (Simia sabaea)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Cyclin-dependent kinase 4
- E2F transcription factor 1
- Cyclin-dependent kinase 2
- E2F transcription factor 2
- Cyclin D1
- Transcription factor
- E2F transcription factor CC-MB domain-containing protein
- Cyclin-A2
- cyclin-dependent kinase
- E2F transcription factor 4
Sequence:
MPPKTPRKTAAAAAAAAAEPPAPPPPPPPEEDPEQDSGPEDLPLVRLEFEETEEPDFTALCQKLKIPDHVRERAWLTWEKVSSVDGVLGGYIQKKKELWGICIFIAAVDLDEMPFTFTELQKNIEISVHKFFNLLKEIDTSTKVDNAMSRLLKKYDVLFALFSKLERTCELIYLTQPSSSISTEINSALVLKVSWITFLLAKGEVLQMEDDLVISFQLMLCVLDYFIKLSPPVLLKEPYKTAVIPINGSPRTPRRGQNRSARIAKQLENDTRIIEVLCKEHECNIDEVKNVYFKNFIPFMNSLGLVTSNGLPEVESLSKRYEEIYLKNKDLDARLFLDHDKTLQTDSIDSFETQRTPRKSNLDEEVNVIPPHTPVRTVMNTIQQLMMILNSASDQPSENLISYFNNCTVNPKESILKRVKDIGYIFKEKFAKAVGQGCVEIGSQRYKLGVRLYYRVMESMLKSEEERLSIQNFSKLLNDNIFHMSLLACALEVVMATYSRSTSQNLDSGTDLSFPWILNVLNLKAFDFYKVIESFIKAEGNLTREMIKHLERCEHRIMESLAWLSDSPLFDLIKQSKDREGPTDHFESACPLNIPLQNNHTAADMYLSPVRSPKKKGSTTRVNSTANAETQATSAFQTQKPLKSTSLSLFYKKVYRLAYLRLNTLCERLLSEHPELEHIIWTLFQHTLQNEYELMRDRHLDQIMMCSMYGICKVKNIDLKFKIIVTAYKDLPHAVQETFKRVLIKEEEYDSIIVFYNSVFMQRLKTNILQYASTRPPTLSPIPHIPRSPYKFPSSPLRIPGGNIYISPLKSPYKISEGLPTPTKMTPRSRILVSIGESFGTSEKFQKINQMVCNSDRVLKRSAEGSNPPKPLKKLRFDIEGSDEADGSKRLPGESKFQQKLAEMTSTRTRMQKQKMNDSMDTSNKEEK
Protein: C-C motif chemokine 12 (MCP-1-related chemokine) (Monocyte chemoattractant protein 5) (Monocyte chemotactic protein 5) (MCP-5) (Small-inducible cytokine A12) (Q62401)
Organism: Mus musculus (Mouse)
Function: Chemotactic factor that attracts eosinophils, monocytes, and lymphocytes but not neutrophils. Potent monocyte active chemokine that signals through CCR2. Involved in allergic inflammation and the host response to pathogens and may play a pivotal role during early stages of allergic lung inflammation.
Subcellular location: Secreted.
Interaction partners:
- C-C chemokine receptor type 2
- C-C motif chemokine 2
- C-C motif chemokine 6
- C-C motif chemokine 27
- C-C chemokine receptor type 5
- C-C chemokine receptor type 1
- C-C motif chemokine 7
- C-X-C motif chemokine 10
- C-C motif chemokine 8
- C-C chemokine receptor type 8
Sequence:
MKISTLLCLLLIATTISPQVLAGPDAVSTPVTCCYNVVKQKIHVRKLKSYRRITSSQCPREAVIFRTILDKEICADPKEKWVKNSINHLDKTSQTFILEPSCLG