wanglab/gogpt-training-data huggingface dataset:
Protein: Probable alginate O-acetylase AlgI (EC 2.3.1.-) (Alginate biosynthesis protein AlgI) (Q51392)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Together with AlgJ and AlgF, forms an inner membrane complex which probably interacts with the alginate polymerization-transport complex and adds acetyl groups at the O-2 and O-3 positions of mannuronate residues. Acetylation of alginate is important for the architecture of biofilms and increases resistance to opsonic killing in the host.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:12003941, ECO:0000269|PubMed:8636017}; Multi-pass membrane protein {ECO:0000269|PubMed:12003941, ECO:0000269|PubMed:8636017}.
Interaction partners:
- Probable alginate O-acetylase AlgJ
- Alginate biosynthesis protein AlgF
- Alginate biosynthesis protein AlgX
- Mannuronan C5-epimerase
- Alginate lyase
- Mannuronan synthase
- Alginate production protein AlgE
- Mannuronan synthase
- Alginate biosynthesis protein AlgK
- Alginate biosynthesis protein AlgA
Sequence:
MVFSSNVFLFLFLPVFLGLYYLSGERYRNLLLLIASYVFYAWWRVDFLLLFAGVTVFNYWIGLRIGAAGVRTRAAQRWLILGVVVDLCVLGYFKYANFGVDSLNEIITSFGMQPFVLTHILLPIGISFYTFESISYIIDVYRGDTPATHNLIDFAAFVAIFPHLIAGPVLRFKDLVDQFNHRTHTVDKFAEGCTRFMQGFVKKVFIADTLAALADHCFALQNPTTGDAWLGALAYTAQLYFDFSGYSDMAIGLGLMMGFRFMENFNQPYISQSITEFWRRWHISLSTWLRDYLYISLGGNRGSTFQTYRNLFLTMLLGGLWHGANFTYIIWGAWHGMWLAIERALGVNAAPRVLNPLKWVITFLLVVIGWVIFRAENLQVAWRMYEAMFSFGTWQLSELNRANLTGLQVGTLVLAYLVLAFFGLRQFYNQPLQTKAPKAAANSDEVAADGPASAQPRAPREAAGDPAAIAYSPSGALVYQPSWLSQLPVLATRLALLLLFAASVLKLSAQSYSPFLYFQF
Protein: Intraflagellar transport associated protein 2 (Q9XUC2)
Organism: Caenorhabditis elegans
Function: Component of the intraflagellar transport (IFT) complex B required for transport of proteins in the motile cilium. May be required for ciliary entrance and transport of specific ciliary cargo proteins such as che-3 which are related to motility. Regulates specific signaling activities in the cilia, such as the daf-2/insulin receptor-like transduction pathway.
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:16968739}. Note=Moves along the axoneme.
Interaction partners:
- Intraflagellar transport protein 81 homolog
- Intraflagellar transport protein 74 homolog
- Tetratricopeptide repeat protein 30 homolog
- Intraflagellar transport protein 46 homolog
- Intraflagellar transport protein 56 homolog
- Intraflagellar transport protein 52 C-terminal domain-containing protein
- TRAF3-interacting protein 1
- Intraflagellar transport protein che-13
- Intraflagellar transport protein 88 homolog
- Clusterin-associated protein 1 homolog
Sequence:
MATENPQTWALWLILSEMASDMQEDKKVAKILVLGPPKAGKTTLCTFLADFMEDGDTLKKGEDSGERERKFEFEFTSVYRPTKGVRIQEFETHEFFTEQEQNELGGTRRLEDSEIQLWDVSGDKKYEDCWPAIKENAEGVILVVNPEEHKGSDLQQWFYEFVEKENIDLSCVMVILNEQGAKKTNHEQISGFEILPKLRGVHHVAHHFGSEAMQVKMEVNSFMASVLKMDQRQMGSGVDHGLGYADEQEDDF
Protein: Store-operated calcium entry-associated regulatory factor (Transmembrane protein 66) (H0YBH7)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004115}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004115}.
Interaction partners:
Sequence:
XAAACGPGAAGYCLLLGLHLFLLTAGPALGWNDPDRMLLRDVKALTLHYDRYTTSRRLDPIPQLKCVGGTAGCDSYTPKVIQCQNKGWDGYDVQWECKTDLDIAYKFGKTVVSCEGYESSEDQYVLRGSCGLEYNLDYTELGLQKLKESGKQHGFASFSDYYYKWSSADSCNMSGLITIVVLLGIAFVVYKLFLSDGQYSPPPYSEYPPFSHRYQRFTNSAGPPPPGFKSEFTGPQNTGHGATSGFGSAFTGQQGYENSGPGFWTGLGTGGILGYLFGSNRAATPFSDSWYYPSYPPSYPGTWNRAYSPLHGGSGSYSDMVVPGDDKVESWSQTLDAEILDFSSLSL
Protein: Carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase (A0A8I5ZMM2)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MVPPLTCMVPPLTLPAACAVAVVLQLTTLRAPACRSRLLSSAPRSEPRGPTPARGVCLVPVGLAAPPASRCSPCLSSDPMAALVLEDGSVLQGRPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPSDEEDEFGLSKWFESSEIHVAGLVVGECCPTPSHWSATCTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKLVQKGTEPSALPFVDPNARPLAPEVSIKTPRVFNAGGAPRIFAVDCGLKYNQIRCLCQLGAEVTVVPWNHELDSRKYDGLFLSNGPGDPASYPGVVSTLNRVLSEPNPRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGTGRCFLTSQNHGFAVDADSLPAGWAPLFTNANDCSNEGIVHDNLPFFSVQFHPEHRAGPSDMELLFDVFLETVRDTVAGNAEGRTVRERLAQRLCPPELPIPGSGLPPPRKVLILGSGGLSIGQAGEFDYSGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLPITPHYVTQVIRNERPDGILLTFGGQTALNCGVELTKAGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASTKEELSALVAPAFAHTSQVLIDKSLKGWKEIEYEVVRDAYGNCVTVCNMENLDPLGIHTGESIVVAPSQTLNDREYQLLRRTAIKVTQHLGIVGECNVQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLPELRNSVTGGTAAFEPSLDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKALRMVDENCVGFDHTVKPVSDVELETPTDKRIFVVAAALWAGYSVERLYELTRIDCWFLHRMKRIVTHAKLLEQHRGRPLPQDLLHQAKCLGFSDKQIALAVLSTELVVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTYWGNTHDLDFRTPHVLVLGSGVYRIGSSVEFDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGGQLPNNMAMALHRQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVAYTDGDLERFLSSAAAVSKEHPVVISKFIQEAKEIDVDAVACDGIVSAIAISEHVENAGVHSGDATLVTPPQDITPKTLERIKAIVHAVGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRIIMGEKVESVGLMTGSGVVGVKVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPKKNILLTIGSYKNKSELLPTVRLLESLGYSLYASLGTADFYTEHGVKVTAVDWHFEEAVDGECPPQRSILDQLAENHFELVINLSMRGAGGRRLSSFVTKGYRTRRLAADFSVPLIIDIKCTKLFVEALGQIGPAPPLKVHVDCMTSQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFTLFLGASSENAGTLGAVAGSAAGLKLYLNETFSELRLDSVAQWMEHFETWPSHLPIVAHAERQSVAAVLMVAQLTRRSVHICHVARKEEILLIKTAKAQGLPVTCEVAPHHLFLNREDLERLGPGKGEVRPELGSREDMEALWENMAVIDCFASDHAPHTLEEKCGPKPPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPLQEDTYVEVDLEHEWTVPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYIDGQVLVPPGYGQDVRKWPQGAVPQPPPPTPTTTEITTTPERPRRVIPGLPDGRFHLPPRIHRASDPGLPAMYLRPGAGISWGSRAWAEEPKEKPPRKVAESELIGTPDGPCYPVPPVPRQASPQNLGSSGLLHPQMSPLLHSLVGQHILSVKQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATSSVQKGESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGDLKHGRTVHSLACLLTQYRVSLRYVAPPSLRMPSSVWDFVASRGTKQEEFESIEEALPDTDVLYMTRIQKERFGSSQEYEACFGQFILTPHIMTRAKKKMVVMHPMPRVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLGRF
Protein: Mannan endo-1,6-alpha-mannosidase DFG5 (EC 3.2.1.101) (Endo-alpha-1->6-D-mannanase DFG5) (Q5ACZ2)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Required for normal synthesis of the cell wall and alkaline pH-induced hypha formation.
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:12912894}. Cell membrane {ECO:0000269|PubMed:12912894}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:12912894}.
Interaction partners:
- Mannan endo-1,6-alpha-mannosidase DCW1
- Autophagy-related protein 17
- Autophagy-related protein 13
Sequence:
MVSLQQLTISILLLFTASVQSLDINVDDKDSICSAAKYVVQGIWNYYEGLKYGGTVGMFAPPNYWWNAGEAFGGLVDFYTYCQSDNSTLEKLIYNGMYHQAGENYNYIPSNQSMTEGNDDQGVWGMAIMEAVERNFTEPESHSWLEMVQAVFNTMNARWDADNCGGGLRWQIFTWNSGYDYKNSISNGCLFHLAARLARYTGNSSVYVDTAEKVWKWMEDVGFLTEEDNGDVRIYDGAKITNNCSSVTDLRWSYTYGVFMAGCAYLYNFTGDDVWLTRTNEIVQASLSYFFANKIMQETTCQPQNKCNNDQRSFRCLFSRCLGLTTQLAPETKDRIREVLEASAEGAAKSCSGGSDGVTCGENWAIDKWDGVYGLGEQTSALEVMMALIVEPPLSVKTGGTNRTDYSAGTNSEDNANKNELTITGKDKAGAGVLTAIVLAVILGGAIWMIF
Protein: Alcohol dehydrogenase 8b (Mixed alcohol dehydrogenase Adh8b) (Q7T2J4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- S-formylglutathione hydrolase
- Aldehyde dehydrogenase 9 family, member A1a, tandem duplicate 2
- Aldehyde dehydrogenase
- Aldehyde dehydrogenase
- Aldehyde dehydrogenase 1 family member A3
- Aldehyde dehydrogenase 1 family, member A2
- Alcohol dehydrogenase iron-containing 1.
- 4-trimethylaminobutyraldehyde dehydrogenase A
- Aldehyde dehydrogenase 2 family member, tandem duplicate 1
- Amine oxidase [flavin-containing]
Sequence:
MATAGKVIKCRAAVAWEPKAPLVMEEIEVAPPQEGEVRIKILYTSLCHTDLFHLLESTDNKGFPTILGHEAAGVVESVGPGVTEFKPGDKVIPNSGCQCRECKFCKSPRTNLCERSWVNDHIEYMSYPKTSFTCRGKPILQFTNTGTLAEYIVIRQIYVVKIDDDAPLDRVCLLGCGVTTGYGAAVNSAGVTPGSVCAVFGLGAVGLAAVMGCKNAGASRIFAVDINEKKFEKAKVFGATDFLNPKAYNKPISEVLIEMTNGGVDFSLECVGNTEVSRLALESCAKGWGLSVLVGYTNTDFSSKPIQLIYGKTWKGTLLGGFKIKDGVPKLVLDYMSGKIMLDEFITQRMKLEQVNDVVKLMKNGECIRCILDMSK
Protein: Ankyrin repeat and LEM domain containing 1 (A0A499FJM0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MWTPVRRGAAWLGTLLGPGEGPPEPRGGAAHAHKPPAGSRKSTDQAVRFGPSQGMCSEARLARRLRDALREEEPWAVEELLRCGADPNLVLEDGAAAVHLAAGARHPRGLRCLGALLRQGGDPNARSVEALTPLHVAAAWGCRRGLELLLSQGADPALRDQDGLRPLDLALQQGHLECARVLQDLDTRTRTRTRIGAETQEPEPAPGTPGLSGPTDETLDSIALQKQPCRGDNRDIGLEADPGPPSLPVPLETVDKHGSSASPPGHWDYSSDASFVTAVEVSGAEDPASDTPPWAGSLPPTRQGLLHVVHANQRVPRSQGTEAELNARLQALTLTPPNAAGFQSSPSSMPLLDRSPAHSPPRTPTPGASDCHCLWEHQTSIDSDMATLWLTEDEASSTGGREPVGPCRHLPVSTVSDLELLKGLRALGENPHPITPFTRQLYHQQLEEAQIAPGPEFSGHSLELAAALRTGCIPDVQADEDALAQQFEQPDPARRWREGVVKSSFTYLLLDPRETQDLPARAFSLTPAERLQTFIRAIFYVGKGTRARPYVHLWEALGHHGRSRKQPHQACPKVRQILDIWASGCGVVSLHCFQHVVAVEAYTREACIVEALGIQTLTNQKQGHCYGVVAGWPPARRRRLGVHLLHRALLVFLAEGERQLHPQDIQARG
Protein: N-acetyltransferase B complex (NatB) non catalytic subunit (Q585L6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- N-acetyltransferase complex ARD1 subunit, putative
- N-acetyltransferase, putative
- N-acetyltransferase subunit ARD1
- N-acetyltransferase, putative
- Mak10 subunit, NatC N
Sequence:
MAGRVSDRIFDLIDTGKLGQAEGLLEDALSKFPNDHAVLAAEALLLLRKKVIDKARSKAEALSLQNVTDGSAVNALVHVLQQCCSWEALVRTYERLKGIQDEKVVLENLFQTYVRMGAYNMAQKTALQLNSGWPNPRYHVWVVQSMLAQVPRDSVDHALLKVSANLLEAAVLTEKGTMTTSTSRTYVQVLQQQKLYADAVKFLCSTRGASVGLPPARLEMLAKVLQLNGELAKANAIAKQLWTHQPENWTFVELYLNSLSESNATEGVLELDGPEESKCVSINLSNSDRTLEDALRFARSLSAESLKGSSGSRLGRGPSMAVLEILSRLGDDVQLRNETVAYAKRFYKASCCFLDISTYVDATAASAIYAWSQEDGGPEGKERLHYHMRRILGLRCHVALWGITAETQPSHAEVEELLQACIRSYEEARPLSENLSWSEEGLCDGYITVALNISLHVYEATKNVEWVQKGLALLDSVDRRENNPTWLTFSVCFARILGLADVAACCQLDFKSIQRDTMSHVGYWPLVAGGALDGVCEWNTAAWEHYGMLQRDCSLLRIKVFTYMSWPAMKDIQEYERRQTNSLARVIYSLSRIAGELRQCQTQRNVFDLMQAEERVLSQVFEALQDPQAKDLVDNTDWVVVRSMVLGNIHSQKVEALANTLVGMPTVNERVEHARQLVGSLMLLHDVSMLEAHRVQVSNLPKRRKGKGGKSDAAPQDVPLPMLLCQQHTETLQTLPVMSSIAPLTLEFVKTYGSGARIAHTDSFAHALRAVLEVENIKSFLFPEASILTALLQVAPTSTLPVAAWAKDLQAATESARDRLRQSPPMKALGKREQKIREASLSRINSALTDILREAAAASRRR
Protein: LOB domain-containing protein 23 (ASYMMETRIC LEAVES 2-like protein 14) (AS2-like protein 14) (P59467)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- LOB domain-containing protein 37
Sequence:
MNPKRCAACKYLRRRCPKDCVFSPYFPPNDPQKFACVHRIYGAGNVSKMLQQLPDQTRAEAVESLCFEAKCRVDDPVYGCVGIIHLLKTQIQKTQNELAKTQAEIAVAQTKLSQTHISDFM
Protein: Probable ECA polymerase (P27835)
Organism: Escherichia coli (strain K12)
Function: Probably involved in the polymerization of enterobacterial common antigen (ECA) trisaccharide repeat units. Required for the assembly of the phosphoglyceride-linked form of ECA (ECA(PG)) and the water-soluble cyclic form of ECA (ECA(CYC)).
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01003, ECO:0000305}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01003}.
Interaction partners:
- Lipid III flippase
- Putative O-antigen transporter
- ECA polysaccharide chain length modulation protein
- Lipopolysaccharide biosynthesis protein WzxC
- TDP-N-acetylfucosamine:lipid II N-acetylfucosaminyltransferase
- UDP-N-acetyl-D-mannosaminuronic acid transferase
- Undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphate transferase
- Putative O-antigen polymerase
- UTP--glucose-1-phosphate uridylyltransferase
- Tyrosine-protein kinase wzc
Sequence:
MSLLQFSGLFVVWLLCTLFIATLTWFEFRRVRFNFNVFFSLLFLLTFFFGFPLTSVLVFRFDVGVAPPEILLQALLSAGCFYAVYYVTYKTRLRKRVADVPRRPLFTMNRVETNLTWVILMGIALVSVGIFFMHNGFLLFRLNSYSQIFSSEVSGVALKRFFYFFIPAMLVVYFLRQDSKAWLFFLVSTVAFGLLTYMIVGGTRANIIIAFAIFLFIGIIRGWISLWMLAAAGVLGIVGMFWLALKRYGMNVSGDEAFYTFLYLTRDTFSPWENLALLLQNYDNIDFQGLAPIVRDFYVFIPSWLWPGRPSMVLNSANYFTWEVLNNHSGLAISPTLIGSLVVMGGALFIPLGAIVVGLIIKWFDWLYELGNREPNRYKAAILHSFCFGAIFNMIVLAREGLDSFVSRVVFFIVVFGACLMIAKLLYWLFESAGLIHKRTKSSLRTQVEG
Protein: KSR (Q24170)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSSNNNAPASAPDTGSTNANDPISGSLSVDSNLVIIQDMIDLSANHLEGLRTQCAISSTLTQQEIRCLESKLVRYFSELLLAKMRLNERIPANGLVPHTTGNELRQWLRVVGLSQGTLTACLARLTTLEQSLRLSDEEIRQLLADSPSQREEEELRRLTRAMQNLRKCMESLESGTAASNNDPEQWHWDSWDRPTHIHRGSVGNIGLGNNSTASPRTHHRQHGVKGKNSALANSTNFKSGRQSPSATEELNSTQGSQLTLTLTPSPPNSPFTPSSGLSSSLNGTPQRSRGTPPPARKHQTLLSQSHVQVDGEQLARNRLPTDPSPDSHSSTSSDIFVDPNTNASSGGSSSNVLMVPCSPGVGHVGMGHAIKHRFTKALGFMATCTLCQKQVFHRWMKCTDCKYICHKSCAPHVPPSCGLPREYVDEFRHIKEQGGYASLPHVHGAAKGSPLVKKSTLGKPLHQQHGDSSSPSSSCTSSTPSSPALFQQRERELDQAGSSSSANLLPTPSLGKHQPSQFNFPNVTVTSSGGSGGVSLISNEPVPEQFPTAPATANGGLDSLVSSSNGHMSSLIGSQTSNASTAATLTGSLVNSTTTTSTCSFFPRKLSTAGVDKRTPFTSECTDTHKSNDSDKTVSLSGSASTDSDRTPVRVDSTEDGDSGQWRQNSISLKEWDIPYGDLLLLERIGQGRFGTVHRALWHGDVAVKLLNEDYLQDEHMLETFRSEVANFKNTRHENLVLFMGACMNPPYLAIVTSLCKGNTLYTYIHQRREKFAMNRTLLIAQQIAQGMGYLHAREIIHKDLRTKNIFIENGKVIITDFGLFSSTKLLYCDMGLGVPHNWLCYLAPELIRALQPEKPRGECLEFTPYSDVYSFGTVWYELICGEFTFKDQPAESIIWQVGRGMKQSLANLQSGRDVKDLLMLCWTYEKEHRPQFARLLSLLEHLPKKRLARSPSHPVNLSRSAESVF
Protein: Calsenilin (A-type potassium channel modulatory protein 3) (DRE-antagonist modulator) (DREAM) (Kv channel-interacting protein 3) (KChIP3) (Q9QXT8)
Organism: Mus musculus (Mouse)
Function: Calcium-dependent transcriptional repressor that binds to the DRE element of genes including PDYN and FOS. Affinity for DNA is reduced upon binding to calcium and enhanced by binding to magnesium. Seems to be involved in nociception.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22311982}. Cell membrane {ECO:0000250|UniProtKB:Q9Y2W7}; Lipid-anchor. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9Y2W7}. Golgi apparatus {ECO:0000250|UniProtKB:Q9Y2W7}. Nucleus {ECO:0000250|UniProtKB:Q9Y2W7}. Note=The sumoylated form is present only in the nucleus. In the presence of PSEN2, associated with the endoplasmic reticulum and Golgi. {ECO:0000250|UniProtKB:Q9Y2W7}.
Interaction partners:
- A-type voltage-gated potassium channel KCND2
- Voltage-gated potassium channel KCNC1
- A-type voltage-gated potassium channel KCND3
- A-type voltage-gated potassium channel KCND1
- Presenilin-2
- Inactive dipeptidyl peptidase 10
- Potassium voltage-gated channel subfamily A member 4
Sequence:
MQRTKEAVKASDGNLLGDPGRIPLSKRESIKWQRPRFTRQALMRCCLIKWILSSAAPQGSDSSDSELELSTVRHQPEGLDQLQAQTKFTKKELQSLYRGFKNECPTGLVDEDTFKLIYSQFFPQGDATTYAHFLFNAFDADGNGAIHFEDFVVGLSILLRGTVHEKLKWAFNLYDINKDGCITKEEMLAIMKSIYDMMGRHTYPILREDAPLEHVERFFQKMDRNQDGVVTIDEFLETCQKDENIMNSMQLFENVI
Protein: Flotillin-like protein 1 (AtFLOT1) (Nodulin-like protein 1) (Q501E6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May act as a scaffolding protein within caveolar membranes, functionally participating in formation of caveolae or caveolae-like vesicles.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Membrane, caveola {ECO:0000269|PubMed:15618420}.
Interaction partners:
- Protein DMP1
- Plant intracellular Ras-group-related LRR protein 2
- Hypersensitive-induced response protein 4
- B3 domain-containing protein REM6
- B3 domain-containing protein REM1
- soluble epoxide hydrolase
- Remorin
- Uncharacterized GPI-anchored protein At5g19250
- Ammonium transporter 1 member 3
- Remorin 1.4
Sequence:
MFKVARASQYLAITGAGIEDIKLSKKSWVFPWQSCTVFDVSPVNYTFKVQAMSAEKLPFVLPAVFTIGPRVDDDDALILYARLISPHDKDSNHVHELVEGVIEGETRVLAASMTMEEIFKGTKEFKKEVFDKVQLELNQFGLVIYNANVKQLVDVPGHEYFSYLGQKTQMEAANQARIDVSEAKMKGEIGAKERTGLTLQNAAKIDAESKIISMQRQGEGTKEEIKVRTEVKVFENQKEADVAKANAELAMKKAAWTKDAQVAEVEATKAVALREAELQTQVEKMNALTRTEKLKAEFLSKASVEYETKVQEANWELYNKQKQAEAVLYEKQKQAEAQKAQADAAFYSKQKEAEGLVALASAQGTYLRTLLDAVQNDYSCLRDFLMINNGIYQEIAKTNAMAVRDLQPKISVWNHGGEQGGGSGNAMKDIAGLYKMLPPVLDTVYEQTGMQPPAWIGTLRGAEPKQVTRS
Protein: Peroxisomal membrane protein PEX13 (Peroxin-13) (Q92968)
Organism: Homo sapiens (Human)
Function: Component of the PEX13-PEX14 docking complex, a translocon channel that specifically mediates the import of peroxisomal cargo proteins bound to PEX5 receptor. The PEX13-PEX14 docking complex forms a large import pore which can be opened to a diameter of about 9 nm (By similarity). Mechanistically, PEX5 receptor along with cargo proteins associates with the PEX14 subunit of the PEX13-PEX14 docking complex in the cytosol, leading to the insertion of the receptor into the organelle membrane with the concomitant translocation of the cargo into the peroxisome matrix. Involved in the import of PTS1- and PTS2-type containing proteins.
Subcellular location: Peroxisome membrane {ECO:0000269|PubMed:11390669, ECO:0000269|PubMed:8858165}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Peroxisomal biogenesis factor 19
- Peroxisomal membrane protein PEX14
- Peroxisomal targeting signal 1 receptor
- Peroxisome assembly protein 12
- Peroxisome biogenesis factor 10
- Peroxisomal targeting signal 2 receptor
- Peroxisome biogenesis factor 2
- Peroxisomal biogenesis factor 3
- Peroxisomal ATPase PEX6
- Peroxisomal membrane protein PEX16
Sequence:
MASQPPPPPKPWETRRIPGAGPGPGPGPTFQSADLGPTLMTRPGQPALTRVPPPILPRPSQQTGSSSVNTFRPAYSSFSSGYGAYGNSFYGGYSPYSYGYNGLGYNRLRVDDLPPSRFVQQAEESSRGAFQSIESIVHAFASVSMMMDATFSAVYNSFRAVLDVANHFSRLKIHFTKVFSAFALVRTIRYLYRRLQRMLGLRRGSENEDLWAESEGTVACLGAEDRAATSAKSWPIFLFFAVILGGPYLIWKLLSTHSDEVTDSINWASGEDDHVVARAEYDFAAVSEEEISFRAGDMLNLALKEQQPKVRGWLLASLDGQTTGLIPANYVKILGKRKGRKTVESSKVSKQQQSFTNPTLTKGATVADSLDEQEAAFESVFVETNKVPVAPDSIGKDGEKQDL
Protein: Ankyrin 2 (A0A5F9ZH18)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MNGNTALAIAKRLGYISVVDTLKVVTEEVTTTTTTITEKHKLNVPETMTEVLDVSDEEGDDTMTGDGGEYLRPEDLKELGDDSLPSSQFLDGMNYLRYSLEGGRSDSLRSFSSDRSHTLSHASYLRDSAVMDDSVVIPSHQVSTLAKEAERNSYRLSWGTENLDNVALSSSPIHSGFLVSFMVDARGGAMRGCRHNGLRIIIPPRKCTAPTRVTCRLVKRHRLATMPPMVEGEGLASRLIEVGPSGAQFLGPVIVEIPHFAALRGKERELVVLRSENGDSWKEHFCDYTEDELNEILNGMDEVLDSPEDLEKKRICRIITRDFPQYFAVVSRIKQDSNLIGPEGGVLSSTVVPQVQAVFPEGALTKRIRVGLQAQPMHSELVKKILGNKATFSPIVTLEPRRRKFHKPITMTIPVPKASSDVMLNGFGGDAPTLRLLCSITGGTTPAQWEDITGTTPLTFVNECVSFTTNVSARFWLIDCRQIQESVTFASQVYREIICVPYMAKFVVFAKSHDPIEARLRCFCMTDDKVDKTLEQQENFAEVARSRDVEVLEGKPIYVDCFGNLVPLTKSGQHHIFSFFAFKENRLPLFVKVRDTTQEPCGRLSFMKEPKSTRGLVHQAICNLNITLPIYTKESESDQEQEEEIDMTSEKNPQDEQERIEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIVHLMETNTEPLQERISHSYAEIEQTITLDHSEGFSVLQEELCTAQHKQKEEQAVSKESETCDHPPIVSEEDISVGYSTFQDGVPKTEGDSSATALFPQTHKEQVQQDFSGKMQDLPEESSLEYQQEYFVTTPGTETSETQKAMIVPSSPSKTPEEVSTPAEEEKLYLQTPTSSERGGSPIIQEPEEPSEHREESSPRKTSLVIVESADNQPETCERLDEDAAFEKGDDMPEIPPETVTEEEYIDEHGHTVVKKVTRKIIRRYVSSEGTEKEEIMVQGMPQEPVNIEEGDGYSKVIKRVVLKSDTEQSEVTLCEPSILSSTSQFQAEPVEGRRVSKVVKTTVVLGERMEKHLGDSSLATDLPSAKDDFEEDNNE
Protein: Uncharacterized protein C24C9.04 (O13964)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 4
- Mediator of RNA polymerase II transcription subunit 21
- Mediator of RNA polymerase II transcription subunit 14
- DNA-directed RNA polymerase II subunit rpb1
- Mediator of RNA polymerase II transcription subunit 7
- Mediator of RNA polymerase II transcription subunit 10
- DNA-directed RNA polymerases I, II, and III subunit RPABC4
- DNA-directed RNA polymerase II subunit rpb4
- Mediator of RNA polymerase II transcription subunit 11
- Mediator of RNA polymerase II transcription subunit 31
Sequence:
MDPAHHIKDTSAELLSQQDFSILQSRLLEFLASQEARETVTASKELTLLRQGIRQLKEKVSKMEPEEMTVKEKKSIIEILKARIALKKAFLKMALSESNDTVVKKEDVRESPVDTFMENAT
Protein: L-tryptophan decarboxylase (EC 4.1.1.105) (Psilocybin biosynthesis decarboxylase) (P0DPA6)
Organism: Psilocybe cubensis (Psychedelic mushroom) (Stropharia cubensis)
Function: L-tryptophan decarboxylase; part of the gene cluster that mediates the biosynthesis of psilocybin, a psychotropic tryptamine-derived natural product. The first step in the pathway is the decarboxylation of L-tryptophan to tryptamine by the decarboxylase psiD. 4-hydroxy-L-tryptophan is accepted as substrate by psiD as well. The cytochrome P450 monooxygenase psiH then converts tryptamine to 4-hydroxytryptamine. The kinase psiK catalyzes the 4-O-phosphorylation step by converting 4-hydroxytryptamine into norbaeocystin. The methyltransferase psiM then catalyzes iterative methyl transfer to the amino group of norbaeocystin to yield psilocybin via a monomethylated intermediate, baeocystin. 4-hydroxy-6-methyl-l-tryptophancan also be converted the decarboxylase PsiD, kinase PsiK, and methyltransferase PsiM into respectively 6-methyl-norbaeocystin, 6-methylbaeocystin, and 6-methylpsilocybin.
Interaction partners:
Sequence:
MQVIPACNSAAIRSLCPTPESFRNMGWLSVSDAVYSEFIGELATRASNRNYSNEFGLMQPIQEFKAFIESDPVVHQEFIDMFEGIQDSPRNYQELCNMFNDIFRKAPVYGDLGPPVYMIMAKLMNTRAGFSAFTRQRLNLHFKKLFDTWGLFLSSKDSRNVLVADQFDDRHCGWLNERALSAMVKHYNGRAFDEVFLCDKNAPYYGFNSYDDFFNRRFRNRDIDRPVVGGVNNTTLISAACESLSYNVSYDVQSLDTLVFKGETYSLKHLLNNDPFTPQFEHGSILQGFLNVTAYHRWHAPVNGTIVKIINVPGTYFAQAPSTIGDPIPDNDYDPPPYLKSLVYFSNIAARQIMFIEADNKEIGLIFLVFIGMTEISTCEATVSEGQHVNRGDDLGMFHFGGSSFALGLRKDCRAEIVEKFTEPGTVIRINEVVAALKA
Protein: Distal-less homeobox 1 isoform A (X5D2F9)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MTMTTMPESLNSPVSGKAVFMEFGPPNQQMSPSPMSHGHYSMHCLHSAGHSQPDGAYSSASSFSRPLGYPYVNSVSSHASSPYISSVQSYPGSASLAQSRLEDPGADSEKSTVVEGGEVRFNGKGKKIRKPRTIYSSLQLQALNRRFQQTQYLALPERAELAASLGLTQTQVKIWFQNKRSKFKKLMKQGGAALEGSALANGRALSAGSPPVPPGWNPNSSSGKGSGGNAGSYIPSYTSWYPSAHQEAMQQPQLM
Protein: E3 ubiquitin-protein ligase MARCHF7 (EC 2.3.2.27) (Axotrophin) (Membrane-associated RING finger protein 7) (Membrane-associated RING-CH protein VII) (MARCH-VII) (RING-type E3 ubiquitin transferase MARCHF7) (Q9WV66)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin-protein ligase which may specifically enhance the E2 activity of HIP2. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates (By similarity). May be involved in T-cell proliferation by regulating LIF secretion. May play a role in lysosome homeostasis (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9H992}.
Interaction partners:
- F-box/LRR-repeat protein 2
Sequence:
MESKPSRIPRRISVQPSGSLSTRMVSGNRGTSLNDSYHSRDSSFRLDSEYQSASASACASPCQPAWYSESEIPQGARARAQTQQRDHDSKRPKLSCTNCASTSAGRNGGSGLNTVSDSSWRHSQVPRSSSMVLGSFGTDLMRERRDLDRRRESSISNLMDYNHRSGDFTTSSYVQERVPSSYSQGARPKENAVSTLQLNSSSTNHQLPSDHQTVPSSRDSSRSSFRSHFSPRQSESFRNSSHPAFSYFSSRNETPTISNSERGSSQRPYRESSDNEGRRTTRRLLSRIASSMSSTFFSRRSSQDSLNTRSLSSENYISPRTLTSQSRNNGTSSSSDVSEGRAAEASQGFRFLRRRWGLSSLSQNHSSEPEAENFNQESEGRNSGPWLSSSLRNRCTPLFSRRRREGRDESSRMSTSDVPPRSHIFRRDSNEVVHLEAQGDSLGAAANRPQASGASSSAAAGGSTPELPQGGRNPGLTGILPGSLFRFAVPPALGSNLADNVMITVDIIPSGWNSTDGKNDKAKSAPSRDPEKLQKIKESLLLEDSDDEEEGDLCRICQMAAASSSNLLIEPCKCTGSLQYVHQECMKKWLQAKINSGSSLEAVTTCELCKEKLQLNLEDFDIHELHRAHANEQAEYEFISSGLYLVVLLHLCEQSFSDMMGNTIEPSTRVRFINLARTLQAHMEDLETSEDEF
Protein: Coiled-coil domain-containing protein 80 (Up-regulated in BRS-3 deficient mouse) (Q8R2G6)
Organism: Mus musculus (Mouse)
Function: Promotes cell adhesion and matrix assembly.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:15325258, ECO:0000269|PubMed:18757743}.
Interaction partners:
- Ubiquitin-like protein FUBI
Sequence:
MMWKMGPHFTTLLAMWLVCGSASHSPALDSDSHTGRKVPLVSPISSRSARYLRHTGRSGGVEKSTQEEPNPQPFQRRKSVPVLRLAHPTMRPPPSGINGVPVRPEVRPIARSSAREMVRDEGSSARTRMLRFPSGSSSPNILASFAGKNRVWVISAPHASEGYYRLMMSLLKDDVYCELAERHIQQIVLFHQAGEEGGKVRRITNEGQILEQPLDPNLIPKLMSFLKLEKGKFSMVLLKKTLQVEERYPYPVRLEAMYEVIDQGPIRRIEKIRQKGFVQKCKASGIEGHVVQEGNEGGGGAGGTGLGGDKRKEDPRRTQVHPTREAPRKQATSKAATPQPPPTPRATTLPPAPVTTATRATSRVVTIAARPTTTTAYPATQRPWTSRLHPFSVSHRPPATAEVTTARGPSVSEQLYPLPRKEQQREKPQATRRPSKATNYGSFTATPPPTLWEVSARVVGTSRFRDNRTDKREHGHQDPNAVPGPHKPVKGKLPKKKDRILSNEYEDKYDLSQPTSSQGEEERQVDSVPSQNAKESKKLEKLEKPEKEKKKKGKSAKQDKLLKSEKQAKKAEKKTKQEKDKNKKKKAGKTEQDDNQKPTAKHLAPSPKKSVADLLGSFEGKRRLLLITTPKAENNMYVQQRDEYLESFCKMATRRISVVTIFGPVNNSSMKIDHFQLDNEKPMRVVDDDDLVDQHLISELRKEYGMTYDDFFMVLTDVDLRVKQYYEVPIAMKSVFDLIDTFQSRIKDMEKQKKEGIACKEDKRQSLENFLSRFRWRRRLLVISAPNDEDWAYSQQLSALNGQACNFGLRHITILKLLGVGEEVGGVLELFPINGSSIVEREDVPAHLVKDIRNYFQVSPEYFSMLLVGKDGNVKSWYPSPMWSMVIVYDLIDSMQLRRQEMAIQQSLGMRCPEDEYAGYGYHSYHQGYQDGYQDDYRHHESYHHGYPY