wanglab/gogpt-training-data huggingface dataset:
Protein: Interleukin-20 (IL-20) (Cytokine Zcyto10) (Q9NYY1)
Organism: Homo sapiens (Human)
Function: Pro-inflammatory and angiogenic cytokine mainly secreted by monocytes and skin keratinocytes that plays crucial roles in immune responses, regulation of inflammatory responses, hemopoiesis, as well as epidermal cell and keratinocyte differentiation. Enhances tissue remodeling and wound-healing activities and restores the homeostasis of epithelial layers during infection and inflammatory responses to maintain tissue integrity. Affects multiple actin-mediated functions in activated neutrophils leading to inhibition of phagocytosis, granule exocytosis, and migration. Exert its effects via the type I IL-20 receptor complex consisting of IL20RA and IL20RB. Alternatively, can mediate its activity through a second receptor complex called type II IL-20 receptor complex composed of IL22RA1 and IL20RB. Acts as an arteriogenic and vascular remodeling factory by activating a range of signaling processes including phosphorylations of JAK2 and STAT5 as well as activation of the serine and threonine kinases AKT and ERK1/2 (By similarity). Alternatively, can activate STAT3 phosphorylation and transcriptional activity in a JAK2, ERK1/2 and p38 MAPK-dependent manner in keratinocytes.
Subcellular location: Secreted {ECO:0000269|PubMed:34403503}.
Interaction partners:
- Interleukin-20 receptor subunit alpha
- Interleukin-20 receptor subunit beta
- Interleukin-22 receptor subunit alpha-1
- Interleukin-24
- Interleukin-19
- Interleukin-13 receptor subunit alpha-2
Sequence:
MKASSLAFSLLSAAFYLLWTPSTGLKTLNLGSCVIATNLQEIRNGFSEIRGSVQAKDGNIDIRILRRTESLQDTKPANRCCLLRHLLRLYLDRVFKNYQTPDHYTLRKISSLANSFLTIKKDLRLCHAHMTCHCGEEAMKKYSQILSHFEKLEPQAAVVKALGELDILLQWMEETE
Protein: Xylose transport system permease protein XylH (P0AGI4)
Organism: Escherichia coli (strain K12)
Function: Part of the binding-protein-dependent transport system for D-xylose. Probably responsible for the translocation of the substrate across the membrane.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Xylose import ATP-binding protein XylG
- D-xylose-binding periplasmic protein
- D-allose-binding periplasmic protein
- Ribose import binding protein RbsB
- Xylose operon regulatory protein
- Arabinose import ATP-binding protein AraG
- Ribose import ATP-binding protein RbsA
- Galactofuranose-binding protein YtfQ
- Galactofuranose transporter ATP-binding protein YtfR
- D-allose import ATP-binding protein AlsA
Sequence:
MSKSNPSEVKLAVPTSGGFSGLKSLNLQVFVMIAAIIAIMLFFTWTTDGAYLSARNVSNLLRQTAITGILAVGMVFVIISAEIDLSVGSMMGLLGGVAAICDVWLGWPLPLTIIVTLVLGLLLGAWNGWWVAYRKVPSFIVTLAGMLAFRGILIGITNGTTVSPTSAAMSQIGQSYLPASTGFIIGALGLMAFVGWQWRGRMRRQALGLQSPASTAVVGRQALTAIIVLGAIWLLNDYRGVPTPVLLLTLLLLGGMFMATRTAFGRRIYAIGGNLEAARLSGINVERTKLAVFAINGLMVAIAGLILSSRLGAGSPSAGNIAELDAIAACVIGGTSLAGGVGSVAGAVMGAFIMASLDNGMSMMDVPTFWQYIVKGAILLLAVWMDSATKRRS
Protein: Tail tube terminator protein p142 (TrP-142) (Tail protein p142) (Tail-to-head joining protein p142) (THJP) (Q6QGE1)
Organism: Escherichia phage T5 (Enterobacteria phage T5)
Function: Plays an essential role in tail assembly by capping the rapidly polymerizing tail once it has reached its requisite length and serving as the interaction surface for the completion protein.
Subcellular location: Virion {ECO:0000269|PubMed:24198424, ECO:0000269|PubMed:36961893}. Note=Component of the tail (PubMed:24198424, PubMed:36961893). Located between the last TTP-pb6 ring and the phage capsid connector (PubMed:36961893). {ECO:0000269|PubMed:24198424, ECO:0000269|PubMed:36961893}.
Interaction partners:
Sequence:
MDHRTSIAQAMVDRISKQMDGSQPDEYFNNLYGNVSRQTYKFEEIREFPYVAVHIGTETGQYLPSGQQWMFLELPILVYDKEKTDIQEQLEKLVADIKTVIDTGGNLEYTVSKPNGSTFPCEATDMIITSVSTDEGLLAPYGLAEINVTVRYQPPRRSLRR
Protein: Coronin (Q9W3W1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MAWRFKASKYKNAAPIVPKAEACVREICVGSYQTYGNNIAASGAFMAFNWEHTGSSVAVLPLDDCGRKSKTMPLLHGHTDTVTDLKFSPFHDGLLATASQDCLVKIWHIPEKGLEQSLSDPEAIFSHKQRRVETVGFHPTADGLMYSTAAGCVALFDLSTQKEIFSNNEHPEVIQSASWREDGSVLATSCKDKNVRIFDPRAAGSPIQLTAESHQSIKDSRVVWLGNQHRILTTGFDAARLRQVIIRDVRNFNTPEKTLELDCSTGILMPLFDPDTNMLFLAGKGDTTINYLEITDKDPYLIEGLRHTGEQTKGACLVPKRALKVMEAEVNRVLQLTSNMVIPIMYQVPRKTYRDFHADLYPETTGYKTELVAGEWLNGSNQAVPKMSLDPAKREHGDEPIIPRLGPKPFSSTTGDVSFDKVFAVPLAPGSHENISNVGQDSGVEMTPAQGAKPDLIVEIEIKKKHEREPAVSGNGVQKSLTTSERRKIFEQNSESSENSTEGEDRTDADLRRNCTSRSSFAERRRIYENRSKSQVDEKPQSPVPLRREHSKVEPLKPNQQQQQQGNVIDTKRISVPEGKLMEEHRRGNGAGLKKSATEAAFSAASTKRTSTVFGKVSKFRHLKGTPGHKSTHIENLRNLSRQIPGECNGFHANQERVAVPLSGPGGKIAIFELSRPGRLPDGVIPSLVNGSNIMDFQWDPFDAQRLAVACDDGIVKIWHIEAGGLSEPTNTPAGELTAHLDKIYFIRFHPLAADVLLTASYDMTIKLWDLRTMTEKCSLSGHTDQIFDFAWSPCGRLGATVCKDGKIRVYNPRKSETPIREGNGPVGTRGARITWALEGHYIVCTGFDKVSERQISVYNAQKLSAPLNTASLDVSPSILIPFYDEDSSTLFVTGKGDSTIYCYEITDEEPYICPLSHHRCTSLHQGLSFLTKNHCDVASVEFSKAYRLTNTTIEPLSFTVPRIKSELFQDDLFPPTRITWSATLSSEDWFASNDKAAPKVSLKPEGMETLSSIQQVPAQPVKKPDHPQFGGQKSEYEINKQQEIQKSVSARMEFTTKLEQDDMEGVDENEWQE
Protein: Major fimbrium subunit FimC (B2RH57)
Organism: Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561)
Function: Minor component of fimbriae. These long, filamentous pili are attached to the cell surface; they mediate biofilm formation, adhesion onto host cells and onto other bacteria that are part of the oral microbiome. They play an important role in invasion of periodontal tissues and are major virulence factors (Probable). FimC, FimD and FimE contribute to interaction with host CXCR4 and thereby down-regulate the TLR2-mediated host immune response.
Subcellular location: Fimbrium {ECO:0000269|PubMed:17526848, ECO:0000269|PubMed:19506009}. Cell outer membrane {ECO:0000305}. Note=Probably synthesized as a palmitoylated precursor. Efficient export to the outer membrane and integration into fimbriae requires lipidation and subsequent proteolytic removal of the lipidated propeptide (Probable). Probably part of the fimbrium tip, as a part of the complex formed by FimC, FimD and FimE. {ECO:0000305, ECO:0000305|PubMed:17675496}.
Interaction partners:
Sequence:
MKMKYFHHPSGLLPRLLLLLLLTMGAVACTKEDNPDQPTSDEVATVKMSLDDVEMRGGDLYSGEDLIKKVRIFVFREGLNGLWVLDKQKLFASGQSDFQNPFTISAHAGPRQIYVIANEPDALTTKLDKILFKKELEDMQAPDVNEPIVRPFTMTGMATATLNPQGTVQANISLNRIAAKITLDIKQVTPGSDVIKITKVQILRNAKNSRLLEGTNKPTGYWNWANACDLPLTNNGSAQSIIQASAPLYVYENIGSDSDSSGRATQLVVEALYNGIKTRYYAYVNDKTTTANHHYSIRRNHHYKLDGTITKMGEFSSLLLTTTVLPWTVENLDYGFLVPYVAEINPHAVITQDNVVTFENSLSFTVRIKGRDGSRWKATLDNGLEFGFDSGSAIDGAADGTTVYTIKVKALKPNGIGIQRRTNLFFTVDGKKVILDKNINPQPTDIKIIQQGL
Protein: Cytochrome b5 (P56395)
Organism: Mus musculus (Mouse)
Function: Cytochrome b5 is a membrane-bound hemoprotein functioning as an electron carrier for several membrane-bound oxygenases. It is also involved in several steps of the sterol biosynthesis pathway, particularly in the C-5 double bond introduction during the C-5 desaturation.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Microsome membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
Interaction partners:
- NADH-cytochrome b5 reductase 3
- NADH-cytochrome b5 reductase-like
- NADH-cytochrome b5 reductase 1
- NADPH--cytochrome P450 reductase
- Steroid 17-alpha-hydroxylase/17,20 lyase
- Acyl-CoA desaturase 1
- Membrane-associated progesterone receptor component 1
- Peptidyl-prolyl cis-trans isomerase G
- Cytochrome b5 reductase 4
- Cytochrome P450 2E1
Sequence:
MAGQSDKDVKYYTLEEIQKHKDSKSTWVILHHKVYDLTKFLEEHPGGEEVLREQAGGDATENFEDVGHSTDARELSKTYIIGELHPDDRSKIAKPSDTLITTVESNSSWWTNWVIPAISALAVALMYRLYMAED
Protein: Zinc finger protein 644 (Zinc finger motif enhancer-binding protein 2) (Zep-2) (Q9H582)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus.
Interaction partners:
- Histone-lysine N-methyltransferase EHMT2
- Protein Wiz
- Zinc finger protein 292
- Chromodomain Y-like protein
Sequence:
MRSFLQQDVNKTKSRLNVLNGLANNMDDLKINTDITGAKEELLDDNNFISDKESGVHKPKDCQTSFQKNNTLTLPEELSKDKSENALSGGQSSLFIHAGAPTVSSENFILPKGAAVNGPVSHSSLTKTSNMNKGSVSLTTGQPVDQPTTESCSTLKVAADLQLSTPQKASQHQVLFLLSDVAHAKNPTHSNKKLPTSASVGCDIQNSVGSNIKSDGTLINQVEVGEDGEDLLVKDDCVNTVTGISSGTDGFRSENDTNWDPQKEFIQFLMTNEETVDKAPPHSKIGLEKKRKRKMDVSKITRYTEDCFSDSNCVPNKSKMQEVDFLEQNEELQAVDSQKYALSKVKPESTDEDLESVDAFQHLIYNPDKCGEESSPVHTSTFLSNTLKKKCEESDSESPATFSTEEPSFYPCTKCNVNFREKKHLHRHMMYHLDGNSHFRHLNVPRPYACRECGRTFRDRNSLLKHMIIHQERRQKLMEEIRELKELQDEGRSARLQCPQCVFGTNCPKTFVQHAKTHEKDKRYYCCEECNFMAVTENELECHRGIAHGAVVKCPMVTSDIAQRKTQKKTFMKDSVVGSSKKSATYICKMCPFTTSAKSVLKKHTEYLHSSSCVDSFGSPLGLDKRKNDILEEPVDSDSTKTLTKQQSTTFPKNSALKQDVKRTFGSTSQSSSFSKIHKRPHRIQKARKSIAQSGVNMCNQNSSPHKNVTIKSSVDQKPKYFHQAAKEKSNAKANSHYLYRHKYENYRMIKKSGESYPVHFKKEEASSLNSLHLFSSSSNSHNNFISDPHKPDAKRPESFKDHRRVAVKRVIKESKKESSVGGEDLDSYPDFLHKMTVVVLQKLNSAEKKDSYETEDESSWDNVELGDYTTQAIEDETYSDINQEHVNLFPLFKSKVEGQEPGENATLSYDQNDGFYFEYYEDTGSNNFLHEIHDPQHLETADASLSKHSSVFHWTDLSLEKKSCPYCPATFETGVGLSNHVRGHLHRAGLSYEARHVVSPEQIATSDKMQHFKRTGTGTPVKRVRKAIEKSETTSEHTCQLCGGWFDTKIGLSNHVRGHLKRLGKTKWDAHKSPICVLNEMMQNEEKYEKILKALNSRRIIPRPFVAQKLASSDDFISQNVIPLEAYRNGLKTEALSVSASEEEGLNFLNEYDETKPELPSGKKNQSLTLIELLKNKRMGEERNSAISPQKIHNQTARKRFVQKCVLPLNEDSPLMYQPQKMDLTMHSALDCKQKKSRSRSGSKKKMLTLPHGADEVYILRCRFCGLVFRGPLSVQEDWIKHLQRHIVNANLPRTGAGMVEVTSLLKKPASITETSFSLLMAEAAS
Protein: Cyclin-dependent kinase 2 homolog (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (cdc2-related kinase 2) (Q8IDW1)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Oocyst capsule protein
- Cell division cycle protein 20 homolog, putative
- Cyclin-dependent kinases regulatory subunit
- ATPase AAA-type core domain-containing protein
- Cyclin-dependent kinase 2 homolog
- Origin recognition complex subunit 2
- Cyclin
Sequence:
MNRIDISNFDFLYVIGKGTYGIVYKALDKKENNFVAIKKIINLCDENYGISKCILRELTILQKIKHKNIINLKYVFYGKDIEDKLKGENLENSCLYLAFEYCDIDLFNLIKKHNLNIKEIKYIIFELLLALSYFHSNNYIHRDIKPENIFITSEGEIKLGDLGMSVEKSDHMTPTVVTLWYRAPEILLKSTNYDQKVDIWSLGCLFMELIQGRPLFPGKNDCTQLELIYLLLGDKDKLTTVDKERKDMFPYFEINMLKDAIDDEHTLDLISKMLIYDPNYRISSKEALKHPCFQDIEQVKFSYNF
Protein: Small ribosomal subunit protein uS11A (40S ribosomal protein S14a) (C0HKA0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Small ribosomal subunit protein uS7B
- Large ribosomal subunit protein eL36
- Large ribosomal subunit protein eL6
- Large ribosomal subunit protein uL30
- Small ribosomal subunit protein eS25
- Small ribosomal subunit protein eS6
- Small ribosomal subunit protein uS9
- Small ribosomal subunit protein eS8
- Large ribosomal subunit protein eL31
- GEO07453p1
Sequence:
MAPRKAKVQKEEVQVQLGPQVRDGEIVFGVAHIYASFNDTFVHVTDLSGRETIARVTGGMKVKADRDEASPYAAMLAAQDVAEKCKTLGITALHIKLRATGGNKTKTPGPGAQSALRALARSSMKIGRIEDVTPIPSDSTRRKGGRRGRRL
Protein: PX domain-containing protein (Q9GYJ9)
Organism: Caenorhabditis elegans
Interaction partners:
- Vacuolar protein sorting-associated protein 29
- PX domain-containing protein
- Vacuolar protein sorting-associated protein 26
- Vacuolar protein sorting-associated protein 35
- Sorting nexin-3
- Sorting nexin-27
- Endocytosis protein RME-8
- Uncharacterized protein
- Amphiphysin
- Sorting nexin lst-4
Sequence:
MLSEEDVHTNSYAGRTVAVMEQPDLFSDDCDEINLGNEDTPPSKLRLHTTEEPKESSSPAVINSIEDHDQYVGNDNHYAQISPEPALSNFKVTMREFEKRGDGMNAYIVYKLETEVSGVVGYTKQHYETWRRFSDFLGLHGKIVEKYLAKGIVIPQPPEKSISALTKTKTNSDPAMSREVGIQRARQLERYICRLIQHPRMRNDCDVRDFLTIESDLPKAVQTAALSSFGVKKIFKNFQVVFSKMAFHMEEGDRWFEQVQSQVDELDEALRKLYTVTETLVASRRDMATSGEQLGKALSMLAACEESTSLSRALSSLTDVTENVSAVYGKQAEVDNSKFSESIYEYIMLISALKDVFGERVRAWQQWQDAQQTLARKRDQKTKIDLSAGGRNERSDQLKGEIEDTVQKMDQLEQHFIELSKAIREEVARFDADRKQDMKKMLVEYMESMIHTHTELLHLWEKFEPEANNIRV
Protein: Receptor-like serine/threonine-protein kinase (EC 2.7.11.1) (O49974)
Organism: Zea mays (Maize)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MVSSPRLLFLLLAGASLCCVAAQKTDTLRQGESLSGAATLVSSPEGVFEAGFFAPDPKQPSRQYLGIWYHSISPRTVVWVANRVAPATSASPSLTLTVTGDLRVLDGTAANGTADAPLLWSSNTTSRAGPRGGYSAVLQDTGSLEVRSEDGVLWDSFWHPTDTILSGMRITLQAPGRGPKERMLFTSWASETDPSPGRYALGLDPGNSGQAYIWKDGNVTYWRSGQWNGVNFIGIPWRPLYRSGFTPAIDPVLGNYYTYTATNTSLQRFVVLPNGTDICYMVRKSSQDWELVWYQPSNECEYYATCGPNAKCTASQDGKAKCTCLKGFHPKLQEQWNAGNWSQGCIRSPPLGCETNQSGDGFLPMGNIKWPDFSYWVSTVGDEPGCRTVCLNNCSCGAYVYTATTGCLAWGNELIDMHELQTGAYTLNLKLPASELRGHHPIWKIATIISAIVLFVLAACLLLWWKHGRNIKDAVHGSWRSRHSSTQSQQNSAMLDISQSIRFDDDVEDGKSHELKVYSLDRIRTATSNFSDSNKLGEGGFGPVYMGTLPGGEEVAVKRLCRNSGQGLEEFKNEVILIAKLQHRNLVRLLGCCIPREEKILVYEYMPNKSLDAFLFNPEKQRLLDWKKRFDIIEGIARGLLYLHRDSRLRVVHRDLKASNILLDADMKPKISDFGMARMFGGDQNQFNTNRVVGTFGYMSPEYAMEGIFSVKSDVYGFGVLILEIITGKRAVSFHCHEDSLNIAGYAWRQWNEDNAAELIDPVIRASCSVRQVLRCIHIALLCVQDHADERPDIPTVILMLSNDSSSLPNPRPPTLMLRGREIESSKSSEKDRSHSIGTVTMTQLHGR
Protein: Beta-1,3-galactosyltransferase brn (EC 2.4.1.62) (Brainiac protein) (Neurogenic secreted-signaling protein brn) (Q24157)
Organism: Drosophila melanogaster (Fruit fly)
Function: Neurogenic protein essential for the development and maintenance of epithelial structure. Required in the germline for establishing the follicular epithelium and for determining the dorsal-ventral polarity. Collaborates with Notch on the apical surface of follicle cells to mediate germline-follicle cell adhesion. Brn has a role in chorion formation.
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Beta-1,4-mannosyltransferase egh
- Beta1,4-N-acetylgalactosaminyltransferase B
- Nidogen
- Hemolectin, isoform A
- Beta1,4-N-acetylgalactosaminyltransferase A
Sequence:
MQSKHRKLLLRCLLVLPLILLVDYCGLLTHLHELNFERHFHYPLNDDTGSGSASSGLDKFAYLRVPSFTAEVPVDQPARLTMLIKSAVGNSRRREAIRRTWGYEGRFSDVHLRRVFLLGTAEDSEKDVAWESREHGDILQAEFTDAYFNNTLKTMLGMRWASDQFNRSEFYLFVDDDYYVSAKNVLKFLGRGRQSHQPELLFAGHVFQTSPLRHKFSKWYVSLEEYPFDRWPPYVTAGAFILSQKALRQLYAASVHLPLFRFDDVYLGIVALKAGISLQHCDDFRFHRPAYKGPDSYSSVIASHEFGDPEEMTRVWNECRSANYA
Protein: Crossveinless c, isoform C (Crossveinless c, isoform D) (A8JR05)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Ras-like GTP-binding protein Rho1
- Crossveinless
- CIN85 and CD2AP related, isoform J
- GH13542p
Sequence:
MSNARELALIEKWADIATPATPNRPTLSPTSPPALHRSIVKFCCCPQRRRYNLKQAKSHGGSNKLNVNTLHARNIFVDSDFSYIDDVPRRRQDCHSDYDDCNYDSDCGGDKADDEANDIAAAPRDDGNVALILMNQRNLSEQWRQDNKGNSNSNKAATKTCAVTKSPQSGNEQQQHQQQQQQQQQQRQPTQRLSNSLQQQQQQEQQLQQQQQQQHSNKENTLSYDNNNKPHCNYCKLPDTAEPQTNSNSNSKIDSPKSSQNKMTITTATDTETATATTATATGECGLPAATSQEFVGAATEVLCNDKATLTAATPAATATTAATTPKPRIAARPTTPSRLKTVIKTTMVKRSPSHDSTATAAHVLLPHSCSSNSNSSSNNIGAHDEPRRSVRERIAAFAAGNEQQQAARQHDKVKKLTKMQCNSNTNQNNMTAEDVKSAISNSSSSSSNQLQQQQHQTLINGQAATVPAATAAATGGVAAATSGRTSAIAADTTRYKSGLSDVAANGDVDGRPTSSATTSVVATGAPSVFSTGCATMPRTRQYGSNVAAALATGATLATSATSATSSATGATSPGSHTMTADKKFLSQAAPVQGHHHHKLQFADKADSELAALDNLDLAHSLDLLDVDGEDPYGALQDYLERVKREINEVFELRKVQRLEQQLREQLEERLSQAGVQQLDELSRSTESDSGFDSSSTTATSGTPATATAAGAGAVTSGKPVTTKLRALPPPPLSPTKTTTNSMPTPPVQADDVNIWACKFLRDLDSLMAAGDKLPPHLAALAEGSGSGSASSSPTSRTAPILLSAAASAAIQSRLGKGSSSIMEHQLQQQQQQQNGLVLKPEKHATIPLQSFYLDCGRNEASPATKSNVAYMRTLSAPNGGFASGGGGGAARGSGAPALPPQSQRKSLACPPLNGQADTITPTPATHKLTNFQSALKIEEMAAAKGTAMATGESQLATTIEDLKSRRQRQLSGGDMETMLASQPMSMPKRVGINHAVLTSRNAITPPPASASSASQSAASVHSAKGSSSAGTTPGYLVDVTKKGSTSTIWTSEESILRSVGAVDEDNNSTSSSSACEEATGVLSSGKSGISLDSSGLDNDNNESGIGTATPPKDMSHYWKSHHLQHHHHHHHRKCTGSAQDNESVSSLEALRKMKFQKSGSVASSDDPDVLEVLSQCGSGGEANESQDDMLDEEKDKMSKSQDYDEIWDCDCTDGDASSASGGGGVTATPVILRRKYTAPPPILVPRTQRSHSLDHYHSPQPLVHPRKVLPIHHHALKSKERGQLSLVLRQEPFQSLLSPSATAANQLHHFVELPSPSSASLHSGLGDSGGIQELCTKSNSAPMLLKEREMSRRFDNFEAQHLTLRYSRSQSDRYLAEIEAVEACKWLRAAGFPQYAQMYEDHQFPIDLNNVAKDHTNLENDQLQSLYRRLCVLNRCATMRLDQSHKPQTPQQKEESDDENFALSEHWTFQPHIRRWSRIGEMGLELPPPGLLSLNVEKTESSSKESSPDRFEEDGAGITLVTPGCSKAGGIPNDGSSLGEGSDSGRLRRSGSERIKDQAKALLRRVESIKSRRRKRQNRENVVISGPTVLDLSQFGQRSSLRKPDAVYSTPPSPSALSPMHTFPKAPFFGNDLKVPSHSDNFLSPNRSSPKRTPTTPRSMRTSPLHFFSSPMSQLKEGKSDDSSSYYSDSQESSTGGKLSLRKPSKARRFLQRTGKVDDIGAHSDSECHQGRKLLIKDANSNTTEVKVKKLTRGGSLNLGKDPKKRDGFRSSSFRSRSTSRKEAKNDEDTAGATTNGGSKRQPVVRWHSFQMEERPNMIFRKCFSKKIEPLQEDAGGMPFAAMSAGQLQIIRKLALVTLTGHMERYCPSHRSGWNWELPKFIKKIKMPDYKDKKVFGVPLLMILQRSGQTLPLAVRAAFRWLQLNALDQVGIFRKSGGKSRIMKLREQIEVTDSTAECMDVFDLQQAYDVADMLKQYFRELPESLLTTKMSETFVAIFQHLPAEVRLDAVQCAVLLLPDENREILYVLLEFLTIVAANSQQNQMTSNNLGVCLAQSIFHSSISTGSASVSASPRRKGKGSGMPDMKELAEAKASHECLSFMIEHYKQIYTAAKEKLSKCNFSYMEESKPLPLEALGEGMQFHNWRGYLYECTSATIKEGREKTRGWFSINSLNDSSVDIAYKKVGDGHPLRLWRCSTEIEGPPKEVLEFVIKQRASWDTNLLQCQTVKKLDDRTEIYQYALDGQLTTDFCVLRSWQTDLPRGACVIVETSIDHAKAKPLFGAVRGVVLASRYLIEPCGSGRSRVMHLARVDVKGKTPEWYNKNYGHICSHYLSRIRLAFKHVADGPESKV
Protein: tryptophan synthase (EC 4.2.1.20) (Q9FFW8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Tryptophan synthase alpha chain
- Tryptophan synthase alpha chain, chloroplastic
- Indole-3-glycerol phosphate synthase, chloroplastic
- indole-3-glycerol-phosphate synthase
- Threonine dehydratase biosynthetic, chloroplastic
- Anthranilate synthase beta subunit 2, chloroplastic
- N-
- N-
- N-
- anthranilate synthase
Sequence:
MASQLLLPPNQFTKSVSPQVFITGDCQGFSDLTLKRKSNQATRVSNGSSLRVKAALRSTHNKSVVEIPKQWYNLVADLSVKPPPPLHPKTFEPIKPEDLAHLFPNELIKQEATQERFIDIPEEVLEIYKLWRPTPLIRAKRLEKLLQTPARIYFKYEGGSPAGSHKPNTAVPQAYYNAKEGVKNVVTETGAGQWGSSLAFASSLFGLDCEVWQVANSYHTKPYRRLMMQTWGAKVHPSPSDLTEAGRRILESDPSSPGSLGIAISEAVEVAARNEDTKYCLGSVLNHVLLHQTIIGEECIQQMENFGETPDLIIGCTGGGSNFAGLSFPFIREKLKGKINPVIRAVEPSACPSLTKGVYAYDFGDTAGLTPLMKMHTLGHDFIPDPIHAGGLRYHGMAPLISHVYEQGFMEAISIPQIECFQGAIQFARTEGIIPAPEPTHAIAATIREALRCKETGEAKVILMAMCGHGHFDLTSYDKYLKGELVDLSFSEEKIRESLSKVPHVV
Protein: ADP-ribosylation factor-like protein 2 (Q9D0J4)
Organism: Mus musculus (Mouse)
Function: Small GTP-binding protein which cycles between an inactive GDP-bound and an active GTP-bound form, and the rate of cycling is regulated by guanine nucleotide exchange factors (GEF) and GTPase-activating proteins (GAP). GTP-binding protein that does not act as an allosteric activator of the cholera toxin catalytic subunit. Regulates formation of new microtubules and centrosome integrity. Prevents the TBCD-induced microtubule destruction. Participates in association with TBCD, in the disassembly of the apical junction complexes. Antagonizes the effect of TBCD on epithelial cell detachment and tight and adherens junctions disassembly. Together with ARL2, plays a role in the nuclear translocation, retention and transcriptional activity of STAT3. Component of a regulated secretory pathway involved in Ca(2+)-dependent release of acetylcholine. Required for normal progress through the cell cycle.
Subcellular location: Mitochondrion intermembrane space. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Nucleus. Cytoplasm. Note=The complex formed with ARL2BP, ARL2 and SLC25A6 is expressed in mitochondria. Not detected in the Golgi, nucleus and on the mitotic spindle. Centrosome-associated throughout the cell cycle. Not detected to interphase microtubules (By similarity). The complex formed with ARL2BP, ARL2 and SLC25A4 is expressed in mitochondria. {ECO:0000250}.
Interaction partners:
- ADP-ribosylation factor-like protein 2-binding protein
- Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta
- Tubulin-specific chaperone D
- Protein unc-119 homolog A
- Protein unc-119 homolog B
- Tubulin-specific chaperone E
- Tubulin-folding cofactor B
Sequence:
MGLLTILKKMKQKERELRLLMLGLDNAGKTTILKKFNGEDVDTISPTLGFNIKTLEHRGFKLNIWDVGGQKSLRSYWRNYFESTDGLIWVVDSADRQRMQDCQRELQSLLVEERLAGATLLIFANKQDLPGALSCNAIQEALELDSIRSHHWRIQGCSAVTGEDLLPGIDWLLDDISSRVFTAD
Protein: Proprotein convertase subtilisin/kexin type 1 inhibitor, like precursor (Proprotein convertase subtilisin/kexin type 1 inhibitor,-like) (F1QCH5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Pleckstrin and Sec7 domain-containing 3,-like.
- Membrane-spanning 4-domains subfamily A member 4A
- Ependymin-like 1
- O-acyltransferase-like.
- C-type natriuretic peptide-like isoform X1
- Carboxypeptidase A6
- DNA
- Ubiquitin carboxyl-terminal hydrolase 7
- DNA ligase
- Palmdelphin b.
Sequence:
MSGLLSSSLLFFLSLTLFQIHTPEAKPLSAMRGGVRSYDVPVRLRRELRDSVPYEAQMISYPSADFKSRSNDYYPSEVLRAQGLGQALQRLVESDQRREQEAAYLASMLRLLNEAQGTGQGRAGDQEEEGGDFQGPYPPDYDETEQAVSMAKPQASWQGLLDPQLTQALLNRYKQERLVQAGLAPAANRIPEREQDKDQEMLRYLVEKILSSLASGGNQGSSSNPRAKRDLSAVSSIERPIKPALKRSRRSLDSAPGPQAEASLLRVKRLDDDDDVDEDAVAGQSNGTPHIGLQRMKRIDTDLPPPKKHSRKRRALSYDPALIAQHILQYLPA
Protein: tRNA-dihydrouridine(20a/20b) synthase [NAD(P)+] (EC 1.3.1.90) (mRNA-dihydrouridine synthase dus4) (EC 1.3.1.-) (tRNA-dihydrouridine synthase 4) (O74553)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs. Also able to mediate dihydrouridylation of some mRNAs, thereby affecting their translation.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- 18S rRNA aminocarboxypropyltransferase
- Putative tRNA pseudouridine synthase C16C4.06c
- tRNA
- tRNA
Sequence:
MRDRLKDPVKIFEINKGKRPVHIAAPMVRYSKLPFRQLVRDYNTDIVYTPMILAKEFLHPKGRYFDFSTNDADASLILQFGVDDPVILEKAAQLVGPYVDGIGINCGCPQTWAIQEGIGSALLDEPEKVHKLVRAVKSTLGESFCTEVKIRIAKDLNKTRHLMQVIEKSGADIITVHGRTRQDRSSFPVNLDAIREVRPCVQIPVVANGDVKSLRKGLEIAKYTETQGIMSARGLLENPALFAGYEETPWGCVERFLWYSTSYSLNFHLFYHHLTTMMGQMTTKRERMTIPKDSFASVMDWLDEHFVVRRPDEPMFGESVLPCRRY
Protein: Otolin-1-A (zOtolin1) (A5PN28)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Collagen-like protein, which provides an organic scaffold for otoliths onto the sensory epithelium of the inner ear. Acts as a scaffold for biomineralization by sequestering calcium.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q4ZJM7}. Note=Localized in both the surrounding otoconial matrix and otoconia. {ECO:0000250|UniProtKB:Q4ZJM7}.
Interaction partners:
- Otoconin 90.
- Otolith matrix protein 1
- Otopetrin 1.
- SPARC-like 2
- Growth/differentiation factor 10
Sequence:
MPNILHPFIIIMTLLVVATGNQASIDKTTQWPRMKPTKKPPPRDEGPSKLGSISTTVSPTAIGITEEVTDAMMDAYTITSTGSTTFSSDTYSADYHTEAMVPPGVGPGNYTLDYNECFFNFCECCPPERGPPGPVGEKGLPGIPGGKGEMGPPGPPGQEGLTGAPGTHGVKGEKGDTGASGLPGIPGVTGKQGEKGESGPKGDKGDTGFPGLKGDPGERGEPGWNGTKGGMGEPGKQGLTGPPGPDGIKGEKGDKGDCPFGEKGQKGSIGEPGPQGPKGDPGVPGTNGTDGLPGSKGPKGDPGPLSKQGEPGPPGPQGPPGQRGMPGMKGTRGLKGARGIRGFKGFKGEPAVQKRSAFSVGLFPSRSFPPPGLPIRFDKIIYNEEAHWDPNASKFNCTHGGVYVFSYYITVRNRPLRAALVVNGIRKLRTRDSLYGQDIDQASNMAVLRLSSGDQVWLETLRDWNGVYSSSEDDSTFSGFLLYADATKD
Protein: Aldehyde dehydrogenase family 3 member B1 (EC 1.2.1.28) (EC 1.2.1.5) (EC 1.2.1.7) (Aldehyde dehydrogenase 7) (Long-chain fatty aldehyde dehydrogenase) (EC 1.2.1.48) (Medium-chain fatty aldehyde dehydrogenase) (Q80VQ0)
Organism: Mus musculus (Mouse)
Function: Oxidizes medium and long chain saturated and unsaturated aldehydes. Metabolizes also benzaldehyde (By similarity). Low activity towards acetaldehyde and 3,4-dihydroxyphenylacetaldehyde (By similarity). May not metabolize short chain aldehydes. Can use both NADP(+) and NAD(+) as electron acceptor (By similarity). May have a protective role against the cytotoxicity induced by lipid peroxidation (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:25286108}; Lipid-anchor {ECO:0000269|PubMed:25286108}. Note=Primarily in the plasma membrane as well as in some punctate structures in the cytoplasm. {ECO:0000269|PubMed:25286108}.
Interaction partners:
- All-trans-retinol dehydrogenase [NAD
- All-trans-retinol dehydrogenase [NAD
- Aldo-keto reductase family 1 member A1
- Alcohol dehydrogenase class-3
- Acetyl-coenzyme A synthetase 2-like, mitochondrial
- Acetyl-coenzyme A synthetase, cytoplasmic
- 4-aminobutyrate aminotransferase, mitochondrial
- Alcohol dehydrogenase 1
- Cytochrome P450 2E1
- Amine oxidase [flavin-containing] A
Sequence:
MDSFEDKLQQLREAFKEGRTRSAEFRAAQLQGLSHFLRDNKQQLQEALAQDLHKSAFEAEVSEIAISQAEVDLALRNLRSWMKDEKVSKNLATQLDSAFIRKEPFGLVLIIVPWNYPINLTLVPLVGAIAAGNCVVLKPSEISKATEKILAEVLPRYLDQSCFTVVLGGRQETGQLLEHKFDYIFFTGNAYVGKIVMAAAAKHLTPITLELGGKNPCYVDDNCDPQIVANRVAWFRYFNAGQTCVAPDYILCSQEMQERLVPALQNAITRFYGDNPQTSPNLGRIINQKHFKRLQGLLGCGRVAIGGQSDEGERYIAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNRREKPLALYAFSKRSQVIKQVLARTSSGGFCGNDGFMHMTLSSLPFGGVGTSGMGRYHGKFSFDTFSNQRACLLRSPGMEKINDLRYPPYSSRNLRVLLVAMEERCCSCTLL