wanglab/gogpt-training-data huggingface dataset:
Protein: Lysine-specific demethylase hairless (EC 1.14.11.65) ([histone H3]-dimethyl-L-lysine(9) demethylase hairless) (P97609)
Organism: Rattus norvegicus (Rat)
Function: Histone demethylase that specifically demethylates both mono- and dimethylated 'Lys-9' of histone H3. May act as a transcription regulator controlling hair biology (via targeting of collagens), neural activity, and cell cycle.
Subcellular location: Nucleus.
Interaction partners:
Sequence:
MESMPSFLKDTPAWEKTAPVNGIVGQEPGTSPQDGLHHGALCLGEPVPFWRGVLSAPDSWLPPGFLQGPKDTLSVVEGEGSRNGERKANWLGSKEGLRWKEAMLAHPLAFCGPACPPRYGPLIPEHSSGHPKSDPVAFRPLHCPFLLETKILERAPFWVPTCLPPYLMSSLPPERSYDWPLAPSPWVYSGSQPKVPSAFSLGSKGFYHKDPNILRPAKEPLAASESGMLGLAPGGHLQQACDAEGPSLHQRDGETGAGRQQNLCPVFLGYPDTVPRTPWPSCPPGLVHTLGNVWAGPGSNSFGYQLGPPVTPRCPSPGPPTPPGGCCSSHLPAREGDPGPCRKCQDSPEGSSSGPGESSEERNKAGSRASPPSHHTKLKKTWLTRHSEQFECPGGCPGKGESPATGLRALKRAGSPEVQGARGPAPKRPSHTFPGTGRQGARAWQETPETSTGSKAEAQQQEEQRGPRDGRIRLRESRLEDTSCQHHLAGVTQCPSCVQAAGEVEILTSHSQKSHKLPLEEKPLEEDSCATSEEGGGSSPEASINKGLAKHLLSGLGDRLCRLLRKEREALAWAQREGQGPAMTEDSPGIPHCCSRCHHGLFNTHWRCSHCSHRLCVACGRIAGAGKNREKTGSREQRTDDCAQEAGHAACSLILTQFVSSQALAELSTVMHQVWAKFDIRGHCFCQVDARVWAPGDGGQQKEPTEKTPPAPQLSCNGDSNRTKDIKEETPDSTESPAEDRAGRSPLPCPSLCELLASTAVKLCLGHERIHMAFAPVTPALPSDDRITNILDSIIAQVVERKIQEKALGPGLRAGSGLRKGLSLPLSPVRTQLSPPGALLWLQEPRPKHGFRLFQEHWRQGQPVLVSGIQKTLRLSLWGMEALGTLGGQVQTLTALGPPQPTSLDSTAFWKGFSHPEARPKLDEGSVLLLHRPLGDKDESRVENLASSLPLPEYCAHQGKLNLASYLPLGLTLHPLEPQLWAAYGVNSHRGHLGTKNLCVEVSDLISILVHAEAQLPPWYRAQKDFLSGLDGEGLWSPGSQTSTVWHVFRAQDAQRIRRFLQMVCPAGAGTLEPGAPGSCYLDSGLRRRLREEWGVSCWTLLQAPGEAVLVPAGAPHQVQGLVSTISVTQHFLSPETSALSAQLCHQGASLPPDHRMLYAQMDRAVFQAVKVAVGTLQEAK
Protein: Fumarate and nitrate reduction regulatory protein (P0A9E5)
Organism: Escherichia coli (strain K12)
Function: Global transcription factor that controls the expression of over 100 target genes in response to anoxia. It facilitates the adaptation to anaerobic growth conditions by regulating the expression of gene products that are involved in anaerobic energy metabolism. When the terminal electron acceptor, O(2), is no longer available, it represses the synthesis of enzymes involved in aerobic respiration and increases the synthesis of enzymes required for anaerobic respiration.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Universal stress protein E
- Molybdenum cofactor guanylyltransferase
- Methylated-DNA--protein-cysteine methyltransferase
Sequence:
MIPEKRIIRRIQSGGCAIHCQDCSISQLCIPFTLNEHELDQLDNIIERKKPIQKGQTLFKAGDELKSLYAIRSGTIKSYTITEQGDEQITGFHLAGDLVGFDAIGSGHHPSFAQALETSMVCEIPFETLDDLSGKMPNLRQQMMRLMSGEIKGDQDMILLLSKKNAEERLAAFIYNLSRRFAQRGFSPREFRLTMTRGDIGNYLGLTVETISRLLGRFQKSGMLAVKGKYITIENNDALAQLAGHTRNVA
Protein: Ubiquitin carboxyl-terminal hydrolase 17-like protein D (EC 3.4.19.12) (Deubiquitinating enzyme 2A) (G5E8G2)
Organism: Mus musculus (Mouse)
Function: Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes that may include cell proliferation, progression through the cell cycle, apoptosis, cell migration, and the cellular response to viral infection.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q6R6M4}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q6R6M4}.
Interaction partners:
- Zinc finger-containing ubiquitin peptidase 1
Sequence:
MVVSLSFPEADPALSSPGAQQLHQDEAQVVVELTANDKPSLSWECPQGPGCGLQNTGNSCYLNAALQCLTHTPPLADYMLSQEYSQTCCSPEGCKMCAMEAHVTQSLLHSHSGDVMKPSQILTSAFHKHQQEDAHEFLMFTLETMHESCLQVHRQSEPTSEDSSPIHDIFGGLWRSQIKCLHCQGTSDTYDRFLDVPLDISSAQSVNQALWDTEKSEELRGENAYYCGRCRQKMPASKTLHIHSAPKVLLLVLKRFSAFMGNKLDRKVSYPEFLDLKPYLSQPTGGPLPYALYAVLVHEGATCHSGHYFSYVKAGHGKWYKMDDTKVTSCDVTSVLNENAYVLFYVQQTDLKEVSIDMPEGRIHEVLDPEYQLKKSRRKKHKKKSPCTEDVGEPSKNREKKATKETSLGEGKVLQEKNHKKAGQKHENTKLVPQEQNHQKLGQKHRNNEILPQEQNHQKTGQSLRNTEGELDLPADAIVIHLPRSIANWGRDTPDKVNQPWHNADRLLTSQDLVNTGQLCRQEGRRRSKKGKNKNKQGQKLLLVR
Protein: Calmodulin-2 (CaM-2) (P0DH97)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:23204523}. Cytoplasm {ECO:0000269|PubMed:23204523}. Note=Recruited by IQD1 to microtubules. {ECO:0000269|PubMed:23204523}.
Interaction partners:
- Kinesin-like protein KIN-14E
- Plasma membrane-associated cation-binding protein 1
- Mitogen-activated protein kinase 8
- Calmodulin-binding transcription activator 3
- Two pore calcium channel protein 1
- CDPK-related kinase 1
- Calcium/calmodulin-regulated receptor-like kinase 1
- Calreticulin-1
- Protein IQ-DOMAIN 1
- Heat shock 70 kDa protein 4
Sequence:
MADQLTDDQISEFKEAFSLFDKDGDGCITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLNLMARKMKDTDSEEELKEAFRVFDKDQNGFISAAELRHVMTNLGEKLTDEEVDEMIKEADVDGDGQINYEEFVKVMMAK
Protein: IFT81 calponin homology domain-containing protein (A8DYR7)
Organism: Caenorhabditis elegans
Subcellular location: Cell projection, cilium {ECO:0000256|ARBA:ARBA00004138}.
Interaction partners:
- Intraflagellar transport associated protein 2
- Intraflagellar transport protein 74 homolog
- Intraflagellar transport protein 46 homolog
- Tetratricopeptide repeat protein 30 homolog
- Intraflagellar transport protein 52 C-terminal domain-containing protein
- Intraflagellar transport protein che-13
- Intraflagellar transport protein 88 homolog
- Tetratricopeptide repeat protein 21 homolog
- TRAF3-interacting protein 1
- Clusterin-associated protein 1 homolog
Sequence:
MSNDIQGFILHFLNEEPFNLNLSSLQFDQLPPQQLLQILSNVLSWVSDTDRIDIKREAAEETAIRILNMLRILRYRPPQDQDEQEEWRAGIVEGRKTSLYPLLVFLFENSEGLKERAYLSKYLMKTDVPGEFFDYDIEELQNEIGELTMEFKEIHAEMKGIMADVLLLDDIKEDLKSMEKEKQILLRKIEKTEKKVQNIPYFDKQMQLALQLRGEKTRYADFAIEKQQERQKVLNIEARINRMKINLTEAQAVADTLDEQALMEKLEDEVATNTYLVNGKLFQEIESKENKLKELTAMARSNSVREEDVSRMNSEIEEMSKRIRKLEDERDHKEVDIDENMSVFRHQTSLLERKKETAVQKLQELRQELAKIEKDVDERKTNLKDKVGGEVVSNVQYRKYLEQYRVKSEEQKKKRKEIELMHTEVAVLKRTIDIVSKRYNKLETHIESIGGEIVEVLNVPTKYDRPKTAAPQTNNAEDIKSDMKDMMAALDERKDKITDQRTKRDEVKYVVQQKMSQLATIKMEADQFMAELERDNKRLVENVKELETTVRDCDDRIPELKNELAILLDDKNKMEGVSGENLEELLSKAAEKEQRIDTEIEEMGDFDESRMQAELWKGLLTIFETKIEIFKERANSRN
Protein: Neopentalenolactone D synthase (EC 1.14.13.171) (Neopentalenolactone biosynthesis protein E) (Q82IY8)
Organism: Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680)
Function: Catalyzes the flavin-dependent Baeyer-Villiger oxidation of 1-deoxy-11-oxopentalenic acid to neopentalenolactone D in the biosynthesis of neopentalenolactone antibiotic.
Interaction partners:
Sequence:
MVDIEAVRAKYREERDKRVQADGGRQYLSAQGEFAHYADDPHAKPIERAPVSDEVDVTIIGAGIGGLLLGARLREACAFDTIRLVDKAGDVGGTWYWNRFPGLRCDVESYVYMPLLEELGRLPSEKYATGAEIFEHCQAIARTYDLYDEALLQTSVTELSWDEDSSRWLVRTDRGDLVRSRFVAMAIGSLHRPKLPSIPGTEAFQGHSFHTSRWDFAYTGGDISGGLEKLGDKRVGIVGTGATAVQCIPHLAESAAHLYVFQRTPSTVSVRNNRPTDPGWAAGLEPGWQQRRMDNFHALTSGVDQDVDLVQDGWTEITSKLAAILPKSAADADPKDIGTAVELADFHKMEELRKRVDAIVHDKDTADALKPYYRLFCKRPCFHDGYLDTYNRPNVTLVDTQGRGVERLTPTSVVAGGREYPVDCLIFASGYESEFGVPYTNRTGFSIVGRDGIRLSEKWAEGARTFHGLQVNGFPNCFILSKAQSGLHVNVPYMLNEQSKHVAYILKAVQQRGRQVVEASATGEKEWVETILRLANRNLDFTESCTPGLFNNEGNPRNVAILNSSYGGGSVGFVNILKRWREADDLADLELREG
Protein: Synaptobrevin homolog YKT6 (G0S5G3)
Organism: Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (Thermochaetoides thermophila)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00046280}; Single-pass type IV membrane protein {ECO:0000256|ARBA:ARBA00046280}.
Interaction partners:
- Small conjugating protein ligase-like protein
- t-SNARE coiled-coil homology domain-containing protein
- Probable vacuolar protein sorting-associated protein 16 homolog
- SNAP receptor-like protein
- t-SNARE coiled-coil homology domain-containing protein
- t-SNARE coiled-coil homology domain-containing protein
- Microbial-type PARG catalytic domain-containing protein
- t-SNARE coiled-coil homology domain-containing protein
- V-SNARE coiled-coil homology domain-containing protein
Sequence:
MASSSTSTPLLYACIAYETTILTETTLSPSSHASSLSSLALPKIDHSKPQKATYAREPYHIHYLASSASEYPDDEASAGRLTYLVISPDKTLYRVTCFEFLTTLRTRFLARFPPEKHDFSNFLPYGCAEFEGELRKLMAEYSQRALDVENNGGDSINSVQREIEDVRGIMSRNIEGLLERGERIDLLVDKTDRLGGSAREFRLRSRGLKRKMWWKNVKLMGLLGFVVVLILLTIVTSVKGGV
Protein: Sodium/potassium-transporting ATPase subunit alpha (Q6VYM7)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Cell membrane {ECO:0000256|RuleBase:RU362084}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU362084}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MGDKDGKSSPSKKNKKGKDMDELKKEVPITEHKMSIEECCRKFNTDIVQGLTNAKAAEFLIRDGPNCLTPPPTTPEWIKFCRQLFGGFSILLWTGAILCFLAYAIQAATEDEPAGDNLYLGIVLSVVVVVTGCFSYFQEAKSSKIMESFKNMVPQQALVIREGEKMTINAEEVVAGDLVEVKGGDRIPADLRVVSAHGCKVDNSSLTGESEPQSRSPDCTHDNPLETRNVAFFSTNCVEGTARGIVVCTGDRTVMGRIATLTSGLESGKTPIAKEIEHFIHLITGVAVFLGITFFILAVCLGYTWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMAKKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTEDQSGASFDKTSASWAALARVAALCNRAVFKAGQDQLPILKRDTAGDASESALLKCIELSCGSVKQIREKNKKVAEIPFNSTNKYQLSVHETEDPNDNRYLLVMKGAPERILDRCTTIIIQGKEQPMDEEMKESFQNAYMELGGLGERVLGFCHLLMPEDQYPKGFAFDCDDVNFTTESLCFVGLMSMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIASRLNIPVSRSNPRDAKACVIHGTDLKELSQDQMDDILRNHTEIVFARTSPQQKLIIVEGCQRLGAIVAVTGDGVNDSPALKKADIGVAMGISGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLLFIIVNIPLPLGTITILCIDLGTDMVPAISLAYEAAESDIMKRQPRNPTRDKLVNERLISIAYGQIGMIQALGGFFSYFVILAENGFLPSILVGIRLNWDDRACNDLEDSYGQQWTYEQRKIVEFTCHTAFFVSIVVVQWADVIVCKTRRNSVFQQGMKNKILIFGLFEETALAAFLSYTPGMDVALRMFPLKPSWWFCAVPYSVLIFVYDEIRKLLIRRNPGGWVERETYY
Protein: NRAMP2 isoform 1 (B3F8C5)
Organism: Gallus gallus (Chicken)
Subcellular location: Late endosome membrane {ECO:0000256|ARBA:ARBA00004107}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004107}. Lysosome membrane {ECO:0000256|ARBA:ARBA00004155}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004155}.
Interaction partners:
Sequence:
MGPPYSDLRESDEDRPAEAVGSVSGSRNALQPLPGEDDEEPFTTYFDSKIPIPDDETHSCFSFRKLWAFTGPGFLMSIAYLDPGNIESDLQSGAVAGFKLLWVLLLATVIGLLLQRLAARLGVVTGLHLAEVCHRQYRTVPRIILWLMVELAIIGSDMQEVIGSAIAINLLSVGKIPLWGGVLITIADTFVFLFLDKYGLRKLEAFFGFLITIMALTFGYEYVTVRPDQKQLLRGLFVPECRGCGTPQLEQAVGIVGAVIMPHNMYLHSALVKSRQVNRSNPREVRDANKYFFAESCTALFVSFIINVFVVSVFAEAFYGKTNADVHEVCANASSAHAALFPSDNATLEVDIYKGGAVLGCYFGPAALYIWAIGILAAGQSSTMTGTYSGQFVMEGFLNLRWSRFARVLLTRSIAITPTLFVAIFQDVEHLTGMNDFLNVLMSLQLPFALIPVLTFTSLPSVMNDFANGLFWKIGGGAVILLVCSINMYFVVAYVMALNHVGLYAGAAILSVIYLAFVAYLTWLCLIALGASALSCGTTHCWAFGARPELFLLNNVGADAAVMR
Protein: Protein arginine N-methyltransferase 2 (EC 2.1.1.-) (Protein-arginine N5-methyltransferase) (Type IV protein arginine N-methyltransferase) (Type IV PRMT) (Q10170)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: S-adenosyl-L-methionine-dependent protein-arginine N-methyltransferase that methylates the delta-nitrogen atom of arginine residues to form N5-methylarginine (type IV) in target proteins. Monomethylates ribosomal protein L12.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Protein arginine N-methyltransferase 1
- Ribosomal protein arginine N-methyltransferase rmt3
- Large ribosomal subunit protein uL11m
- Probable MRF1 mitochondrial N
- Alpha N-terminal protein methyltransferase 1
- Ribosomal lysine N-methyltransferase 4
- eRF1 methyltransferase catalytic subunit mtq2
- SET domain and MYND-type zinc finger protein 6
- PWWP domain-containing protein 1
Sequence:
MDAPLVNESVEFQESQESLSLLEASKQLDLKKIQNLVDQGAVTSAIDIESGKNALHFIASYAEKETEVQAIEVTKWILSNGGVWNGIDRANETPGCIARRRNLLRLYETIVDAGVRSELLLSLLERKELTNEQLDTNEKYLQSALSYTQPTEDSSSLLDSDANAVMMSWERKIMHRSAEIIAPTKGRRVLNVGFGLGIIDTFLQEKEPSLHVIIEPHPDVLKHMRKNGWMDRENVIVYETTWENAINDIASKYVFDGIYYDAFAESYEDLRNFFDSVVGLLDPETDSKFSFFNGLGADNQTFYDVYKKLVPIDLVSFGLQCTYESMPVSSKDEEWKGAKRRYWDVSKYFLPIVTFDF
Protein: Homeobox-leucine zipper protein ATHB-52 (HD-ZIP protein ATHB-52) (Homeodomain transcription factor ATHB-52) (Q9FN29)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Serine/threonine-protein kinase WAG2
- Serine/threonine-protein kinase WAG1
- Protein ETHYLENE INSENSITIVE 3
Sequence:
MENSQSQGKNKKKRLTQDQVRQLEKCFTMNKKLEPDLKLQLSNQLGLPQRQVAVWFQNKRARFKTQSLEVQHCTLQSKHEAALSDKAKLEHQVQFLQDELKRARNQLALFTNQDSPVDNSNLGSCDEDHDDQVVVFDELYACFVSNGHGSSSTSWV
Protein: Choline trimethylamine-lyase (Choline TMA-lyase) (EC 4.3.99.4) (Choline utilization protein C) (Glycyl radical enzyme CutC) (GRE CutC) (Q30W70)
Organism: Oleidesulfovibrio alaskensis (strain ATCC BAA-1058 / DSM 17464 / G20) (Desulfovibrio alaskensis)
Function: Glycine radical enzyme that catalyzes the cleavage of a C-N bond in choline, producing trimethylamine (TMA) and acetaldehyde. Is involved in the anaerobic choline utilization pathway that allows D.alaskensis to grow on choline as a source of carbon and energy. Is strictly specific for choline as substrate.
Interaction partners:
- Choline trimethylamine-lyase activating enzyme
- Isethionate sulfite-lyase activating enzyme
- Glycyl-radical enzyme activating protein family
- Acetaldehyde dehydrogenase
- Uncharacterized protein
- EamA domain-containing protein
Sequence:
MDLQDFSHKLAEATKNLTPAERASLKKIFEGVSAEVFSQPAPVSAVATGAESGIPDGPTPRHVKLKENFLKQVPSITVQRAVAITKIAKENPGLPKPLLRAKTFRYCCETAPLVIQDHELIVGSPNGAPRAGAFSPEVAWRWLQDELDTIGSRPQDPFYISEEDKKVLREEVFPFWQNKSVDEFCEGQYREADLWEMSGESFVSDCSYHAVNGGGDSNPGYDVILMKKGMLDIQREAREKLEQLDYANPEDIDKIYFYKSVIETAEGVMIYARRLSAYAAELAARETDPRRKAELQKISEVNARVPAHAPSNFWEAIQAVWTVESLLVVEENQTGMSIGRVDQYMYPFYRADIDSGRLTEYEAFDLAGCMLVKMSEMMWITSEGASKFFAGYQPFVNMCVGGVTREGHDATNDLTYMLMDAVRHVRIYQPTLATRVHNKSPQKYLKKIVDVIRSGMGFPAVHFDDAHIKMMLAKGVSIEDARDYCLMGCVEPQKSGRLYQWTSTGYTQWPICIELVLNHGVPLWYGKKVTPDMGDLSQYDTYEKFEAAVKEQIRWITKNTSVATVISQRAHRELAPKPLMSLMYEGCMESGRDVSAGGAMYNFGPGVVWSGLATYVDSMAAIKKLVYDDRKYTLAQLNEALKADFAGYDQILADCLAAPKYGNDDDYADMIAADLVHFTETEHRKYKTLYSVLSHGTLSISNNTPFGQLLGASANGRRAWMPLSDGISPTQGADYKGPTAIIKSVSKMANDNMNIGMVHNFKLMSGLLDTPEGENGLITLIRTACMLGNGEMQFNYLDNELLLDAQKHPEKYRDLVVRVAGYSAFFVELCKDVQDEIISRTMLHGF
Protein: Nuclear receptor subfamily 1, group I, member 2, isoform CRA_b (Pregnane X nuclear receptor variant 2) (F1D8P9)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU004334}.
Interaction partners:
Sequence:
MTVTRTHHFKEGSLRAPAIPLHSAAAELASNHPRGPEANLEVRPKESWNHADFVHCEDTESVPGKPSVNADEEVGGPQICRVCGDKATGYHFNVMTCEGCKGFFRRAMKRNARLRCPFRKGACEITRKTRRQCQACRLRKCLESGMKKEMIMSDEAVEERRALIKRKKSERTGTQPLGVQGLTEEQRMMIRELMDAQMKTFDTTFSHFKNFRLPGVLSSGCELPESLQAPSREEAAKWSQVRKDLCSLKVSLQLRGEDGSVWNYKPPADSGGKEIFSLLPHMADMSTYMFKGIISFAKVISYFRDLPIEDQISLLKGAAFELCQLRFNTVFNAETGTWECGRLSYCLEDTAGGFQQLLLEPMLKFHYMLKKLQLHEEEYVLMQAISLFSPDRPGVLQHRVVDQLQEQFAITLKSYIECNRPQPAHRFLFLKIMAMLTELRSINAQHTQRLLRIQDIHPFATPLMQELFGITGS
Protein: Protease 3 (EC 3.4.24.55) (Pitrilysin) (Protease III) (Protease pi) (Q7MIS6)
Organism: Vibrio vulnificus (strain YJ016)
Interaction partners:
Sequence:
MHLSPNDTHHYRYLTLDNQLRVLLISSEDATKSAAALAVNVGHFDDPIEREGLAHYLEHMLFLGTEKYPKVGDFQSYINQHGGSNNAWTGTEHTCFFFDVSANVFEKALDRFSQFFVAPLFNEEALDKERQAVESEYRLKLNDDSRRFYQVNKEVVNPNHPFAKFSVGNLETLNDRDGISIRQEIVDFYRTHYSSDLMTLTIYGPQSLDQLQTWTEEKFGPIANNHLAGKTIEAPISDENSTGILVNIEPLKEIRKLIMTFPLPGMDHHYSTKPLSYFAHLLGYEGEGSLMLKLKNKNWVTSLSAGGGAAGSNYRDFTVSCTLTKDGLAHTDEIIQAVFQYIRLIKAEGLEEWRYKEKQAVLESAFRFQEPSRPLDMVSHLVINMQHYAAEDTIYGDYKMAKYDETLLRSLFDYFTVENLRVTLIAKGFEADKEAAWYFTPYRVTPFSDEQKQNYAQINPGWGFELPARNPFICYELDPNPLEADETLPQLIEDLEGFRLWHLQDTEFKVPKGVLYVAIDSPHAVSSAKNIVKTRLCVEMFLDSLAKETYQAEIAGMGYNMYAHQGGVTLTLSGFSQKLPQLLEMILKRFATRDFSPIRFDNIKKQLLRSWRNSAQDRPISQLFNAMTGILQPNNPPFSKLIEALQEIEVEELAEFVDAILAELHVEMFVYGDWQRQQAHDMATTLKNALRVKEQRYEEALRPLIMLGANGSFQREVECGQQDSAVVIYHQCEDTSPHSIALYSLANHLMSATFFHEIRTKQQLGYMVGTGNMPLNKHPGIVLYVQSPNSAPAELVRSIDEFLNAFYMVLLELNEYQWHSSKRGLWNQISAPDTTLRSRAQRLWVAIGNKDTEFNQREKVLEELKNLTRADMIRFVVNELKPRTANRLVMHTQGIAHADAPKIHLGQEIGSIEEFQLRPKDVGLG
Protein: Transcription cofactor vestigial-like protein 1 (Vgl-1) (Protein TONDU) (Q99990)
Organism: Homo sapiens (Human)
Function: May act as a specific coactivator for the mammalian TEFs.
Subcellular location: Nucleus.
Interaction partners:
- Transcriptional enhancer factor TEF-3
- Transcriptional enhancer factor TEF-1
- Transcriptional enhancer factor TEF-5
- Transcription cofactor vestigial-like protein 4
- WW domain-containing transcription regulator protein 1
- Transcriptional coactivator YAP1
- Transcriptional enhancer factor TEF-4
Sequence:
MEEMKKTAIRLPKGKQKPIKTEWNSRCVLFTYFQGDISSVVDEHFSRALSNIKSPQELTPSSQSEGVMLKNDDSMSPNQWRYSSPWTKPQPEVPVTNRAANCNLHVPGPMAVNQFSPSLARRASVRPGELWHFSSLAGTSSLEPGYSHPFPARHLVPEPQPDGKREPLLSLLQQDRCLARPQESAARENGNPGQIAGSTGLLFNLPPGSVHYKKLYVSRGSASTSLPNETLSELETPGKYSLTPPNHWGHPHRYLQHL
Protein: Indole diterpene prenyltransferase paxD (EC 2.5.1.-) (Paxilline synthesis protein D) (Q9C451)
Organism: Penicillium paxilli
Function: Indole diterpene prenyltransferase; part of the gene cluster that mediates the biosynthesis of paxilline, a mycotoxin that acts as an inhibitor of mammalian maxi-K channels. PaxG, the geranylgeranyl diphosphate (GGPP) synthase is proposed to catalyze the first step in paxilline biosynthesis. Condensation of indole-3-glycerol phosphate with GGPP by paxC then forms 3-geranylgeranylindole (3-GGI), followed by epoxidation and cyclization of this intermediate (by paxM and paxB) to form paspaline. Paspaline is subsequently converted to 13-desoxypaxilline by paxP, the latter being then converted to paxilline by paxQ. Finally paxilline can be mono- and di-prenylated by paxD.
Interaction partners:
Sequence:
MQSDELQIPPWESLAEGLGFSNADEEYWWTVFGQPLNKLMDWADYSTSEKYRVLAFIHRYVIPTCGPRPKPNGDQYWDTFMGFDHTPIQVSINFYNSKATVRTGNIPISEASGTTEDPINQKASLDTIASQRHLVPGHNLRLFKHFTDAFFIPNEEANILNAELENRTIAMQAVQCMLSYDFPYRQIQTKVAICPMWKSMQVKRPMGDLMISSIKDLGIDAADYMKSLKVIEDFINSEKAVQSGAYAIFFAFDTMLTDDYQRTRVKIYFATQSTAFNNMVDIFTLGGRLDGPEMQRATKELRKLWMSTMAIPDGLRDDETLPKSPLPCAGVIFNFEIWPGADKPNPKIYLPCAYYGKDDLDIADGMDSFFKDQGWSKSFHSYKDNYIKAFVKDGKVMCRHHDISFSYKGQGAYITAYYKPELSEYADPSVWAPKLFKA
Protein: Retinoid isomerohydrolase (EC 3.1.1.64) (All-trans-retinyl-palmitate hydrolase) (Lutein isomerase) (Meso-zeaxanthin isomerase) (EC 5.3.3.22) (Retinal pigment epithelium-specific 65 kDa protein) (Retinol isomerase) (Q28175)
Organism: Bos taurus (Bovine)
Function: Critical isomerohydrolase in the retinoid cycle involved in regeneration of 11-cis-retinal, the chromophore of rod and cone opsins. Catalyzes the cleavage and isomerization of all-trans-retinyl fatty acid esters to 11-cis-retinol which is further oxidized by 11-cis retinol dehydrogenase to 11-cis-retinal for use as visual chromophore. Essential for the production of 11-cis retinal for both rod and cone photoreceptors. Also capable of catalyzing the isomerization of lutein to meso-zeaxanthin an eye-specific carotenoid (By similarity). The soluble form binds vitamin A (all-trans-retinol), making it available for LRAT processing to all-trans-retinyl ester. The membrane form, palmitoylated by LRAT, binds all-trans-retinyl esters, making them available for IMH (isomerohydrolase) processing to all-cis-retinol. The soluble form is regenerated by transferring its palmitoyl groups onto 11-cis-retinol, a reaction catalyzed by LRAT.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:A9C3R9}. Cell membrane {ECO:0000269|PubMed:19805034}; Lipid-anchor {ECO:0000269|PubMed:19805034}. Microsome membrane {ECO:0000269|PubMed:19805034, ECO:0000269|PubMed:20100834}. Note=Undergoes light-dependent intracellular transport to become more concentrated in the central region of the retina pigment epithelium cells (By similarity). Attached to the membrane by a lipid anchor when palmitoylated (membrane form), soluble when unpalmitoylated. {ECO:0000250|UniProtKB:Q16518, ECO:0000269|PubMed:19805034}.
Interaction partners:
- Lecithin retinol acyltransferase
- Retinol dehydrogenase 5
- Retinol dehydrogenase 10
- NADP-retinol dehydrogenase
- Diacylglycerol O-acyltransferase 1
- Bestrophin
- Bestrophin-2
- Patatin like phospholipase domain containing 4
- Bestrophin
- Acyl-CoA wax alcohol acyltransferase 2.
Sequence:
MSSQVEHPAGGYKKLFETVEELSSPLTAHVTGRIPLWLTGSLLRCGPGLFEVGSEPFYHLFDGQALLHKFDFKEGHVTYHRRFIRTDAYVRAMTEKRIVITEFGTCAFPDPCKNIFSRFFSYFRGVEVTDNALVNIYPVGEDYYACTETNFITKVNPETLETIKQVDLCNYVSVNGATAHPHIENDGTVYNIGNCFGKNFSIAYNIVKIPPLQADKEDPISKSEIVVQFPCSDRFKPSYVHSFGLTPNYIVFVETPVKINLFKFLSSWSLWGANYMDCFESNETMGVWLHIADKKRKKYINNKYRTSPFNLFHHINTYEDHEFLIVDLCCWKGFEFVYNYLYLANLRENWEEVKKNARKAPQPEVRRYVLPLNIDKADTGKNLVTLPNTTATAILCSDETIWLEPEVLFSGPRQAFEFPQINYQKYGGKPYTYAYGLGLNHFVPDRLCKLNVKTKETWVWQEPDSYPSEPIFVSHPDALEEDDGVVLSVVVSPGAGQKPAYLLILNAKDLSEVARAEVEINIPVTFHGLFKKS
Protein: Protein LYK5 (LysM domain receptor-like kinase 5) (LysM-containing receptor-like kinase 5) (O22808)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May recognize microbe-derived N-acetylglucosamine (NAG)-containing ligands.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Chitin elicitor receptor kinase 1
- LysM domain-containing GPI-anchored protein 1
- LysM domain-containing GPI-anchored protein 2
- U-box domain-containing protein 13
- Extra-large guanine nucleotide-binding protein 2
- LysM domain-containing GPI-anchored protein 3
- U-box domain-containing protein 12
- Elongation factor Tu, chloroplastic
- Respiratory burst oxidase homolog protein D
- Elongation factor Tu
Sequence:
MAACTLHALSVTLFLLLFFAVSPAKAQQPYVNNHQLACEVRVYDNITNGFTCNGPPSCRSYLTFWSQPPYNTADSIAKLLNVSAAEIQSINNLPTATTRIPTRELVVIPANCSCSSSSGGFYQHNATYNLSGNRGDETYFSVANDTYQALSTCQAMMSQNRYGERQLTPGLNLLVPLRCACPTAKQTTAGFKYLLTYLVAMGDSISGIAEMFNSTSAAITEGNELTSDNIFFFTPVLVPLTTEPTKIVISPSPPPPPVVATPPQTPVDPPGSSSSHKWIYIGIGIGAGLLLLLSILALCFYKRRSKKKSLPSSLPEENKLFDSSTKQSIPTTTTTQWSIDLSNSSEAFGLKSAIESLTLYRFNDLQSATSNFSDENRIKGSVYRATINGDDAAVKVIKGDVSSSEINLLKKLNHSNIIRLSGFCIREGTSYLVFEYSENGSISDWLHSSGKKSLTWKQRVEIARDVAEALDYLHNYITPPHIHKNLESTNILLDSNFRAKIANFGVARILDEGDLDLQLTRHVEGTQGYLAPEYVENGVITSKLDVFAFGVAVLELLSGREAVTIHKKKEGEEEVEMLCKVINSVLGGENVREKLKEFMDPSLGNEYPLELAYTMAQLAKSCVATDLNSRPSVTQVLTTLSMIVSSSIDWEPSDDLLRSGSLGN
Protein: Trissin (Q4V645)
Organism: Drosophila melanogaster (Fruit fly)
Function: Activates the G-protein coupled receptor TrissinR in vitro, leading to increased intracellular calcium ion levels.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Natalisin, isoform D
- Trissin receptor
- Ecdysis triggering hormone
- Cardioactive peptide
- Allatostatin C, isoform A
- Beta glycoprotein hormone related polypeptide
Sequence:
MTKTTMHWLAHFQIILLCIWLMCPPSSQAIKCDTCGKECASACGTKHFRTCCFNYLRKRSDPDALRQSSNRRLIDFILLQGRALFTQELRERRHNGTLMDLGLNTYYP
Protein: Eukaryotic translation initiation factor 5A (eIF-5A) (eIF-4D) (P13651)
Organism: Dictyostelium discoideum (Social amoeba)
Function: mRNA-binding protein involved in translation elongation. Has an important function at the level of mRNA turnover, probably acting downstream of decapping. Critical for the efficient synthesis of peptide bonds between consecutive proline residues. Can resolve ribosomal stalling caused by consecutive prolines during translation (By similarity). Involved in actin dynamics and cell cycle progression, mRNA decay and probably in a pathway involved in stress response and maintenance of cell wall integrity. Functions as a regulator of apoptosis (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P23301}.
Interaction partners:
- Small ribosomal subunit protein eS30
- Small ribosomal subunit protein eS1
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein uS19
- Large ribosomal subunit protein eL13
- Large ribosomal subunit protein eL21
- Small ribosomal subunit protein eS6
- Small ribosomal subunit protein uS13
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein uL29
Sequence:
MSDNEALDVEDYAQAGSGASLTFPIQCSALRKNGFVVIKGFPCKIVDMSTSKTGKHGHAKVNITAIDIFTGKKYEEICPSTHNIDVPNVSRKEYTVMDVQDGYLSLLDAGGEVKEDLALPEDDIGKEITQMLKEGKEPLVSVISALGKEGVVSVKVSNN