wanglab/gogpt-training-data huggingface dataset:
Protein: Oxidation resistance protein 1 (B7Z0T3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
MSRENSPRHGSFRRTLNSRDPSAGAPGSGSGSGPGSPHHQQSNHQHYQHHHHHHHHHQPPIMEHAGAPISTSASNIATVLEDGENQQLPPLTGSGPSRQRSLRDRLKDGITGSFSWQSKSRSVDHGLAAPFDLDSLRSKVEQRFESVDKLSRQKSSLPTIPTISYTVGNRDTLTSVAARFDTTPSELTHLNRLNSSFIYPGQQLLVPDKSAKDDASSSSTHDADGASLSGKSSPVERKLSGDESREKDILEGLRPGSPKPGHIERVGGSSQQQQAEEEANKSDDPVITQRFLKINVRHITDGQGVVGGVLLVTPNAVMFDPNVSDPLVIEHGPESYGVIAPMELVVNAAIFHDIAHMRVAGGAGQGLNSASGDAEKPEIYYPKPVLVEEDSKELPEQQSLLGEDGNKRLDAEIGSLEIADDQESLCSSTGRDGDAFPKAFDRERVEDSSMEAKDSAKTDALDDEDKKAGLGLSSTRSTLEERRKSLLDHHWAIPSKDRSSEDEGDNESNVTVDSGARVQDPHSANSSVSGVPLSQPPVAAAAAAAAVAPASAVVPLPPSGIDLEHLEQLSKQSCYDSGIDIREPVPNVQPIPKKTVYSDADIVLSSDWVPPKTIVPTHFSESPPRSTILGQSLDAGTGGAGGVRKKTSSVSFSVDDEAAQQAQAQSAALAVTDKQADKKNKMLKRLSYPLTWVEGLTGEGGAVPPGGVGSGSLNKSGDTDSAPNTGDSNQSVFSKVFSRRSSIGTFIRPHSSEGTSSSTKLKEAKQAPKLDYRSMVSMDDKPELFISVDKLIPRPARACLDPPLYLRLRMGKPIGKAIPLPTSVMSYGKNKLRAEYWFSVPKNRVDELYRFINTWVKHLYGELDEEQIKARGFELIQEDTEWTKSGTTKAGMGGGSQDGEEISDLTRESWEVLSMSTDEYRKTSLFATGSFDLDFPIPDLIGKTEILTEEHREKLCSHLPARAEGYSWSLIFSTSQHGFALNSLYRKMARLESPVLIVIEDTEHNVFGALTSCSLHVSDHFYGTGESLLYKFNPSFKVFHWTGENMYFIKGNMESLSIGAGDGRFGLWLDGDLNQGRSQQCSTYGNEPLAPQEDFVIKTLECWAFV
Protein: U2 snRNP component IST3 (Increased sodium tolerance protein 3) (U2 snRNP protein SNU17) (P40565)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for pre-mRNA splicing and spliceosome assembly. As part of the pre-mRNA retention and splicing (RES) complex, required for nuclear pre-mRNA retention and efficient splicing. Required for MER1-activated splicing.
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- U2 snRNP component HSH155
- Pre-mRNA-splicing factor CEF1
- Pre-mRNA-splicing factor RDS3
- Pre-mRNA-splicing factor RSE1
- Pre-mRNA-splicing helicase BRR2
- Pre-mRNA-splicing factor CWC26
- Pre-mRNA leakage protein 1
- Pre-mRNA-processing factor 19
- Cold sensitive U2 snRNA suppressor 1
- Pre-mRNA-splicing factor CWC2
Sequence:
MNKIQQINDKELQSGILSPHQSWHNEYKDNAYIYIGNLNRELTEGDILTVFSEYGVPVDVILSRDENTGESQGFAYLKYEDQRSTILAVDNLNGFKIGGRALKIDHTFYRPKRSLQKYYEAVKEELDRDIVSKNNAEKLILAKKDQPN
Protein: Protein disulfide-isomerase A3 (EC 5.3.4.1) (Endoplasmic reticulum resident protein 57) (ER protein 57) (ERp57) (Endoplasmic reticulum resident protein 60) (ER protein 60) (ERp60) (Q4VIT4)
Organism: Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops)
Function: Disulfide isomerase which catalyzes the formation, isomerization, and reduction or oxidation of disulfide bonds (By similarity). Associates with calcitriol, the active form of vitamin D3 which mediates the action of this vitamin on cells (By similarity). Association with calcitriol does not affect its enzymatic activity (By similarity).
Subcellular location: Endoplasmic reticulum {ECO:0000250|UniProtKB:P30101}. Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:P11598}. Melanosome {ECO:0000250|UniProtKB:P30101}.
Interaction partners:
Sequence:
MRLRRLALFPGVALLLAAARLAAASDVLELTDDNFESRVSDTGSAGLMLVEFFAPWCGHCKRLAPEYEAAATRLKGIVPLAKVDCTANTNTCNKYGVSGYPTLKIFRDGEEAGAYDGPRTADGIVSHLKKQAGPASVPLRTEEEFKKFISDKDASVVGFFDDLFSEAHSEFLKAASNLRDNYRFAHTNVKSLVNEYDDNGEGIILFRPSHLTNKFEDKTVAYTEQKMTSGKIKKFIQENIFGICPHMTEDNKDLIQGKDLLIAYYDVDYEKNAKGSNYWRNRVMMVAKKFLDAGHKLNFAVASRKTFSHELSDFGLESTAGEIPVVAIRTAKGEKFVMQEEFSRDGKALERFLQDYFDGNLKRYLKSEPIPESNDGPVKVVVAENFDEIVNNENKDVLIEFYAPWCGHCKNLEPKYKELGEKLSKDPNIVIAKMDATANDVPSPYEVRGFPTIYFSPANKKLNPKKYEGGRELSDFISYLQREATNPPVIQEEKPKKKKKAQEDL
Protein: Delayed-rectifier potassium channel regulatory subunit KCNS1 (Delayed-rectifier K(+) channel alpha subunit 1) (Delayed-rectifier potassium channel subunit Kv9.1) (Potassium voltage-gated channel modifier subfamily S member 1) (O35173)
Organism: Mus musculus (Mouse)
Function: Potassium channel subunit that does not form functional channels by itself. Can form functional heterotetrameric channels with KCNB1 and KCNB2; modulates the delayed rectifier voltage-gated potassium channel activation and deactivation rates of KCNB1 and KCNB2.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q96KK3}; Multi-pass membrane protein {ECO:0000305}. Note=May not reach the plasma membrane but remain in an intracellular compartment in the absence of KCNB1 or KCNB2 (PubMed:9305895). {ECO:0000269|PubMed:9305895}.
Interaction partners:
- Ubiquitin-like protein FUBI
- Potassium voltage-gated channel subfamily B member 1
- Delayed-rectifier potassium channel regulatory subunit KCNS2
- Voltage-gated potassium channel subunit beta-2
- Voltage-gated potassium channel subunit beta-1
Sequence:
MVSEFPGPGSRVPWRPRDEALRVNVGGVRRLLSARALARFPGTRLGRLQAAASEEQARRLCDDYDAAAHEFYFDRHPGFFLGLLHFYRTGHLHVLDELCVFAFGQEADYWGLGENALATCCRARYLERRVARPRAWDEDSDAPSSVDPCPDEISDVQRELARYGAARCGRLRRRLWLTMENPGYSLPSKLFSCVSIGVVLASIAAMCIHSLPEYQAREAAAAVAAVAAGRSAEEVRDDPVLRRLEYFCIAWFSFEVSSRLLLAPSTRNFFCHPLNLIDIVSVLPFYLTLLAGAALGDQRGASGEELGDLGKVVQVFRLMRIFRVLKLARHSTGLRSLGATLKHSYREVGILLLYLAVGVSVFSGVAYTAEEENEGFHTIPACWWWGTVSMTTVGYGDVVPETVGGKLAASGCILGGILVVALPITIIFNKFSHFYRRQKALEAAVRSSGQREFEDLLSSVDGVSDVSLETSRDTSQEGRSTDLETQAPREPAKSHSY
Protein: Protein CHROMATIN REMODELING 4 (AtCHR4) (EC 3.6.4.-) (Protein PICKLE RELATED 1) (F4KBP5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Chromatin-remodeling protein that binds DNA through histones and regulates gene transcription. May specifically recognize and bind trimethylated 'Lys-27' (H3K27me3) and non-methylated 'Lys-4' of histone H3 (By similarity). Probable chromatin remodeling factor.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
Interaction partners:
- High mobility group B protein 15
- High mobility group B protein 9
- High mobility group B protein 10
- Putative high mobility group B protein 11
- Chromatin structure-remodeling complex protein SYD
- WD-40 repeat-containing protein MSI4
- WD-40 repeat-containing protein MSI5
- Gb|AAF19561.1
- WD-40 repeat-containing protein MSI2
- WD-40 repeat-containing protein MSI3
Sequence:
MKDSGSEMIKRDWVMKQKRRKLPSILDILDQKVDSSMAFDSPEYTSSSKPSKQRLKTDSTPERNSSKRKGNDGNYFECVICDLGGDLLCCDSCPRTYHTACLNPPLKRIPNGKWICPKCSPNSEALKPVNRLDAIAKRARTKTKKRNSKAGPKCERASQIYCSSIISGEQSSEKGKSISAEESKSTGKEVYSSPMDGCSTAELGHASADDRPDSSSHGEDDLGKPVIPTADLPSDAGLTLLSCEDLSESKLSDTEKTHEAPVEKLEHASSEIVENKTVAEMETGKGKRKKRKRELNDGESLERCKTDKKRAKKSLSKVGSSSQTTKSPESSKKKKKKNRVTLKSLSKPQSKTETPEKVKKLPKEERRAVRATNKSSSCLEDTNSLPVGNLQVHRVLGCRIQGLTKTSLCSALSDDLCSDNLQATDQRDSLVQDTNAELVVAEDRIDSSSETGKSSRDSRLRDKDMDDSALGTEGMVEVKEEMLSEDISNATLSRHVDDEDMKVSETHVSVERELLEEAHQETGEKSTVADEEIEEPVAAKTSDLIGETVSYEFLVKWVDKSNIHNTWISEAELKGLAKRKLENYKAKYGTAVINICEDKWKQPQRIVALRVSKEGNQEAYVKWTGLAYDECTWESLEEPILKHSSHLIDLFHQYEQKTLERNSKGNPTRERGEVVTLTEQPQELRGGALFAHQLEALNWLRRCWHKSKNVILADEMGLGKTVSASAFLSSLYFEFGVARPCLVLVPLSTMPNWLSEFSLWAPLLNVVEYHGSAKGRAIIRDYEWHAKNSTGTTKKPTSYKFNVLLTTYEMVLADSSHLRGVPWEVLVVDEGHRLKNSESKLFSLLNTFSFQHRVLLTGTPLQNNIGEMYNLLNFLQPSSFPSLSSFEERFHDLTSAEKVEELKKLVAPHMLRRLKKDAMQNIPPKTERMVPVELTSIQAEYYRAMLTKNYQILRNIGKGVAQQSMLNIVMQLRKVCNHPYLIPGTEPESGSLEFLHDMRIKASAKLTLLHSMLKVLHKEGHRVLIFSQMTKLLDILEDYLNIEFGPKTFERVDGSVAVADRQAAIARFNQDKNRFVFLLSTRACGLGINLATADTVIIYDSDFNPHADIQAMNRAHRIGQSKRLLVYRLVVRASVEERILQLAKKKLMLDQLFVNKSGSQKEFEDILRWGTEELFNDSAGENKKDTAESNGNLDVIMDLESKSRKKGGGLGDVYQDKCTEGNGKIVWDDIAIMKLLDRSNLQSASTDAADTELDNDMLGSVKPVEWNEETAEEQVGAESPALVTDDTGEPSSERKDDDVVNFTEENEWDRLLRMRWEKYQSEEEAALGRGKRLRKAVSYREAYAPHTSGPVNESGGEDEKEPEPELKKEYTPAGRALKEKFTKLRERQKNLIARRNSVEESLPSGNVDQVTEVANQDEESPTSMDLDDSKASQQCDAQKRKASSSDPKPDLLSQHHHGAECLPSLPPNNLPVLGLCAPNFTQSESSRRNYSRPGSRQNRPITGPHFPFNLPQTSNLVEREANDQEPPMGKLKPQNIKEEPFQQPLSNMDGWLPHRQFPPSGDFERPRSSGAAFADFQEKFPLLNLPFDDKLLPRFPFQPRTMGTSHQDIMANLSMRKRFEGTGHSMQDLFGGTPMPFLPNMKIPPMDPPVFNQQEKDLPPLGLDQFPSALSSIPENHRKVLENIMLRTGSGIGHVQKKKTRVDAWSEDELDSLWIGIRRHGYGNWETILRDPRLKFSKFKTPEYLAARWEEEQRKFLDSLSSLPSKSSRTDKSTKSSLFPGLPQGIMNRALHGKYATPPRFQSHLTDIKLGFGDLASPLPLFEPSDHLGFRSEHFPPMANLCTDNLPGEPSAGPSERAGTSTNIPNEKPFPLNSLGMGNLGSLGLDSLSSLNTLRAEEKRDAIKRGKLPLFLDMPLPQMLDSSNNVFLGRSANPSFLHPNRGLNPSNPMGRDIMGISSSENKLPHWLRNVVTVPTVKSPEPPTLPPTVSAIAQSVRVLYGEDSTTIPPFVIPEPPPPAPRDPRHSLRKKRKRKLHSSSQKTTDIGSSSHNAVESSSQGNPQTSATPPLPPPSLAGETSGSSQPKLPPHNLNSTEPLSSEAIIIPPPEEDSVIAAAPSEAPGPSLEGITGTTKSISLESQSSEPETINQDGDLDPETDEKVESERTPLHSDEKQEEQESENALNKQCEPIEAESQNTNAEEEAEAQEEDEESMKMVTGNSLSDD
Protein: GBF-interacting protein 1 (Q8VZS6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plant specific protein that enhances G-box-binding factor (GBF) DNA binding activity. May function as a nuclear chaperone or lever and regulate the multimeric state of GBFs. May contribute to bZIP-mediated gene regulation. Is able to refold denatured rhodanese in vitro. Reduces DNA-binding activity of BZIP16, BZIP68 and GBF1 under non-reducing conditions through direct physical interaction. Acts as negative co-regulator in red and blue light-mediated hypocotyl elongation. Functions to promote hypocotyl elongation during the early stages of seedling development by regulating the repression effect by BZIP16 and the activation effect by BZIP68 and GBF1 on LHCB2.4 expression. Enhances transcriptional activity of LBD18 in the EXP14 promoter. May act as a transcriptional coactivator of LBD18.
Subcellular location: Nucleus {ECO:0000269|PubMed:16117846, ECO:0000269|PubMed:24484953, ECO:0000269|PubMed:25387999}.
Interaction partners:
- Expansin-A14
- LOB domain-containing protein 18
Sequence:
MSRISGDGGSRVSIPADLLQTIQNIREVTGKQHSDEDIFSVFKECFSDPHETTQKLLYLDTFHEVRSKRERKKENLVPNTQGRGRTGRKNFASSYTDASNGRSAAFKKQSGANHIIGGSGTASSAPNNARNDTKPSSIMAPNPISLPSGISNQKIQDAIISPVDKVDTEEQPLSKATSSSKDVVEPDKSKESSVSVAVSDSVVENDTQYAVVETFQIPQQSERVIKSEVAASKCKNESLLKSDVGERPHVTFPVHIQVAKMLENGLTFGSFDSNFVREASSDKFTIGCDDSNIESSHGTAASARKDISTFSQDKNHEISNSAAQNELTLQPDQTVLPEEGSEGDKVKNEVLPITDTHQAAKCDAPPISYPDQYSLAAAQQAMHLYRQQYSLNYFPYGPYFPPYYMPQPYIHQYLSPNGFQQQSYLPPGDDAPAPPGAELPLTHIKPGSDIGNSPPTTIPFSYTSYAFNHIPSAATINATHKEEKKENMYTTGPLSLANLQASPMYNLSLQGQPIAFPTMQAGIRGLYQQTQPILAPLSISARTEPIGPSHVTNQQPQAARTNLGNNY
Protein: Cyclic nucleotide-gated channel alpha-4 (CNG channel alpha-4) (CNGa4) (Olfactory cyclic nucleotide-gated channel subunit 2) (OCNC2) (Q8IV77)
Organism: Homo sapiens (Human)
Function: Second messenger, cAMP, causes the opening of cation-selective cyclic nucleotide-gated (CNG) channels and depolarization of the neuron (olfactory sensory neurons, OSNs). CNGA4 is the modulatory subunit of this channel which is known to play a central role in the transduction of odorant signals and subsequent adaptation. By accelerating the calcium-mediated negative feedback in olfactory signaling it allows rapid adaptation to odor stimulation and extends its range of odor detection (By similarity).
Subcellular location: Cell projection, cilium membrane {ECO:0000250|UniProtKB:Q64359}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cyclic nucleotide-gated channel beta-1
- Cyclic nucleotide-gated channel alpha-2
- Calmodulin-1
- Calmodulin-like protein 4
- Calmodulin-like protein 3
- Calmodulin-like protein 6
- Calmodulin-like protein 5
- Cyclic nucleotide-gated channel beta-3
- Adenylate cyclase type 3
- Anoctamin-2
Sequence:
MSQDTKVKTTESSPPAPSKARKLLPVLDPSGDYYYWWLNTMVFPVMYNLIILVCRACFPDLQHGYLVAWLVLDYTSDLLYLLDMVVRFHTGFLEQGILVVDKGRISSRYVRTWSFFLDLASLMPTDVVYVRLGPHTPTLRLNRFLRAPRLFEAFDRTETRTAYPNAFRIAKLMLYIFVVIHWNSCLYFALSRYLGFGRDAWVYPDPAQPGFERLRRQYLYSFYFSTLILTTVGDTPPPAREEEYLFMVGDFLLAVMGFATIMGSMSSVIYNMNTADAAFYPDHALVKKYMKLQHVNRKLERRVIDWYQHLQINKKMTNEVAILQHLPERLRAEVAVSVHLSTLSRVQIFQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGQEMYIIREGQLAVVADDGITQYAVLGAGLYFGEISIINIKGNMSGNRRTANIKSLGYSDLFCLSKEDLREVLSEYPQAQTIMEEKGREILLKMNKLDVNAEAAEIALQEATESRLRGLDQQLDDLQTKFARLLAELESSALKIAYRIERLEWQTREWPMPEDLAEADDEGEPEEGTSKDEEGRASQEGPPGPE
Protein: GRAM domain-containing protein 4 (Death-inducing protein) (Q8CB44)
Organism: Mus musculus (Mouse)
Function: Plays a role as a mediator of E2F1-induced apoptosis in the absence of p53/TP53 (By similarity). Inhibits TLR9 response to nucelic acids and regulates TLR9-mediated innate immune response.
Subcellular location: Mitochondrion membrane {ECO:0000250|UniProtKB:Q6IC98}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:25917084}; Multi-pass membrane protein {ECO:0000255}. Note=Colocalizes with COX4I1. {ECO:0000250}.
Interaction partners:
Sequence:
MGIASHSAFRERESSPTGASLDASPRPWDKGLSGREPPRHVQVRPRSAVLNMLRRLDRIRFRGHKREDLLDLAESPNASDTECGDEIPLKTPRPSPRDSEELRDPAGPGTLIMAAGVQDFNRTEFDRLNEIKGHLEIALLEKHFLQEELRKLREETNSEMLRQELDRERQRRIELEQKMQEVLKARSEEQPAQPQQPPKGQSQASNGTGTERRSQGLASRVQKWFYERFGEYIEDFRFQPEENTVETEEPLSARRLTENMRRLKRGAKPVTNFVKNLSALSDWYSIYTSAIAFTVYMNAVWHGWAIPMFLFLAILRLSLNYLIARGWRIQWSIVPEVSEAVEPAKEDLTVSEKFQLVLDVAQKAQNLFGKMADILEKIKNLFMWVQPETTQKLYVALWAAFLASCFFPYRLVGLAVGLYAGIKFFLIDFIFKRCPRLRAKYDTPYIIWRSLPTDPQLKERAGATVSRRLQTASSRSYVSSAPAGLSKDEDAGRFHSTKKGNFHEIFNLTENERPLAVCENGWRCCLINRDRKMPTDYIRNGVLYVTENYLCFESSKSGSSKRNKVIKLMDITDIQKYKVLSVLPGSGMGIAVSTPSTQKPLVFGAMVHRDEAFETIFSQYVKITSAAASGGDS
Protein: Uronate dehydrogenase (EC 1.1.1.203) (D-galacturonate dehydrogenase) (D-glucuronate dehydrogenase) (Hexuronate dehydrogenase) (Q7CRQ0)
Organism: Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens (strain C58))
Function: Catalyzes the oxidation of D-galacturonate and D-glucuronate to galactarate and D-glucarate, respectively. In fact, in water solution the substrate D-galacturonate is predominantly in pyranosic form whose beta anomer is converted by the enzyme to D-galactaro-1,5-lactone; in solution, this reaction product rearranges to the more stable D-galactaro-1,4-lactone. Makes part of the oxidative degradation pathway of D-galacturonate, which allows A.tumefaciens to utilize D-galacturonate as a sole carbon source. Cannot use NADP(+) instead of NAD(+) as cosubstrate. Is not active on D-galactose, D-glucose, D-galactonate and D-gluconate.
Interaction partners:
- D-galactarolactone isomerase
- NAD-dependent epimerase/dehydratase domain-containing protein
- Probable 5-dehydro-4-deoxyglucarate dehydratase
- D-galactarolactone cycloisomerase
Sequence:
MKRLLVTGAAGQLGRVMRERLAPMAEILRLADLSPLDPAGPNEECVQCDLADANAVNAMVAGCDGIVHLGGISVEKPFEQILQGNIIGLYNLYEAARAHGQPRIVFASSNHTIGYYPQTERLGPDVPARPDGLYGVSKCFGENLARMYFDKFGQETALVRIGSCTPEPNNYRMLSTWFSHDDFVSLIEAVFRAPVLGCPVVWGASANDAGWWDNSHLGFLGWKPKDNAEAFRRHITETTPPPDPNDALVRFQGGTFVDNPIFKQS
Protein: Dipeptidase 1 (EC 3.4.13.19) (Beta-lactamase) (EC 3.5.2.6) (Microsomal dipeptidase) (Renal dipeptidase) (P22412)
Organism: Sus scrofa (Pig)
Function: Hydrolyzes a wide range of dipeptides. Hydrolyzes the conversion of leukotriene D4 to leukotriene E4. Hydrolyzes cystinyl-bis-glycine (cys-bis-gly) formed during glutathione degradation. Possesses also beta lactamase activity and hydrolytically inactivates beta-lactam antibiotics (By similarity).
Subcellular location: Apical cell membrane; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:16689534}. Cell projection, microvillus membrane; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:16689534}. Cell membrane {ECO:0000269|PubMed:8045301}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:8045301}. Note=Brush border membrane. {ECO:0000250|UniProtKB:P31429}.
Interaction partners:
Sequence:
MWTSWWLWPLVAVCAADQFRDLAVRIMQDTPVIDGHNDLPWQLLNLFNNQLQDPGANLSSLAHTHTNIPKLKAGFVGGQFWSAYVPCDTQNRDAVKRTLEQIDVIQRMCQAYPETFACVTSSTGIRQAFREGKVASLVGVEGGHSIDSSLGVLRALYHLGMRYMTLTHSCNTPWADNWLVDTGDDKAQSQGLSHFGQSVVKEMNRLGVMIDLAHVSVATMRAALKLSQAPVIFSHSSAYSLCPHRRNVPDDVLQLVKETGSLVMVNFYNDYVSCSAKANLSQVADHLDHIKKVAGAAAVGFGGDYDGVSRVPSGLEDVSKYPDLVAELLRRQWTEAEVRGALADNLLRVFEAVEQASNHAQVPGEEPIPLGQLEASCRTNYGYSAAPSLHLPPGSLLASLVPLLLLSLP
Protein: Leucine-rich repeat-containing protein 10 (Serdin1) (Q5U8X4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MGNVVRGAIAFVPSERCQRFLVGDLKEMPLDRTLDLSSRQLRRFPVRASAFDELVKLYLSDNHLSNLPLELRNLQKLQLLALDFNCFEELPLVICSLVQLNILYFGNNRLYSLPKELQQLTELKTLWLETNCFTSFPQVICELPNIKTLHLGYNQLRSLPAELGRLEELRSIWLAGNLLNDFPPVLLEMHYLEVMDVDRNRICQFPSLTHLRGLKLVIYDHNPCINAPVVAEGVRRVGRWADCSDDEEEEGDGKVANASAKAAVNTGSE
Protein: Protein adenylyltransferase Fic (dFic) (EC 2.7.7.108) (De-AMPylase Fic) (EC 3.1.4.-) (Q8SWV6)
Organism: Drosophila melanogaster (Fruit fly)
Function: Protein that can both mediate the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context. The side chain of Glu-247 determines which of the two opposing activities (AMPylase or de-AMPylase) will take place (By similarity). Acts as a key regulator of the unfolded protein response (UPR) by mediating AMPylation or de-AMPylation of Hsc70-3/BiP. In unstressed cells, acts as an adenylyltransferase by mediating AMPylation of Hsc70-3/BiP at 'Thr-518', thereby inactivating it. In response to endoplasmic reticulum stress, acts as a phosphodiesterase by mediating removal of ATP (de-AMPylation) from Hsc70-3/BiP at 'Thr-518', leading to restore HSPA5/BiP activity.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Endoplasmic reticulum chaperone BiP
Sequence:
MGTEAEQPSPPAQQQDQENPPLCKAQNPKPARLYRFVLIFVAGSLAAWTFHALSSTNLVWKLRQLHHLPTAHYLQTRDEFALYSVEELNAFKEFYDKSVSDSVGASYTEAEQTNIKEALGALRMAQDLYLAGKDDKAARLFEHALALAPRHPEVLLRYGEFLEHNQRNIVLADQYYFQALTISPSNSEALANRQRTADVVQSLDERRLESLDSKRDALSAIHESNGALRRAKKEAYFQHIYHSVGIEGNTMTLAQTRSILETRMAVDGKSIDEHNEILGMDLAMKYINASLVQKIDITIKDILELHRRVLGHVDPIEGGEFRRNQVYVGGHIPPGPGDLALLMQRFERWLNSEHSSTLHPVNYAALAHYKLVHIHPFVDGNGRTSRLLMNTLLMRAGYPPVIIPKQQRSKYYHFLKLANEGDIRPFVRFIADCTEKTLDLYLWATSDLPQQIPMLIQTESEAGERLAQMQSPNVAQRSSILEFYESGSGDLP
Protein: E3 ubiquitin-protein ligase RNF170 (EC 2.3.2.27) (RING finger protein 170) (RING-type E3 ubiquitin transferase RNF170) (Q7SZN2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: E3 ubiquitin-protein ligase that plays an essential role in stimulus-induced inositol 1,4,5-trisphosphate receptor (ITPR) ubiquitination and degradation via the endoplasmic reticulum-associated degradation (ERAD) pathway. Also involved in ITPR turnover in resting cells.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q96K19}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q96K19}.
Interaction partners:
- Erlin-1
- Erlin-2.
- Erlin-2
Sequence:
MEGSVCVDGAAAPAPDEASLIEGVSNAVLLVLVLSVTLLAGLTTLLCRSEQQRIHPESQERVRVVREQLQAEQVSSESRHQFYSDMSCPVCLQQAVLPVETNCGHLFCGSCIIAYWRYGTWLGAISCPICRQMVTLLFPLFQDSEQSAVAADSPVEPTLILTDISDYNRRFSGQPRSLLDRLRDVPTLLRHAFREMFSVGGLFWMFRVRILLCVCGALAYLVSPLDFLPEGVLGLLGFLDDFFVILLLFIYISIMYREVVTQRLAG
Protein: Embryonic polyadenylate-binding protein 2-B (Embryonic poly(A)-binding protein 2-B) (XePABP2-B) (ePABP-2B) (ePABP2-B) (Embryonic poly(A)-binding protein type II-B) (Q6TY21)
Organism: Xenopus laevis (African clawed frog)
Function: Binds the poly(A) tail of mRNA. Unable to interact with the cap-binding complex and is therefore unlikely to be involved in translation initiation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15083517}.
Interaction partners:
Sequence:
MSERVSEEPGLDKGDRAEECELDDPELKAIRMRVREMEEEAERLKGLSGQDKSIGVSTRPCMQTTHSKMTAGAYTEGPPQPLSAEEKKEIDKRSVYVGNVDYGSTAQDLEAHFSSCGSINRITILCDKFSGHPKGYAYIEFAERNSVDAAVAMDETVFRGRTIKVLPKRTNMPGISSTDRGGFRGRPRGNRGNYQRGQRPRGRPFRGRGRPGPLNNPY
Protein: PipX (Q7X386)
Organism: Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805) (Anacystis nidulans R2)
Interaction partners:
- Nitrogen regulatory protein P-II
- Global nitrogen regulator
- Pyridoxal phosphate homeostasis protein
- Acetylglutamate kinase
- DNA-directed RNA polymerase subunit omega
- DUF4335 domain-containing protein
- Cell division protein SepF
- 2TM domain-containing protein
- DUF3155 domain-containing protein
- DUF3493 domain-containing protein
Sequence:
MASENYLNHPTFGLLYQICSFGDSKELFATLYAQRLFFLVAFDARGTRFEPIGRNEARMLVDNRLRQLRRDASLQEYNQLQQVFKQTFL
Protein: Protein DGS1, mitochondrial (Protein DGD1 SUPPRESSOR 1) (Q8GUK1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in galactoglycerolipid biosynthesis. Contributes to an intracellular signal that regulates an alternative DGD1-independent galactoglycerolipid biosynthesis pathway in chloroplasts. Being involved in mitochondrial lipid homeostasis, modulates mitochondrion biogenesis and physiology, as well as stress responses.
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:18208519, ECO:0000269|PubMed:31118221}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- AT5g19430/F7K24_180
- Pentatricopeptide repeat-containing protein At3g22690
- MICOS complex subunit MIC60, mitochondrial
- Protein RETARDED ROOT GROWTH-LIKE
- Digalactosyldiacylglycerol synthase 1, chloroplastic
- DNA damage-repair/toleration protein DRT102
- Mitochondrial import receptor subunit TOM40-1
- Receptor-like protein 14
- DNA polymerase I A, chloroplastic/mitochondrial
- Asparagine synthetase 2
Sequence:
MDSQPPVNESTPSTALSNFGELVPFYSSYLWNRLASLLPTSKPIFLGKISNLYRQTVSRKRSISFPLPLPSDFPSSSTITSNVSADTARIHGVLEEIMADVLSNLHDIQKSLDFWRSRAEGSNARKAYFMIFERGPTAFVNESTKFVSKSLSEDSAMQHLCQSSSSHMTERMRVLVELRSALASFIAQLYVELDKRGEDLVKIPEKALPSLLAVINGLFSNLEGSFSHLHAVRECDSSVDGSYPMPLVFDRLPEVNEEGSQWTDCELTDAINLVHKNLEKLNSYLSVMVGKHRKPRRMTLYWVRYTCGAVGLSVFSIWLLRHSSLMGSSDIENWVHDAKEATMSFFSDHVEQPLLSIRDELFDTFRKRHKGVMETEEVQLTQDSLHRMLRNFCEQATREKVPDNASDQEMLEVVMNRYEKELVHPIHNLLSGELARGLLIQVQKLKLDIETAMLELDQILRANEINFAILAALPAFFLSIVMLTVLRTWLKKDSKAQGRGRIARIHRRLLVVEIEKRIMQYQSYIEQGRDKDAETVFGLLIYSLERLYRVVEKPARATDEWDLVKQDLIELGRPQQQTSYKLTVTQRLVTVYDCLLPTLKRQ
Protein: Probable UDP-3-O-acyl-N-acetylglucosamine deacetylase 1, mitochondrial (UDP-3-O-acyl-GlcNAc deacetylase 1) (EC 3.5.1.108) (Protein LIPID X C1) (AtLpxC1) (UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase 1) (F4IAT8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that in bacteria anchors the lipopolysaccharide to the outer membrane of the cell. Lipid A-like molecules in plants may serve as structural components of the outer membranes of mitochondria and/or chloroplasts, or may be involved in signal transduction or plant defense responses (Potential).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:21709257, ECO:0000305|PubMed:25732537}.
Interaction partners:
- Probable UDP-3-O-acylglucosamine N-acyltransferase 1, mitochondrial
- Probable UDP-3-O-acylglucosamine N-acyltransferase 2, mitochondrial
- Probable lipid-A-disaccharide synthase, mitochondrial
- Probable tetraacyldisaccharide 4'-kinase, mitochondrial
- Probable acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase, mitochondrial
- Probable 3-deoxy-D-manno-octulosonic acid transferase, mitochondrial
- At3g27200
- Protein SET DOMAIN GROUP 40
- Inositol diphosphatase DSP5
- Is a member of the PF|00364 Biotin-requiring enzymes family
Sequence:
MRLPVTVKATKPSFLVIWIRYSSAASSPTVSLNPSGRLQQTLAGSVEVKGKSLHSGKFSTVKLNPEIAGAGRFFEFRSRFIPASIEFAQESPLCTTLLKDELKIRTVEHLLSALEAKGVDNCRIQIESESSDDREVEVPIFDGSAKEWVDAIQGVGINAAQNHDGESVEKMVAHVNKPVYVCKNDTFVAAFPALETRITCGIDFPQVPAIGCQWFSWRPIHESSFAKDIASSRTFCVYEEVERMREAGLIKGGSLDNAIVCSAEHGWMNPPLRFDDEACRHKILDLIGDLSLVSRGGNGGLPVAHIVAYKAGHALHTDLARHLTMD
Protein: Protein kinase, putative (EC 2.7.1.-) (Q583N6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Elongation initiation factor 2 alpha subunit, putative
Sequence:
MDSQSDIRHHCPAMASECSALPDASLLLVLLDGRLRCVSLKDGRERWSAQLPCGEMFSCGESGIISERRQMHPSPSDFATCKQCEVMGARYGNSSTTDRYVSVVQNPCGGCSGLSQHPFCASLPNNEVDCCLILSPRESSDVGRSPSFEWYFSGGVSGKGRDKLYFPVDVLLEHFSASRCPAHGLRDLNHRESVYIEFDFDNGVELFHLSAERGLSVPRPRRPLNDNVSSDTAVASDGNDGPQMPLCSTSQIRIAVQRATDYRTLFFPPVPRYRSGPSKGVEDNSRSLFVKKSTVIINIVGCLETNSLEGTGLDDTLRIEQTLSDSGVRVHWLAVGDNNNGPQPTVPVSPGIVESSPVVSAYVLHPHRLATGNAVTEEYCAGVTDFDDGTSYVMACCQIPILNSSSEPSKHVLSIQSCFPENFRRKRLHGFVNRQYGVFFSESLNVPSSSSSSTVSPSPLPTGSECASNDNENISNKAMGDGFFSCEESGEEANHPSPNEMSSGALVLGKSLLSFSESENVEARTQENFMSGKQSFFDENFDVLMILGSGASGVVLLTRHRVTGVLYAVKVLIVRDKFAETAVMQEVRLHAVLHNEHIVRYYTCWSEMITPARLRQLASVGLCSKREVRQTFRALEANCVSCGSSHEGAGWLIPRHEGQLGNLLLLKSPAEDCAGVYMAGDDTVDDGTGSTAGSHTEPSEDGSDDTRSNSCESSSSERSSSILEGRVVFLQLEYYRTTLAQRLGSRGSIDRFENIIIALQLFAAVRYVHRSGFLHRDVKPPNIFIDYRVQFSGVDGPGEEDNDEYDYDLDESDGNGWTCTSVREEKEERKMWTEPVNGGGNDDVSAPHQAFQSVFEFLQFYATTPPLSTYLKKIKCAQNEEQKRRAVYLIGKWTCKRFLQVRLGDFSISKSFLAQHVELASNFGRTAMNTTGIGSSLYSSPEQLDGEHCTSSSDAYSCGIVLAEMYVQPKTVSERLHVLKAVRNGVFPESSLLKRYPELCVVQYLTLKDPSHRMSLMDASRALRRTVYRILLSFFSEV