wanglab/gogpt-training-data huggingface dataset:
Protein: 6-methylsalicylic acid decarboxylase (EC 4.1.1.52) (Patulin synthesis protein G) (A1CFL4)
Organism: Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107)
Function: 6-methylsalicylic acid decarboxylase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria. PatG catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol. The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) patK via condensation of acetate and malonate units. The 6-methylsalicylic acid decarboxylase patG then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol). These first reactions occur in the cytosol. The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase patH converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase patI. The oxidoreductases patJ and patO further convert gentisyl alcohol to isoepoxydon in the vacuole. PatN catalyzes then the transformation of isoepoxydon into phyllostine. The cluster protein patF is responsible for the conversion from phyllostine to neopatulin whereas the alcohol dehydrogenase patD converts neopatulin to E-ascladiol. The steps between isoepoxydon and E-ascladiol occur in the cytosol, and E-ascladiol is probably secreted to the extracellular space by one of the cluster-specific transporters patC or patM. Finally, the secreted patulin synthase patE catalyzes the conversion of E-ascladiol to patulin (Probable).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:A0A075TXZ1}.
Interaction partners:
Sequence:
MAKIDVHHHFYPQAMREALERAGGDPSGWYIPPWTLDLDKEISRVLKVQTTILSVTAPGPGIETDPGKAAALARLCNEEAAAIRDAHPLQYGFFASVPSLFDTAAVLAEIEHAFTNLHADGVTLYTRYGAGHSYLGDERFRPIWAELSKRRAVVFIHPTHAVDTQLINSWMPQPMFDYPHETGRTAMDLLTRGVIRDYPGCKIILSHAGGTLPYLIHRAATMLPFMPRNLGMSREEIVEAARTFYFDTAISANPVTLKALLEFAKPGHVLFGSDFPNAPRGAITHFTSFLEGYDNMSEETRRLVEREAALELFPRLRGQSTRACL
Protein: Diguanylate cyclase DgcP (EC 2.7.7.65) (Q9HT84)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules. Cyclic-di-GMP is a second messenger which controls cell surface-associated traits in bacteria. Localizes at the cell poles through interaction with FimV where it increases the local pools of c-di-GMP (By similarity).
Subcellular location: Cell inner membrane {ECO:0000250|UniProtKB:A0A0H2ZJS2}. Note=Localizes at the cell poles in a FimV-dependent manner. {ECO:0000250|UniProtKB:A0A0H2ZJS2}.
Interaction partners:
- Endonuclease/exonuclease/phosphatase domain-containing protein
- tRNA N6-adenosine threonylcarbamoyltransferase
- Cyclic di-GMP phosphodiesterase RocR
- Cyclic di-GMP phosphodiesterase PA2567
- EAL domain-containing protein
- cyclic-guanylate-specific phosphodiesterase
- cyclic-guanylate-specific phosphodiesterase
- cyclic-guanylate-specific phosphodiesterase
- Ribosomal RNA small subunit methyltransferase B
- Thiol:disulfide interchange protein DsbA
Sequence:
MSRDDVQRWKDKYLENIEQQERLQRRWDARIDLLRRGLVRSSLAAEGSDKAVDQCMKELREILRRDDMDAGLSGLIPRLEKAVLDSEQRRQQRTQQNIDALGELAQQLLALDLPRELRKPLKQFARDIEERARQSREIPILLSELSRLQRQALAERKGGDAEDGRPSLLQRLFGGKESETTAEPSASVPSVVAASNTPIQPAAAAPSLPVAEHDEAPGGPPQPLPARTVAAIESAPAGWVGVAERGEPNQILLDEPREIWLDSLPLPAGLSFSETLEEAGAEPSPAMPADVESAPEAPATPVDNLDGQAVDEAYELPPPIPEPGYSAVAPHIEASLLRLLDGLSLPSSHQPQAEALRERIDGSLNWYELVPVLDDLAVLVLSLADSGQRDFEEYLRQLNERLESFLGHLGDAHAGYTDVLDNARGFDQSLREQVSGLQASVQQATDLNSLKLAVDSRLNGLLASMDEHQREQAEHEQEVSGRLQALMERVNSMEQDAKAFHSHLEDQRQKALTDPLTGLPNRAALSERLEQEVARRHRDGGDLLLAVLDIDHFKRINDDFGHLAGDKVLKIIAGELRKRLRQADFIARFGGEEFVVLLPATSLEAGRQLLERLRAAIAACPFHFKGEPLSITCSAGITAFEGNEAGEAVFERADQALYRAKRAGRDRLEVA
Protein: Dual oxidase maturation factor 1 (Dual oxidase activator 1) (Numb-interacting protein) (Q1HG43)
Organism: Homo sapiens (Human)
Function: May be required for the maturation and the transport from the endoplasmic reticulum to the plasma membrane of functional DUOX1.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Dual oxidase 1
- Dual oxidase 2
- NADPH oxidase activator 1
- NADPH oxidase 5
Sequence:
MATLGHTFPFYAGPKPTFPMDTTLASIIMIFLTALATFIVILPGIRGKTRLFWLLRVVTSLFIGAAILAVNFSSEWSVGQVSTNTSYKAFSSEWISADIGLQVGLGGVNITLTGTPVQQLNETINYNEEFTWRLGENYAEEYAKALEKGLPDPVLYLAEKFTPRSPCGLYRQYRLAGHYTSAMLWVAFLCWLLANVMLSMPVLVYGGYMLLATGIFQLLALLFFSMATSLTSPCPLHLGASVLHTHHGPAFWITLTTGLLCVLLGLAMAVAHRMQPHRLKAFFNQSVDEDPMLEWSPEEGGLLSPRYRSMADSPKSQDIPLSEASSTKAYCKEAHPKDPDCAL
Protein: Peripherin-2 (Retinal degeneration slow protein) (P15499)
Organism: Mus musculus (Mouse)
Function: Essential for retina photoreceptor outer segment disk morphogenesis, may also play a role with ROM1 in the maintenance of outer segment disk structure. Required for the maintenance of retinal outer nuclear layer thickness. Required for the correct development and organization of the photoreceptor inner segment.
Subcellular location: Membrane {ECO:0000250|UniProtKB:P17810}; Multi-pass membrane protein {ECO:0000255}. Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:10802659, ECO:0000269|PubMed:17260955, ECO:0000269|PubMed:26406599, ECO:0000269|PubMed:29961824}. Photoreceptor inner segment {ECO:0000269|PubMed:17260955, ECO:0000269|PubMed:26406599}.
Interaction partners:
- Rod outer segment membrane protein 1
- Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit beta
- Protein RD3
- Rhodopsin
- Amelogenin, X isoform
- Somatotropin
- Neuropeptide Y receptor type 2
- Somatoliberin
- BPI fold-containing family A member 2
- Retinal-specific phospholipid-transporting ATPase ABCA4
Sequence:
MALLKVKFDQKKRVKLAQGLWLMNWLSVLAGIVLFSLGLFLKIELRKRSEVMNNSESHFVPNSLIGVGVLSCVFNSLAGKICYDALDPAKYAKWKPWLKPYLAVCIFFNVILFLVALCCFLLRGSLESTLAYGLKNGMKYYRDTDTPGRCFMKKTIDMLQIEFKCCGNNGFRDWFEIQWISNRYLDFSSKEVKDRIKSNVDGRYLVDGVPFSCCNPSSPRPCIQYQLTNNSAHYSYDHQTEELNLWLRGCRAALLNYYSSLMNSMGVVTLLVWLFEVSITAGLRYLHTALESVSNPEDPECESEGWLLEKSVPETWKAFLESFKKLGKSNQVEAEGADAGPAPEAG
Protein: Mitochondrial hydrolase YKR070W (EC 3.-.-.-) (P36151)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823961}.
Interaction partners:
- Aspartate--tRNA ligase, cytoplasmic
- Altered inheritance of mitochondria protein 19
- ATPase synthesis protein 25, mitochondrial
- Nuclear control of ATPase protein 2
- Ribosome assembly protein RSM22
Sequence:
MIGKRFFQTTSKKIAFAFDIDGVLFRGKKPIAGASDALKLLNRNKIPYILLTNGGGFSERARTEFISSKLDVDVSPLQIIQSHTPYKSLVNKYSRILAVGTPSVRGVAEGYGFQDVVHQTDIVRYNRDIAPFSGLSDEQVMEYSRDIPDLTTKKFDAVLVFNDPHDWAADIQIISDAINSENGMLNTLRNEKSGKPSIPIYFSNQDLLWANPYKLNRFGQGAFRLLVRRLYLELNGEPLQDYTLGKPTKLTYDFAHHVLIDWEKRLSGKIGQSVKQKLPLLGTKPSTSPFHAVFMVGDNPASDIIGAQNYGWNSCLVKTGVYNEGDDLKECKPTLIVNDVFDAVTKTLEKYA
Protein: Enterotoxin type H (SEH) (P0A0M0)
Organism: Staphylococcus aureus
Function: Staphylococcal enterotoxin that activates the host immune system by binding as unprocessed molecules to major histocompatibility (MHC) complex class II and T-cell receptor (TCR) molecules via their alpha domain, in particular TRAV27. In turn, this ternary complex activates a large number of T-lymphocytes initiating a systemic release of pro-inflammatory cytokines. Causes also the intoxication staphylococcal food poisoning syndrome. The illness characterized by high fever, hypotension, diarrhea, shock, and in some cases death.
Subcellular location: Secreted.
Interaction partners:
Sequence:
MINKIKILFSFLALLLSFTSYAKAEDLHDKSELTDLALANAYGQYNHPFIKENIKSDEISGEKDLIFRNQGDSGNDLRVKFATADLAQKFKNKNVDIYGASFYYKCEKISENISECLYGGTTLNSEKLAQERVIGANVWVDGIQKETELIRTNKKNVTLQELDIKIRKILSDKYKIYYKDSEISKGLIEFDMKTPRDYSFDIYDLKGENDYEIDKIYEDNKTLKSDDISHIDVNLYTKKKV
Protein: Immunoglobulin heavy constant gamma 3 (HDC) (Heavy chain disease protein) (Ig gamma-3 chain C region) (P01860)
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.
Subcellular location: [Isoform 1]: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
ASTKGPSVFPLAPCSRSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYTCNVNHKPSNTKVDKRVELKTPLGDTTHTCPRCPEPKSCDTPPPCPRCPEPKSCDTPPPCPRCPEPKSCDTPPPCPRCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVQFKWYVDGVEVHNAKTKPREEQYNSTFRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKTKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESSGQPENNYNTTPPMLDSDGSFFLYSKLTVDKSRWQQGNIFSCSVMHEALHNRFTQKSLSLSPELQLEESCAEAQDGELDGLWTTITIFITLFLLSVCYSATVTFFKVKWIFSSVVDLKQTIIPDYRNMIGQGA
Protein: PPE family protein PPE11 (P9WI39)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: May play an important role in the persistence of mycobacteria in host cells. May regulate the innate immune response of macrophages by promoting the production of pro-inflammatory cytokines and inhibiting the production of anti-inflammatory cytokines. Promotes the death of macrophages during infection.
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:30366125}. Note=Cell wall-associated. {ECO:0000269|PubMed:30366125}.
Interaction partners:
- Probable periplasmic iron-transport lipoprotein
Sequence:
MTSALIWMASPPEVHSALLSSGPGPGPVLAAATGWSSLGREYAAVAEELGALLAAVQAGVWQGPSAESFAAACLPYLSWLTQASADCAAAAARLEAVTAAYAAALVAMPTLAELAANHATHGAMVATNFFGINTIPIAVNEADYVRMWLQAATTMATYQAVADSAVRSIPDSVPPPRILKSNAQSQHSSSNNSGGADPVDDFIAEILKIITGGRVIWDPEAGTVNGLPYDAYTNPGTLMWWIARSLELLQDFQEFAKLLFTNPVKAFQFLVDLILFDWPTHMLQLATWLAENPQLLVAALTPAISGLGAVSGLAGLTGLVPQPPVVPAPAPDAVVPTVLPLAGTATPTTAPASAPAAGAAPGPPAGTATATSASVPTSAGGFPPYLVGSGPGIDFDAGTPAGSRRAQPAADNVTAVAAAQVSARHQARRRRRAAAKERGNADEFVDMDSGPAIPPSGERDAWASNSGVGGLGFAGTASNETVAAPAGLTTLADDEFQCGPRMPMLPGAWDLGTWDRGD
Protein: Tektin-2 (Tektin-t) (Testicular tektin) (Testicular tektin B1-like protein) (TEKTB1) (Tektin-B1) (Q9UIF3)
Organism: Homo sapiens (Human)
Function: Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia and flagellar axoneme. Plays a key role in the assembly or attachment of the inner dynein arm to microtubules in sperm flagella and tracheal cilia. Forms filamentous polymers in the walls of ciliary and flagellar microtubules.
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:36191189}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:Q922G7}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000250|UniProtKB:Q922G7}. Note=Colocalized with CCDC172 at the perinuclear region. {ECO:0000250|UniProtKB:Q922G7}.
Interaction partners:
- Homeobox protein goosecoid
- EF-hand domain-containing family member C2
- Tektin-1
- Cilia- and flagella-associated protein 45
- Tektin-3
- EF-hand domain-containing protein 1
- RIB43A-like with coiled-coils protein 2
- Tektin-4
- Cilia- and flagella-associated protein 53
- Parkin coregulated gene protein
Sequence:
MATLSVKPSRRFQLPDWHTNSYLLSTNAQLQRDASHQIRQEARVLRNETNNQTIWDEHDNRTRLVERIDTVNRWKEMLDKCLTDLDAEIDALTQMKESAEQNLQAKNLPLDVAIECLTLRESRRDIDVVKDPVEDELHKEVEVIEATKKALQQKVSQAFEQLCLLQEVQQQLNSDHRGKMETLEIDRGCLSLNLRSPNISLKVDPTRVPDGSTTLQQWDDFSRFNKDRAEAEMKAATELREATALTIAETNNELEAQRVATEFAFRKRLREMEKVYSELKWQEKNTLEEIAELQEDIRHLEEDLRTKLLSLKLSHTRLEARTYRPNVELCRDQAQYGLTDEVHQLEATIAALKQKLAQAQDALDALCKHLARLQADIACKANSMLLDTKCMDTRRKLTVPAERFVPEVDTFTRTTNSTLSPLKSCQLELA
Protein: dUTPase (E7DN78)
Organism: Pneumococcus phage Dp-1 (Bacteriophage Dp-1)
Interaction partners:
Sequence:
MQKDVDVKMIDPKLDRLKYTGDWVDVRISSITKIDADSADVSRCRKVLQKAQVYSVAAGECIKIAHGFALELPKGYEAILHPRSSLFKKTGLIFVSSGVIDEGYKGDTDEWFSVWYATRDADIFYDQRIAQFRIQEKQPAIKFNFVESLGNAARGGHGSTGDF
Protein: Protein transport protein Sec16B (Leucine zipper transcription regulator 2) (Regucalcin gene promoter region-related protein p117) (RGPR-p117) (SEC16 homolog B) (Q96JE7)
Organism: Homo sapiens (Human)
Function: Plays a role in the organization of the endoplasmic reticulum exit sites (ERES), also known as transitional endoplasmic reticulum (tER). Required for secretory cargo traffic from the endoplasmic reticulum to the Golgi apparatus. Involved in peroxisome biogenesis. Regulates the transport of peroxisomal biogenesis factors PEX3 and PEX16 from the ER to peroxisomes.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21768384}; Peripheral membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Localizes to endoplasmic reticulum exit sites (ERES), also known as transitional endoplasmic reticulum (tER). {ECO:0000269|PubMed:17192411, ECO:0000269|PubMed:21478858, ECO:0000269|PubMed:21768384, ECO:0000269|PubMed:22355596}.
Interaction partners:
- Protein SEC13 homolog
- Protein transport protein Sec31A
- Regucalcin
- Protein transport protein Sec23A
- Protein transport protein Sec24C
- Protein transport protein Sec16A
- Glucosamine-6-phosphate deaminase 2
- Transmembrane protein 18
- Protein ERGIC-53
- Small COPII coat GTPase SAR1A
Sequence:
MELWAPQRLPQTRGKATAPSKDPDRGFRRDGHHRPVPHSWHNGERFHQWQDNRGSPQPQQEPRADHQQQPHYASRPGDWHQPVSGVDYYEGGYRNQLYSRPGYENSYQSYQSPTMREEYAYGSYYYHGHPQWLQEERVPRQRSPYIWHEDYREQKYLDEHHYENQHSPFGTNSETHFQSNSRNPCKDSPASNSGQEWPGELFPGSLLAEAQKNKPSLASESNLLQQRESGLSSSSYELSQYIRDAPERDDPPASAAWSPVQADVSSAGPKAPMKFYIPHVPVSFGPGGQLVHVGPSSPTDGQAALVELHSMEVILNDSEEQEEMRSFSGPLIREDVHKVDIMTFCQQKAAQSCKSETLGSRDSALLWQLLVLLCRQNGSMVGSDIAELLMQDCKKLEKYKRQPPVANLINLTDEDWPVLSSGTPNLLTGEIPPSVETPAQIVEKFTRLLYYGRKKEALEWAMKNHLWGHALFLSSKMDPQTYSWVMSGFTSTLALNDPLQTLFQLMSGRIPQAATCCGEKQWGDWRPHLAVILSNQAGDPELYQRAIVAIGDTLAGKGLVEAAHFCYLMAHVPFGHYTVKTDHLVLLGSSHSQEFLKFATTEAIQRTEIFEYCQMLGRPKSFIPSFQVYKLLYASRLADYGLVSQALHYCEAIGAAVLSQGESSHPVLLVELIKLAEKLKLSDPLVLERRSGDRDLEPDWLAQLRRQLEQKVAGDIGDPHPTRSDISGAGGTTTENTFYQDFSGCQGYSEAPGYRSALWLTPEQTCLLQPSPQQPFPLQPGSYPAGGGAGQTGTPRPFYSVPETHLPGTGSSVAVTEATGGTVWEEMLQTHLGPGENTVSQETSQPPDGQEVISKPQTPLAARPRSISESSASSAKEDEKESSDEADKNSPRNTAQRGKLGDGKEHTKSSGFGWFSWFRSKPTKNASPAGDEDSSDSPDSEETPRASSPHQAGLGLSLTPSPESPPLPDVSAFSRGRGGGEGRGSASSGGAAAGAGVGGLSGPESVSFELCSNPGVLLPPPALKGAVPLYNPSQVPQLPTATSLNRPNRLAQRRYPTQPC
Protein: Ethylene-responsive transcription factor ERF119 (Q9LUA2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probably acts as a transcriptional activator. Binds to the GCC-box pathogenesis-related promoter element. May be involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MAERKKRSSIQTNKPNKKPMKKKPFQLNHLPGLSEDLKTMRKLRFVVNDPYATDYSSSEEEERSQRRKRYVCEIDLPFAQAATQAESESSYCQESNNNGVSKTKISACSKKVLRSKASPVVGRSSTTVSKPVGVRQRKWGKWAAEIRHPITKVRTWLGTYETLEQAADAYATKKLEFDALAAATSAASSVLSNESGSMISASGSSIDLDKKLVDSTLDQQAGESKKASFDFDFADLQIPEMGCFIDDSFIPNACELDFLLTEENNNQMLDDYCGIDDLDIIGLECDGPSELPDYDFSDVEIDLGLIGTTIDKYAFVDHIATTTPTPLNIACP
Protein: Polychaetoid, isoform G (Polychaetoid, isoform M) (A8JQV7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKFPDYVPNNMLVGDRTTWEYHTVAVTRVPGYGFGIAVSGGRDNPHFANGDPSIAVSDVLKGGPAEDRLQVNDRIISVNGVSLENVEYATAVQVLRDSGNTVQLVVKRRVPLNPINAAGAVQHQHSHSLSSVGLMANGSGGVAPTPITSLSQPNSLNSSLVQNASSGQPIKVTLTKGGKKDDYGVVLGCRLFVKEISSKAREQLNANGYSLQEGDIITRIHNTNCGDTMSLKEAKKIIDGCKERLNLVVLRDITNQTAVSQLNLNNSASHQASGNIYATHQPQVSGCSSSNNNLEDPYLPGGASYSSQNLYVQPPTRTSNGPNINGNGLNDEKSNLTPRGRSRGPIMDGVSLQQLDRPVTPTRGRSAAIDEPPRPPPPRGSSGGAAQEDFYSSRRQLYEERQSAEPRFISFQKEGSVGIRLTGGNEAGIFVTAVQPGSPASLQGLMPGDKILKVNDMDMNGVTREEAVLFLLSLQDRIDLIVQYCKEEYDEVVTNQRGDSFHIKTHFHCDNPSKGEMAFKAGDVFRVIDTLHNGVVGSWQVLKIGRGHQEMQRGVIPNKSRAEELATAQFNATKKEMNANESRGNFFRRRRSTHRRSKSLSRENWDDVVFSDSISKFPAYERVVLRHPGFVRPVVLFGPVSDLARERLAKDFPDKFSTPLQDDDKSAATSGKCRIVRLSNIRDVMDRGKHALLDITPNAVDRLNYAQFYPVVIFLKTDSKHVIKQLRHGLPKAAHKSSKKLLEQCQKLERVWSHIFSTQIALSDEESWYRKLRDSIDLQQSGAVWMSESKVPYDHAVPANPNRRQTMDSSKYSIYGTNVPPQQQQPGVGGDTAAVRPQSLYGINAPDLPPRIDRQSKPGDIPLNTSGSSSRNGTLGRSAQERLFGKAVVQDDVQAEYITRNALVGSGAAETLDRQQQQQQQTHASLERQARLNAQLKANGVGAGGGGASTYDSVSSYDSYNNTQMAMQNLGRLGPNAPDDLKSVPNANGRPLPPTGQSHEYGRTPHDHRSFGGPNDLNRQSSPGRPHYHDMNASRNIDPRNGTPQRPSNLGLESSPRKPLVETKTDYGKYRRYHLHAPHLKHLHMMHSLSPSSSLSLSPSPSSLPLHMSCGLQLTQQQLLRLSTGGFDRRPIAAPRLHALMAPLPPPALMSSASAYDTLDSGSPRSPNGFYYPPTPSHHHYGQQATPGSPSNGHMQPPPPQQQQPTYGGSNGNYGQAPPPQSYPQANGYNGNGHHYNGGSGTGPYIAPHRGMPPPIGNLPPHTPERHALDLAGSREQRGSAFELYRKPQIGATAGHHHNMR
Protein: RNA-binding protein asd-2 (Alternative splicing defective protein 2) (G5EFF1)
Organism: Caenorhabditis elegans
Function: RNA-binding protein that binds to the 5'-NACUAAY-N(1,20)-UAAY-3' consensus sequence in pre-mRNA introns to promote alternative splicing. Required for mutually exclusive alternative splicing where it modulates the switch between mutually exclusive exons during pre-mRNA maturation. Involved in muscle-specific gene expression regulating the alternative splicing of genes such as let-2 and unc-60 to ensure that their respective isoforms are expressed in muscle. Promotes the removal of intron 10 from let-2 pre-mRNA to allow for the exclusive expression of the muscle-specific let-2 isoform (as opposed to the non-muscle-specific isoform expressed in embryos) in body wall muscles during late larval and adult stages of development. Binds cooperatively with RNA-binding protein sup-12 to intron 1A of the unc-60 pre-mRNA to promote alternative splicing and expression of the muscle specific isoform of unc-60.
Subcellular location: Nucleus {ECO:0000269|PubMed:23071450}.
Interaction partners:
- Mec-8 protein
- Peptidase S1 domain-containing protein
- RRM domain-containing protein
Sequence:
MDCDNGVVSEISDDKELLNLETVIPPPPNDSGHEFIGPSSGPPQVTITPSGVQSGSANGVSTSQQQQYSAEYLSQLLKDKKQLAAFPNVFHHLERLADEEINKVRVVLFQCEFSKESAPLPDAEGDSTVHTEKVFVPAKEHPDYNFVGRILGPRGMTAKQLEQETGCKIMVRGRGSMRDKKKEELNRGKPNWEHLSEELHVLIQCEDTENRAKVKLMRAVEEVRKLLVPAPEGEDDLKRKQLMELAIINGTYRSGTDQSALAAAQLAAVKHQQQPFAAALQAAALQRGVLPMMANGLSRSPTMAVCGAPIVMSPSGRASSAGATATSQAALIMQQQSQLHAANAGNAALQQQAALLQQQQAAEYQQLLLSQAGLYDFSAMQQQYAAVGQNAAVAAAQAQAQAQYGALAAAAAANSAGNQQYADYAGVDLTSQQSAHGGYYVRRWA
Protein: Zinc finger Y-chromosomal protein (P08048)
Organism: Homo sapiens (Human)
Function: Probable transcriptional activator. Binds to the consensus sequence 5'-AGGCCY-3'.
Subcellular location: Nucleus.
Interaction partners:
- Ubiquitin carboxyl-terminal hydrolase 9Y
- Sex-determining region Y protein
- ATP-dependent RNA helicase DDX3Y
- Lysine-specific demethylase 5D
- Eukaryotic translation initiation factor 1A, Y-chromosomal
- Histone demethylase UTY demethylase UTY)
- Small ribosomal subunit protein eS4, Y isoform 1
- Neuroligin-4, Y-linked
- Putative serine/threonine-protein kinase PRKY
- Thymosin beta-4, Y-chromosomal
Sequence:
MDEDEFELQPQEPNSFFDGIGADATHMDGDQIVVEIQEAVFVSNIVDSDITVHNFVPDDPDSVVIQDVVEDVVIEEDVQCSDILEEADVSENVIIPEQVLDSDVTEEVSLPHCTVPDDVLASDITSTSMSMPEHVLTSESMHVCDIGHVEHMVHDSVVEAEIITDPLTSDIVSEEVLVADCAPEAVIDASGISVDQQDNDKASCEDYLMISLDDAGKIEHDGSTGVTIDAESEMDPCKVDSTCPEVIKVYIFKADPGEDDLGGTVDIVESEPENDHGVELLDQNSSIRVPREKMVYMTVNDSQQEDEDLNVAEIADEVYMEVIVGEEDAAVAAAAAAVHEQQIDEDEMKTFVPIAWAAAYGNNSDGIENRNGTASALLHIDESAGLGRLAKQKPKKKRRPDSRQYQTAIIIGPDGHPLTVYPCMICGKKFKSRGFLKRHMKNHPEHLAKKKYHCTDCDYTTNKKISLHNHLESHKLTSKAEKAIECDECGKHFSHAGALFTHKMVHKEKGANKMHKCKFCEYETAEQGLLNRHLLAVHSKNFPHICVECGKGFRHPSELRKHMRIHTGEKPYQCQYCEYRSADSSNLKTHIKTKHSKEMPFKCDICLLTFSDTKEVQQHTLVHQESKTHQCLHCDHKSSNSSDLKRHVISVHTKDYPHKCEMCEKGFHRPSELKKHVAVHKGKKMHQCRHCDFKIADPFVLSRHILSVHTKDLPFRCKRCRKGFRQQNELKKHMKTHSGRKVYQCEYCEYSTTDASGFKRHVISIHTKDYPHRCEYCKKGFRRPSEKNQHIMRHHKEVGLP
Protein: Gibberellin 2-beta-dioxygenase 7 (EC 1.14.11.13) (GA 2-oxidase 7) (Gibberellin 2-beta-hydroxylase 7) (Gibberellin 2-oxidase 7) (Q9C6I4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the 2-beta-hydroxylation of gibberellins (GA) precursors, rendering them unable to be converted to active GAs. Hydroxylates the C20-GA GA12 and GA53, but is not active on C19-GAs, like GA1, GA4, GA9 and GA20.
Interaction partners:
- Gibberellin 3-beta-dioxygenase 2
- Dehydration-responsive element-binding protein 1E
- Dehydration-responsive element-binding protein 1F
- Ent-kaur-16-ene synthase, chloroplastic
- Gibberellin 3-beta-dioxygenase 1
- Gibberellin 3-beta-dioxygenase 3
- Gibberellin 3-beta-dioxygenase 4
- Gibberellin 20 oxidase 4
- Gibberellin 20 oxidase 2
- DELLA protein RGL2
Sequence:
MASQPPFKTNFCSIFGSSFPNSTSESNTNTSTIQTSGIKLPVIDLSHLTSGEEVKRKRCVKQMVAAAKEWGFFQIVNHGIPKDVFEMMLLEEKKLFDQPFSVKVRERFSDLSKNSYRWGNPSATSPAQYSVSEAFHIILSEVSRISDDRNNLRTIVETYVQEIARVAQMICEILGKQVNVSSEYFENIFELENSFLRLNKYHPSVFGSEVFGLVPHTDTSFLTILSQDQIGGLELENNGQWISVKPCLEALTVNIGDMFQALSNGVYQSVRHRVISPANIERMSIAFFVCPYLETEIDCFGYPKKYRRFSFREYKEQSEHDVKETGDKVGLSRFLI
Protein: Valerianol synthase TPS8 (EC 4.2.3.204) (Terpene synthase 8) (CsiTPS8) (A0A167V661)
Organism: Camellia sinensis (Tea plant) (Thea sinensis)
Function: Terpene synthase that catalyzes the biosynthesis of the terpene valerianol.
Interaction partners:
Sequence:
MASSQVGDMVNGNAEPTRHLAKFPPSLWGDRFTSFTLDKQLWDKYGNEIEVLKEQVRSMVVAGGRKAAEQINLINVLERLGVSYHFEKEIEEQLEQLFAKFEDNEDYDLFTIALHFRIFRQHGYKMSCDVFNKFRDSNGEFKETVSNDVQGMLSLYEATYLKIRGEGFLDEAHAFTIAQLESLVGGPHLSSDLSEQVMHALKQSIHRGFPRLEAKHFISFYEKDASRNETLLRLAKLDFNQLQLSHREELCHIFRWWKELDLISKVPYARDRAVECFFWSTCAYYEPQHSVGRAVLTKIMLLLSVTDDTYDAYGTYDELKLYTNAVQRWDVSAMDELPDYMKALYRALLNVYDEVERDLAKQGRDYGVHHSKEAFKEIVRSYEIEAEWFKEGYVASFEEYMKNALVTSTGRLHTTSCFMGLEADVATTEAFEWILTKPKMVAASGAIGRLVDDVMSHDEEQERGHVATGLDCYMKQHGVSKQEAIVELYKMIENAWRDINEEMLKPTAISMKLLIRVLNLSRISDVVYKYVDGYTHPEIIKDHVISLFEDPIPM
Protein: Sphingomyelin phosphodiesterase 5 (EC 3.1.4.12) (Mitochondrial neutral sphingomyelinase) (mtnSMase) (D6MZJ6)
Organism: Mus musculus (Mouse)
Function: Catalyzes the hydrolysis of membrane sphingomyelin to form phosphorylcholine and ceramide.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:20378533}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:F1QG30}; Intermembrane side {ECO:0000250|UniProtKB:F1QG30}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:20378533}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Sphingomyelin phosphodiesterase 4
Sequence:
MSLPDISRRRSPVPQEDWPLTPNALRPSPFPNPVLQALYSLSRVLLFPTYWSLDQLLGCWAPSVRSKSLGWFKVLAGSGVLLPLVVVGLPLALVGLALWLPLQVWRRPFCYQPPPACWVWPQPWHPPAERRRCFVFLTANLCLLPHGLAHFNNLSHSLQRAEAVGAALLDSLQSSQYRVSECSQPPPRVPGGELKATLPMGLDFVCLQEVFDLRAARRLVRVLVPNLGPVIYDVGTFGLMAGPYIKVLGSGLLLASRYPLLRATFRCFPNARREDAMASKGLLSVQAQLGIVDGHPIVGYLHCTHLHAPVEDGHIRCKQLTLLLEWVEEFEAENRQSDEAVAFSVLLGDLNFDNCSQDHAKEQGHKLFSCFQDPCRLGVCQEQPWALGTILNSSMLRHSIACSPEMLRRALRQEKGRRLYLSGPLHGSYPAQSWKGRRLDYITYRRVPGSRLSPEAEQVTFSTAFAGLTDHLAMGLKLQVVCS