wanglab/gogpt-training-data huggingface dataset:
Protein: Nuclear speckle splicing regulatory protein 1 (Coiled-coil domain-containing protein 55) (Nuclear speckle-related protein 70) (NSrp70) (Q5NCR9)
Organism: Mus musculus (Mouse)
Function: RNA-binding protein that mediates pre-mRNA alternative splicing regulation.
Subcellular location: Nucleus {ECO:0000250}. Nucleus speckle {ECO:0000250}. Note=Colocalizes with splicing factors SRSF1 and SRSF2 in speckles. {ECO:0000250}.
Interaction partners:
- EF-hand calcium-binding domain-containing protein 5
- Pre-mRNA-splicing factor SLU7
Sequence:
MAIPGRQYGLILPKKTQPLHRVLQKPSVFGSDSDDDETSVSESLQREAAKKQAMKQTKLEIQKALAEDSTVYEYDSVYDEMQKKKEENNPKLLPGKDRKPKYIHNLLKAVEIRKKEQEKRMEKKIQREREMENGEFDDKEAFVTSAYKKKLEERAEEEEREKRAAALEAHLDVTKQKDLSGFYRHLLNQAVGEEAAPKSSFREARTVIKEEKLRGYPDETNSESRPPQQSCVLQRGAQEAEENPDADREFDDESSEDGEKRDHKVKSRGEDTGASMKHPKHHKNRAHSRSSSEERGLGTKHHSRGSQSRGHEHQDRQSRDQESCHKDRSHREEKSSHRHREASHKDHYWKKHEQEDKLKGREQEERQDREGKREKYSSREQERDRQRNDHDRYSEKEKKRKEKEEHTKARRERCEDSGKHREREKPEGHGQSSERHRDRRESSPRSRPKDDLDQERSSKARNTEKDKGEQGKPSHSETSLATKHRLAEERPEKGSEQERPPEAVSKFAKRSNEETVMSARDRYLARQMARINAKTYIEKEDD
Protein: NDH-dependent cyclic electron flow 1 (F4I890)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MASLISFSLLPKPKAVRSSISAPQTQTINTEKLEDKFGRKGIKFSESNNIPMVELKVRNGSSLKLSLSDAHVLSYKPKVYWKDEGFEEVLYTVDGDESRGGVGVVIVNGEEPKGGSSVISGCDWSVKDTDSDAIDALQIELSCTAGVLDITYIVSLYPVSMATALVVKNNGRKPVTLKPGIMSYLRFKKRSGAGIQGLKGCSYCPNPPLSSPFELLSPSEAMKAESSGWFGSEEGEKPGIWAVEDSVITLLEKKMSRIYGAPPAERLKAVYNTPPSKFETIDQKKKKVLDAKNKIKIPKGISNSFRERIVFQDDKDWVRRDVCGIPRIDVGQVWEATLLRVHRSNVNARSCRCSLRRDMERSNGNRA
Protein: G protein-coupled receptor kinase 2 (EC 2.7.11.16) (P32866)
Organism: Drosophila melanogaster (Fruit fly)
Function: Specifically phosphorylates the activated forms of G protein-coupled receptors (By similarity). Required during oogenesis and embryogenesis; component of a signaling pathway that functions during egg chamber maturation.
Subcellular location: Membrane {ECO:0000269|PubMed:9217001}. Note=Associated with nurse cell and oocyte plasma membranes during much of oogenesis.
Interaction partners:
- Protein smoothened
- G protein beta subunit 5
- G protein-coupled receptor kinase 1
- Kurtz arrestin
- Phosrestin-1
- Guanine nucleotide-binding protein subunit beta-1
- Guanine nucleotide-binding protein subunit beta-2
- ARF GTPase-activating protein Git
- Protein hedgehog
- Protein patched
Sequence:
MELENIVANTVYLKAREGGSDSNKGKSKKWRKILQFPHISQCINLKDKLDISYGYVIDQQPIGRELFRLFCENKRPVYFRYITFLDEVVKYEIEYISNRIFIGHDIGRRFLDVEAQLELRNGSGGDALDAETQEELLLNSSNANPTETAETEHCNNTTANNCNNINNSNNSQHSSDINHKKLDTRNHNGDDATGNGSSHQDDGDESVKCQEGHDDAEKGGGGEGGGGGKCVPVGGYPDELVLDVLNDDLIAQVRNKLNSGGKDIFAQCVNAVKAFLAGEPFREFESSMYFHRYLQWKWLEAQPITYKTFRMYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGESMVLIEKQILQKINSPFVVNLAYAYETKDALCLVLTIMNGGDLKFHIYNMGGEPGFELERARFYAAEVACGLQHLHKQGIVYRDCKPENILLDDHGHVRISDLGLAVEIPEGEMVRGRVGTVGYMAPEVIDNEKYAFSPDWFSFGCLLYEMIEGQAPFRMRKEKVKREEVDRRVKEDPEKYSSKFNDEAKSMCQQLLAKSIKQRLGCRNGRMGGQDVMAHPFFHSTQLNWRRLEAGMLEPPFVPDPHAVYAKDVLDIEQFSTVKGVNIDESDTNFYTKFNTGSVSISWQNEMMETECFRELNVFGPEECPTPDLQINAAPEPDKAGCFPFRRKKKQPARTQPIPIPEHLLTTSHSVSSTTVES
Protein: Periostin (PN) (Osteoblast-specific factor 2) (OSF-2) (Q62009)
Organism: Mus musculus (Mouse)
Function: Induces cell attachment and spreading and plays a role in cell adhesion. Enhances incorporation of BMP1 in the fibronectin matrix of connective tissues, and subsequent proteolytic activation of lysyl oxidase LOX.
Subcellular location: Golgi apparatus {ECO:0000269|PubMed:20181949}. Secreted {ECO:0000269|PubMed:10404027, ECO:0000269|PubMed:18450759}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:10404027}. Note=Colocalizes with BMP1 in the Golgi (PubMed:20181949). {ECO:0000269|PubMed:20181949}.
Interaction partners:
- Fibronectin
- Neurogenic locus notch homolog protein 1
- Bone morphogenetic protein 1
- Collagen alpha-1
- Collagen alpha-2
- Integrin alpha-V
- Lumican
- Asporin
- NADH dehydrogenase iron-sulfur protein 2, mitochondrial
- Collagen alpha-1
Sequence:
MVPLLPLYALLLLFLCDINPANANSYYDKVLAHSRIRGRDQGPNVCALQQILGTKKKYFSSCKNWYQGAICGKKTTVLYECCPGYMRMEGMKGCPAVMPIDHVYGTLGIVGATTTQHYSDVSKLREEIEGKGSYTYFAPSNEAWENLDSDIRRGLENNVNVELLNALHSHMVNKRMLTKDLKHGMVIPSMYNNLGLFINHYPNGVVTVNCARVIHGNQIATNGVVHVIDRVLTQIGTSIQDFLEAEDDLSSFRAAAITSDLLESLGRDGHFTLFAPTNEAFEKLPRGVLERIMGDKVASEALMKYHILNTLQCSEAITGGAVFETMEGNTIEIGCEGDSISINGIKMVNKKDIVTKNGVIHLIDEVLIPDSAKQVIELAGKQQTTFTDLVAQLGLASSLKPDGEYTLLAPVNNAFSDDTLSMDQRLLKLILQNHILKVKVGLSDLYNGQILETIGGKQLRVFVYRTAICIENSCMVRGSKQGRNGAIHIFREIIQPAEKSLHDKLRQDKRFSIFLSLLEAADLKDLLTQPGDWTLFAPTNDAFKGMTSEERELLIGDKNALQNIILYHLTPGVYIGKGFEPGVTNILKTTQGSKIYLKGVNETLLVNELKSKESDIMTTNGVIHVVDKLLYPADIPVGNDQLLELLNKLIKYIQIKFVRGSTFKEIPMTVYTTKIITKVVEPKIKVIQGSLQPIIKTEGPAMTKIQIEGDPDFRLIKEGETVTEVIHGEPVIKKYTKIIDGVPVEITEKQTREERIITGPEIKYTRISTGGGETGETLQKFLQKEVSKVTKFIEGGDGHLFEDEEIKRLLQGDTPAKKIPANKRVQGPRRRSREGRSQ
Protein: Ankyrin 2 (A0A5F9ZH34)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MTTMLQKSDSNASFLRAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILLENDTKGKVRLPALHIAARKDDTKSAALLLQNDHNADVQSKSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTALAIAKRLGYISVVDTLKVVTEEVTTTTTTITEKHKLNVPETMTEVLDVSDEEGDDTMTGDGGEYLRPEDLKELGDDSLPSSQFLDGMNYLRYSLEGGRSDSLRSFSSDRSHTLSHASYLRDSAVMDDSVVIPSHQVSTLAKEAERNSYRLSWGTENLDNVALSSSPIHSGFLVSFMVDARGGAMRGCRHNGLRIIIPPRKCTAPTRVTCRLVKRHRLATMPPMVEGEGLASRLIEVGPSGAQFLGPVIVEIPHFAALRGKERELVVLRSENGDSWKEHFCDYTEDELNEILNGMDEVLDSPEDLEKKRICRIITRDFPQYFAVVSRIKQDSNLIGPEGGVLSSTVVPQVQAVFPEGALTKRIRVGLQAQPMHSELVKKILGNKATFSPIVTLEPRRRKFHKPITMTIPVPKASSDVMLNGFGGDAPTLRLLCSITGGTTPAQWEDITGTTPLTFVNECVSFTTNVSARFWLIDCRQIQESVTFASQVYREIICVPYMAKFVVFAKSHDPIEARLRCFCMTDDKVDKTLEQQENFAEVARSRDVEVLEGKPIYVDCFGNLVPLTKSGQHHIFSFFAFKENRLPLFVKVRDTTQEPCGRLSFMKEPKSTRGLVHQAICNLNITLPIYTKESESDQEQEEEIDMTSEKNPQDEQERIEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIVHLMETNTEPLQERISHSYAEIEQTITLDHSEGFSVLQEELCTAQHKQKEEQAVSKESETCDHPPIVSEEDISVGYSTFQDGVPKTEGDSSATALFPQTHKEQVQQDFSGKMQDLPEESSLEYQQEYFVTTPGTETSETQKAMIVPSSPSKTPEEVSTPAEEEKLYLQTPTSSERGGSPIIQEPEEPSEHREESSPRKTSLVIVESADNQPETCERLDEDAAFEKGDDMPEIPPETVTEEEYIDEHGHTVVKKDNNE
Protein: GH07575p (Q7K1H9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- GEO07745p1
- IP04046p
- RE12410p
- RH02620p
- Mucin related 29B
- Uncharacterized protein, isoform A
- Frost
- trypsin
Sequence:
MQSHLIAILLATVAIGSCIANPNLISGPSRILEIMSATSDIQRNNPQLTVECFDYYNDVFKTEYAEYVDEYNLCVDKYDGGYEQVLEQYNSVVWDLSNSTFESCMFLLDCDKQNNSENALSCYSTEGPTYSKQLSNVAANASVSVSSLRQQVETLVFTRDQCCSATSRNYEIRSGESYEDLQKCLSGENPVPERSTTTTSSSSSSSTSTTAANPTTTTTTPSPSTTTSSSSTSSTTRSPSTVAHFSSVENSSGNSQHRFPRRLDNIFKHIL
Protein: Glycerol-3-phosphate dehydrogenase [NAD(P)+] (EC 1.1.1.94) (NAD(P)(+)-dependent glycerol-3-phosphate dehydrogenase) (NAD(P)H-dependent dihydroxyacetone-phosphate reductase) (P0A6S7)
Organism: Escherichia coli (strain K12)
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00394}.
Interaction partners:
- Probable glycerol-3-phosphate acyltransferase
- Glycerol-3-phosphate acyltransferase
- Aerobic glycerol-3-phosphate dehydrogenase
- Protein-export protein SecB
- Anaerobic glycerol-3-phosphate dehydrogenase subunit A
- GTPase Der
- Serine acetyltransferase
- 1-acyl-sn-glycerol-3-phosphate acyltransferase
- Anaerobic glycerol-3-phosphate dehydrogenase subunit C
- Anaerobic glycerol-3-phosphate dehydrogenase subunit B
Sequence:
MNQRNASMTVIGAGSYGTALAITLARNGHEVVLWGHDPEHIATLERDRCNAAFLPDVPFPDTLHLESDLATALAASRNILVVVPSHVFGEVLRQIKPLMRPDARLVWATKGLEAETGRLLQDVAREALGDQIPLAVISGPTFAKELAAGLPTAISLASTDQTFADDLQQLLHCGKSFRVYSNPDFIGVQLGGAVKNVIAIGAGMSDGIGFGANARTALITRGLAEMSRLGAALGADPATFMGMAGLGDLVLTCTDNQSRNRRFGMMLGQGMDVQSAQEKIGQVVEGYRNTKEVRELAHRFGVEMPITEEIYQVLYCGKNAREAALTLLGRARKDERSSH
Protein: Katanin-interacting protein (O60303)
Organism: Homo sapiens (Human)
Function: May influence the stability of microtubules (MT), possibly through interaction with the MT-severing katanin complex.
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:26714646}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:26714646}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:26714646}. Note=When overexpressed, localizes to the cytoplasm where it associates with acetylated alpha-tubulin. {ECO:0000269|PubMed:26714646}.
Interaction partners:
- Katanin p80 WD40 repeat-containing subunit B1
Sequence:
MDGQTLRKAERSWSCSREKKEGYAKDMVTDFDEKHDEYLILLQQRNRILKHLKSKDPVQLRLEHLEQGFSVYVNGANSELKSSPRKAIHSDFSRSASHTEGTHDYGRRTLFREAEEALRRSSRTAPSKVQRRGWHQKSVQIRTEAGPRLHIEPPVDYSDDFELCGDVTLQANNTSEDRPQELRRSLELSVNLQRKQKDCSSDEYDSIEEDILSEPEPEDPALVGHPRHDRPPSSGDWTQKDVHGEQETEGRSSPGPDTLVVLEFNPASKSHKRERNLSAKRKDNAEVFVPTKPEPNLTPQAPAVFPDQERMCSRPGSRRERPLSATRKTLCEAEYPEEDASAVLQAIQVENAALQRALLSRKAEQPASPLQDAEGPPAKPWTSLLEEKEETLELLPITTATTTQEPAGAAGGARAINQAMDRIGLLGSRQQQKLLKVLQAVESDSAHLGRVVSPTKEQVSDTEDKQRMRADEIKDAIYVTMEILSNWGNSWWVGLTEVEFFDLNDTKLYVSPHDVDIRNTATPGELGRLVNRNLAGKKDSSPWTCPFHPPLQLFFVIRNTRQLGDFHLAKIKVRNYWTADGDLDIGAKNVKLYVNRNLIFNGKLDKGDREAPADHSILVDQKNEKSEQLEEAMNAHSEESKGTHEMAGASGDKELGLGCSPPAETLADAKLSSQGNVSGKRKNSTNCRKDSLSQLEEYLRLSAVPTSMGDMPSAPATSPPVKCPPVHEEPSLIQQLENLMGRKICEPPGKTPSWLQPSPTGKDRKQGGRKPKPLWLSPEKPLAWKGRLPSDDVIGEGPGETEARDKGLRHEPGWGTSRSVNTKERPQRATTKVHSDDSDIFNQPPNRERPASGRRGSRKDAGSSSHGDDQPASREDTWSSRTPSRSRWRSEQEHTLHESWSSLSAFDRSHRGRISNTELPGDILDELLQQKSSRHSDLPPSKKGEQPGLSRGQDGYSGETDAGGDFKIPVLPYGQRLVIDIKSTWGDRHYVGLNGIEIFSSKGEPVQISNIKADPPDINILPAYGKDPRVVTNLIDGVNRTQDDMHVWLAPFTRGRSHSITIDFTHPCHVALIRIWNYNKSRIHSFRGVKDITMLLDTQCIFEGEIAKASGTLAGAPEHFGDTILFTTDDDILEAIFYSDEMFDLDVGSLDSLQDEEAMRRPSTADGEGDERPFTQAGLGADERIPELELPSSSPVPQVTTPEPGIYHGICLQLNFTASWGDLHYLGLTGLEVVGKEGQALPIHLHQISASPRDLNELPEYSDDSRALDKLIDGTNITMEDEHMWLIPFSPGLDHVVTIRLDRAESIAGLRFWNYNKSPEDTYRGAKIVHVSLDGLCVSPPEGFLIRKGPGNCHFDFAQEILFVDYLRAQLLPQPARRLDMRSLECASMDYEAPLMPCGFIFQFQLLTSWGDPYYIGLTGLELYDERGEKIPLSENNIAAFPDSVNSLEGVGGDVRTPDKLIDQVNDTSDGRHMWLAPILPGLVNRVYVIFDLPTTVSMIKLWNYAKTPHRGVKEFGLLVDDLLVYNGILAMVSHLVGGILPTCEPTVPYHTILFTEDRDIRHQEKHTTISNQAEDQDVQMMNENQIITNAKRKQSVVDPALRPKTCISEKETRRRRC
Protein: UDP-glucuronosyltransferase 1A5 (UGT1A5) (EC 2.4.1.17) (B5) (UDP-glucuronosyltransferase 1-5) (UDPGT 1-5) (UGT1*5) (UGT1-05) (UGT1.5) (Q64638)
Organism: Rattus norvegicus (Rat)
Function: UDP-glucuronosyltransferase (UGT) that catalyzes phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase the metabolite's water solubility, thereby facilitating excretion into either the urine or bile. Essential for the elimination and detoxification of drugs, xenobiotics and endogenous compounds. Involved in the glucuronidation of the AGTR1 angiotensin receptor antagonist zolarsatan, a drug which can inhibit the effect of angiotensin II.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P22309}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MGLHVTLQGLAGLLLLLYALPWAEGGKVLVFPMEGSHWLSMRDVVRELHARGHQAVVLAPEVTVHIKEEDFFTLQTYPVPYTRQGFRQQMMRNIKVVFETGNYVKTFLETSEILKNISTVLLRSCMNLLHNGSLLQHLNSSSFDMVLTDPVIPCGQVLAKYLGIPTVFFLRYIPCGIDSEATQCPKPSSYIPNLLTMLSDHMTFLQRVKNMLYPLALKYICHFSFTRYESLASELLQREVSLVEVLSHASVWLFRGDFVFDYPRPVMPNMVFIGGINCVIKKPLSQEFEAYVNASGEHGIVVFSLGSMVSEIPEKKAMEIAEALGRIPQTLLWRYTGTRPSNLAKNTILVKWLPQNDLLGHPKARAFITHSGSHGIYEGICNGVPMVMMPLFGDQMDNAKRMETRGAGVTLNVLEMTADDLENALKTVINNKSYKENIMRLSSLHKDRPIEPLDLAVFWVEYVMRHKGAPHLRPAAHDLTWYQYHSLDVIGFLLAIVLTVVFIVYKSCAYGCRKCFGGKGRVKKSHKSKTH
Protein: Nucleobase-ascorbate transporter 6 (AtNAT6) (Q27GI3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Purine-uracil permease NCS1
- Putative purine permease 12
- Adenine/guanine permease AZG1
- ABC transporter I family member 19
- Probable serine/threonine-protein kinase PBL5
- Adenine/guanine permease AZG2
- Glutamate receptor 1.2
- Receptor-like serine/threonine-protein kinase ALE2
Sequence:
MAGGGAPAPKADEPQPHPPKDQLPNISYCITSPPPWPEAILLGFQHYLVMLGTTVLIPTALVPQMGGGYEEKAKVIQTILFVAGINTLLQTLFGTRLPAVVGASYTFVPTTISIILSGRFSDTSNPIDRFERIMRATQGALIVASTLQMILGFSGLWRNVVRFLSPISAVPLVGLVGFGLYEFGFPGVAKCIEIGLPELLILVFVSQYLPHVIKSGKNVFDRFAVIFAVVIVWIYAHLLTVGGAYNGAAPTTQTSCRTDRAGIIGAAPWIRVPWPFQWGAPSFDAGEAFAMMMASFVALVESTGAFVAVSRYASATMLPPSILSRGIGWQGVAILISGLFGTGAGSSVSVENAGLLALTRVGSRRVVQIAAGFMIFFSILGKFGAVFASIPAPIIAALYCLFFAYVGAGGLSFLQFCNLNSFRTKFILGFSVFLGLSIPQYFNEYTAIKGYGPVHTGARWFNDMVNVPFSSEPFVAGSVAFFLDNTLHKKDSSIRKDRGKHWWDKFRSFKGDTRSEEFYSLPFNLNKYFPSV
Protein: CCR4-NOT transcription complex subunit 2 (F8VRS8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVRTDGHTLSEKRNYQVTNSMFGASRKKFVEGVDSDYHDENMYYSQSSMFPHRSEKDMLASPSTSGQLSQFGASLYGQQNGSENVTGLDLSDFPALADRNRREGSGNPTPLINPLAGRAPYVGMVTKPANEQSQDFSIHNEDFPALPGSSYKDPTSSNDDSKSNLNTSGKTTSSTDGPKFPGDKSSTTQNNNQQKKGIQVLPDGRVTNIPQGMVTDQFGMIGLLTFIRAAETDPGMVHLALGSDLTTLGLNLNSPENLYPKFASPWASSPCRPQDI
Protein: Succinate dehydrogenase, putative (Q38EW9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- Succinate--CoA ligase subunit alpha, mitochondrial
- Succinate--CoA ligase subunit beta, mitochondrial
- fumarate hydratase
- fumarate hydratase
- Electron transfer protein, putative
- fumarate reductase
- fumarate reductase
- fumarate reductase
- aspartate transaminase
Sequence:
MPAAPLPGEVAKFCSPLYMHKRILRAAAPKPPTVFTAKDNSKTAFHVVTQRPGFATTPYTVSRWYLKEKVHSSNRNRLEGLYECVLCASCTGSCPQYWWNRELFLGPAVLLQSYRWLIEPLDRDFDSRVKMFEHGPLVNFCHNIFNCSITCPKFLNPGMASKEIKRLSSPATLRVGPPLEDAKVASKY
Protein: UDP-glucose 6-dehydrogenase 4 (At-UGD4) (UDP-Glc dehydrogenase 4) (UDP-GlcDH 4) (UDPGDH 4) (EC 1.1.1.22) (Q9FM01)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the biosynthesis of UDP-glucuronic acid (UDP-GlcA), providing nucleotide sugars for cell-wall polymers.
Interaction partners:
- UDP-D-apiose/UDP-D-xylose synthase 2
- UDP-D-apiose/UDP-D-xylose synthase 1
- Trifunctional UDP-glucose 4,6-dehydratase/UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose-reductase RHM3
- Trifunctional UDP-glucose 4,6-dehydratase/UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose-reductase RHM1
- UDP-sugar pyrophosphorylase
- Trifunctional UDP-glucose 4,6-dehydratase/UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose-reductase RHM2
- UTP--glucose-1-phosphate uridylyltransferase 1
- UTP--glucose-1-phosphate uridylyltransferase 2
- UDP-glucuronic acid decarboxylase 2
- UDP-glucuronic acid decarboxylase 5
Sequence:
MVKICCIGAGYVGGPTMAVIALKCPDIEVAVVDISVPRINAWNSDQLPIYEPGLDDIVKQCRGKNLFFSTDVEKHVREADIVFVSVNTPTKTTGLGAGKAADLTYWESAARMIADVSVSDKIVVEKSTVPVKTAEAIEKILMHNSKGIKFQILSNPEFLAEGTAIADLFNPDRVLIGGRETPEGFKAVQTLKEVYANWVPEGQIITTNLWSAELSKLAANAFLAQRISSVNAMSALCESTGADVTQVSYAVGTDSRIGSKFLNASVGFGGSCFQKDILNLVYICQCNGLPEVAEYWKQVIKINDYQKNRFVNRIVSSMFNTVSNKKVAILGFAFKKDTGDTRETPAIDVCKGLLGDKAQISIYDPQVTEEQIQRDLSMKKFDWDHPLHLQPMSPTTVKQVSVTWDAYEATKDAHAVCVLTEWDEFKSLDYQKIFDNMQKPAFIFDGRNIMNVNKLREIGFIVYSIGKPLDPWLKDMPAFV
Protein: NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial (A0A1D8PCD3)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:O43181}; Peripheral membrane protein {ECO:0000250|UniProtKB:O43181}; Matrix side {ECO:0000250|UniProtKB:O43181}.
Interaction partners:
- NADH-ubiquinone oxidoreductase
- Uncharacterized protein
- Uncharacterized protein
- Nuc2p
- Complex 1 LYR protein domain-containing protein
- NADH dehydrogenase 1 beta subcomplex subunit 9
- Zinc finger CHCC-type domain-containing protein
- Ribosomal protein/NADH dehydrogenase domain-containing protein
- NADH dehydrogenase iron-sulfur protein 3, mitochondrial
- NADH-ubiquinone oxidoreductase B12 subunit
Sequence:
MLSRVSIRSLPLCTRTFATTSILKQSELTAATDSSGKEIVSGAPRELVTERVVRIYQEAKPATQSGHHNGSHWKLDWDVLGKGNRWENDLMGYQGSADYMQGTIMKFDTKESAIKFAENQGWDHYVQEPKKRHFRKKDYSANFYHSAGPLKHIRTK
Protein: Ubiquitin recognition factor in ER-associated degradation protein 1 (Ubiquitin fusion degradation protein 1 homolog) (UB fusion protein 1) (Q9ES53)
Organism: Rattus norvegicus (Rat)
Function: Essential component of the ubiquitin-dependent proteolytic pathway which degrades ubiquitin fusion proteins. The ternary complex containing UFD1, VCP and NPLOC4 binds ubiquitinated proteins and is necessary for the export of misfolded proteins from the ER to the cytoplasm, where they are degraded by the proteasome. The NPLOC4-UFD1-VCP complex regulates spindle disassembly at the end of mitosis and is necessary for the formation of a closed nuclear envelope. It may be involved in the development of some ectoderm-derived structures. Acts as a negative regulator of type I interferon production via the complex formed with VCP and NPLOC4, which binds to RIGI and recruits RNF125 to promote ubiquitination and degradation of RIGI (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:10811609}. Cytoplasm, cytosol {ECO:0000269|PubMed:10811609}.
Interaction partners:
- Transitional endoplasmic reticulum ATPase
- Nuclear protein localization protein 4 homolog
- UBX domain-containing protein 7
- FAS-associated factor 2
- FAS-associated factor 1
- UBX domain-containing protein 7
- Phospholipase A-2-activating protein
- Derlin
- NSFL1 cofactor p47
- Ubiquitin thioesterase OTU1
Sequence:
MFSFNMFDHPIPRVFQNRFSTQYRCFSVSMLAGPNDRSDVEKGGKIIMPPSALDQLSRLNITYPMLFKLTNKNSDRMTHCGVLEFVADEGICYLPHWMMQNLLLEEGGLVQVESVNLQVATYSKFQPQSPDFLDITNPKAVLENALRNFACLTTGDVIAINYNEKIYELRVMETKPDKAVSIIECDMNVDFDAPLGYKEPERPVQHEESIEGEADHSGYAGEVGFRAFSGSGNRLDGKKKGVEPSPSPIKPGDIKRGIPNYEFKLGKITFIRNSRPMVKKVEEDEAGGRFVAFSGEGQSLRKKGRKP
Protein: ABC transporter C family member 1 (ABC transporter ABCC.1) (AtABCC1) (EC 7.6.2.2) (ATP-energized glutathione S-conjugate pump 1) (Glutathione S-conjugate-transporting ATPase 1) (Multidrug resistance-associated protein 1) (Q9C8G9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Pump for glutathione S-conjugates. Mediates the transport of S-(2,4-dinitrophenyl)-glutathione (DNP-GS), GSSG, cyanidin 3-glucoside-GS (C3G-GS) and metolachlor-GS (MOC-GS).
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:15133126, ECO:0000269|PubMed:17151019}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000269|PubMed:15133126}. Note=Tonoplast.
Interaction partners:
- Glutathione gamma-glutamylcysteinyltransferase 1
- Putative cadmium/zinc-transporting ATPase HMA4
- Vacuolar cation/proton exchanger 4
- Ankyrin repeat family protein
- Metal transporter Nramp1
- Metal transporter Nramp3
- Putative inactive cadmium/zinc-transporting ATPase HMA3
- ABC transporter G family member 40
- Cadmium/zinc-transporting ATPase HMA2
- Oligopeptide transporter 6
Sequence:
MGFEPLDWYCKPVPNGVWTKTVDYAFGAYTPCAIDSFVLGISHLVLLILCLYRLWLITKDHKVDKFCLRSKWFSYFLALLAAYATAEPLFRLVMRISVLDLDGAGFPPYEAFMLVLEAFAWGSALVMTVVETKTYIHELRWYVRFAVIYALVGDMVLLNLVLSVKEYYGSFKLYLYISEVAVQVAFGTLLFVYFPNLDPYPGYTPVGTENSEDYEYEELPGGENICPERHANLFDSIFFSWLNPLMTLGSKRPLTEKDVWHLDTWDKTETLMRSFQKSWDKELEKPKPWLLRALNNSLGGRFWWGGFWKIGNDCSQFVGPLLLNELLKSMQLNEPAWIGYIYAISIFVGVVLGVLCEAQYFQNVMRVGYRLRSALIAAVFRKSLRLTNEGRKKFQTGKITNLMTTDAESLQQICQSLHTMWSAPFRIIVALVLLYQQLGVASIIGALFLVLMFPIQTVIISKTQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSAFNMFILNSIPVLVTVVSFGVFSLLGGDLTPARAFTSLSLFSVLRFPLFMLPNIITQMVNANVSLNRLEEVLSTEERVLLPNPPIEPGQPAISIRNGYFSWDSKADRPTLSNINLDIPLGSLVAVVGSTGEGKTSLISAMLGELPARSDATVTLRGSVAYVPQVSWIFNATVRDNILFGAPFDQEKYERVIDVTALQHDLELLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVCILDDPLSALDAHVGQQVFEKCIKRELGQTTRVLVTNQLHFLSQVDKILLVHEGTVKEEGTYEELCHSGPLFQRLMENAGKVEDYSEENGEAEVDQTSVKPVENGNANNLQKDGIETKNSKEGNSVLVKREERETGVVSWKVLERYQNALGGAWVVMMLVICYVLTQVFRVSSSTWLSEWTDSGTPKTHGPLFYNIVYALLSFGQVSVTLINSYWLIMSSLYAAKKMHDAMLGSILRAPMVFFQTNPLGRIINRFAKDMGDIDRTVAVFVNMFMGSIAQLLSTVILIGIVSTLSLWAIMPLLVVFYGAYLYYQNTSREIKRMDSTTRSPVYAQFGEALNGLSSIRAYKAYDRMAEINGRSMDNNIRFTLVNMAANRWLGIRLEVLGGLMVWLTASLAVMQNGKAANQQAYASTMGLLLSYALSITSSLTAVLRLASLAENSLNSVERVGNYIEIPSEAPLVIENNRPPPGWPSSGSIKFEDVVLRYRPELPPVLHGVSFLISPMDKVGIVGRTGAGKSSLLNALFRIVELEKGRILIDECDIGRFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFSEHNDADLWESLERAHLKDTIRRNPLGLDAEVTEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDVLIQKTIREEFKSCTMLIIAHRLNTIIDCDKVLVLDSGKVQEFSSPENLLSNGESSFSKMVQSTGTANAEYLRSITLENKRTREANGDDSQPLEGQRKWQASSRWAAAAQFALAVSLTSSHNDLQSLEIEDDNSILKKTKDAVVTLRSVLEGKHDKEIEDSLNQSDISRERWWPSLYKMVEGLAVMSRLARNRMQHPDYNLEGKSFDWDNVEM
Protein: Phosphatidylinositol N-acetylglucosaminyltransferase subunit C (Phosphatidylinositol-glycan biosynthesis class C protein) (PIG-C) (Q92535)
Organism: Homo sapiens (Human)
Function: Part of the glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex that catalyzes the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol and participates in the first step of GPI biosynthesis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:8806613}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit P
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit H
- Dolichol phosphate-mannose biosynthesis regulatory protein
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit A
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit Q
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit Y
- N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Protein preY, mitochondrial
- 3'-5' exoribonuclease 1
Sequence:
MYAQPVTNTKEVKWQKVLYERQPFPDNYVDRRFLEELRKNIHARKYQYWAVVFESSVVIQQLCSVCVFVVIWWYMDEGLLAPHWLLGTGLASSLIGYVLFDLIDGGEGRKKSGQTRWADLKSALVFITFTYGFSPVLKTLTESVSTDTIYAMSVFMLLGHLIFFDYGANAAIVSSTLSLNMAIFASVCLASRLPRSLHAFIMVTFAIQIFALWPMLQKKLKACTPRSYVGVTLLFAFSAVGGLLSISAVGAVLFALLLMSISCLCPFYLIRLQLFKENIHGPWDEAEIKEDLSRFLS
Protein: Cell wall biosynthesis/cell cycle regulator smi1 (O14362)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Protein involved in the regulation of cell wall assembly and 1,3-beta-glucan synthesis, possibly through the transcriptional regulation of cell wall glucan and chitin synthesis (By similarity). Involved in cellular response to nitrogen starvation and required for quiescence-maintenance by regulating negatively G0 to G1 transition.
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}. Note=Localizes to the division site. {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MSKNSFSSMANSVTSFFQSLTTPNRHADPSFRPSRREKQSRLPTPLQSVAASAYSGVNASQTGLLNDSRANSVTNLPNSSNTSQVGLNNISPAPVGYVPGSKTNELANNSMEMQEISPNGSASLPPPVSESWRRIDRWAEENYYELYCQLCYGATVADVDSLEYELECTLPRDVRESLYIHDGQDRGGQPTGILFGVTLLDIEEIEEESELWRRVAQSYAEATLAGKIDQAVASRQASFPPGAVQCVYAHPGWIPLAKDFVGNNIAIDLAPGPAGQWGQVILFGRDQDTKYVVARSWADFLAIVAYDMENGKWLVDEDDNSLRLIYGPPREQWSYLDILKYRARKAERRKFKKRDGKRTTRPIPKSIAKEDVTNSANSTAPSTGTTVLDDGLDNNYEDIPLYGPSKDEELIKKEELEADTDLGLINTSEINQPANLPDEPTAETSNPVSATTVEAVTTTADNKDEEKNDHVTEDVSQNSTIAEASSLQAQEEEKEIETTSVKQE
Protein: ST2L protein (S6EPL9)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
Sequence:
MTKRFFFSTSTLQVPVLQKMRSFTFRLVDGGLMFLLLSLTRISAQREMSLNPTTISHYTESPCQLFDKYETTVTEGEALSLPAYYDLSELVWASVTEFTWYRNRTQELSSSEEERVHHHGPVLFFLPLLINDSDQYYTYWRKGADTCLIFVTEVIVVKAQPFDHSVLFNDISESAENIAIPCPDPVEKLCQDGKDNLAWYKNFSLIPNESERNLWVYGASKADEGIYTCVCTWEHNGTVLNTSASRRLKIQAPSASHPPQINLPINGSTETTDLYTTKKLRCEAFCGQNIEDNCHVWWEINGVKVRSQQQGYSVNTTSEVEVSSMRSIFTAILTINTVTMRDLQSKFTCVAMNDQKWNYAVVTLKLRAPIGFMGLCVVLLLFFLLAAVAVKVFDIDLALLFRGVFKCCGRSEDGKVYDAYVVYQMDGLDQEREEKVYHFVSIVLPTVLEQKCGFRLFIHGRDDLPGEDNMELVEACMRLSRRLIVILTPSSSTRSGSGGQGSCGQWGYSSSLTTAEDYDCQVGLLQALVHSEMNVILIQLGDMGEGGYTHLPPGLQHLVRKSAPLMWHEGRRGSTLPNSSFWKRVRYMMPWPRSTSFDNQLI