wanglab/gogpt-training-data huggingface dataset:
Protein: Nucleoporin NUP35 (35 kDa nucleoporin) (Nuclear pore complex protein Nup53) (Nucleoporin NUP53) (Q68FY1)
Organism: Rattus norvegicus (Rat)
Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. May play a role in the association of MAD1 with the NPC (By similarity).
Subcellular location: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q8NFH5}. Nucleus membrane {ECO:0000250|UniProtKB:Q8NFH5, ECO:0000269|PubMed:15703211}; Peripheral membrane protein {ECO:0000269|PubMed:15703211}. Note=Tightly associated with the nuclear membrane and lamina. {ECO:0000250|UniProtKB:Q8NFH5}.
Interaction partners:
- Nuclear pore complex protein Nup155
- Nucleoporin 205
- Nucleoporin NUP188
- Nuclear pore complex protein Nup93
- Nuclear pore complex protein Nup98-Nup96
- Nucleoporin NDC1
- Nuclear pore complex protein Nup88
- Nuclear pore complex protein Nup107
- Nuclear pore complex protein Nup153
- Nuclear pore complex protein Nup85
Sequence:
MAAFAVDPQAPTLGSEPMMLGSPTSPKPGANAQFLPGFLMGDLPAPVTPQPRSISGPSVGVMEMRSPLLAGGSPPQPVVPAHKDKSGAPPVRSIYDDISSPGLGSTPLPSRRQANISVLQSPLVGVTTPVTGQSMFSPANIGQPRKTTLSPAQLDPFYTQGDSLTSEDHLDDTWVTVFGFPQASASYILLQFAQYGNILKHVMSNTGNWMHIRYQSKLQARKALSKDGRIFGESIMIGVKPCIDKNVMENSDRGVLSSPSLAFTPPIRTLGTPTQPGSTPRVSTMRPLATAYKASTSDYQVISDRQTPKKDESLVSRAMEYMFGW
Protein: Chloride intracellular channel protein 6 (Glutaredoxin-like oxidoreductase CLIC6) (EC 1.8.-.-) (Q811Q2)
Organism: Rattus norvegicus (Rat)
Function: May insert into membranes and form chloride ion channels. May play a critical role in water-secreting cells, possibly through the regulation of chloride ion transport (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000305|PubMed:14499480}; Single-pass membrane protein {ECO:0000305|PubMed:14499480}. Note=Predominantly cytoplasmic. Upon chloride ion efflux from the cell, it is translocated to the plasma membrane (By similarity). Colocalizes with DRD3 at the plasma membrane. {ECO:0000250}.
Interaction partners:
Sequence:
MAEATEPKEVSSGSQGQPEGAVIEGPGEPGAADLEGREASEGAAEAPRDLGEGAEAMASGKEEGGCGQDGEIGEVQAQDPRPGPGTETPGTSGAPGEAEAAECDSEGALIPQSGGGAKRQQVQGTSSGLDAQGEAPEVPEDARREPEDPKASEAGEEAESGQEALGGSAPESQINPEVQGPVGDNMDTEAPAGEPQGSEGEPQGGGESSPQPQDEAIEIAAAEVGGHEPGELAGASAADAKGEGETLRKDGFEEAAPEEARVDSGENGFEEAAPEEARVDSGENRDQGRLQEETGEEEARPESGLKGPCEEAIQEKAPDGSLDGEEAKSTGHEESQVELSNHLAEETSAQGGEELGRVNGRRENGPASEEGDLGQEHDITLFVKAGSDGESIGNCPFSQRLFMILWLKGVIFNVTTVDLKRKPADLQNLAPGTNPPFMTFDGEVKTDVNKIEEFLEEKLVPPRYPKLGTQHPESNSAGNDVFAKFSAFIKNTKKDANDIYEKNLLRALKKLDSYLNSPLPDEIDAYSTEDVTVSQRKFLDGDELTLADCNLLPKLHIIKIVAKKYRGFEFPSEMTGIWRYLNNAYARDEFTNTCPADQEIEHAYSDAAKRMK
Protein: EGF-like-domain, multiple 6 (Epidermal growth factor-like protein 6 isoform 2) (Q6DHG1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Saccharopine dehydrogenase b.
- Rhomboid-related protein 1
- WD repeat-containing protein 90
Sequence:
MSGLGVCRYGSRLECCYGWKKNTKGQCEAQCDLGCKHGECVGPNKCKCFPGYTGKTCSQDLNECGLKPRPCEHRCMNTFGSYMCYCLNGYMLMPDGSCANSRTCSLAHCQYGCEEVQSEVRCLCPSPGLQLGSDGKTCEDIDECATGKNQCPFNRQCTNTFGSYYCKCQPGYDLKYINGKYDCVDVNECTSNTHKCSHHAECINTLGSYKCKCKQGFRGSGFDCSVKPFYHRSWDSSKGNTDVLVNAIPDFPSKTRILGKFENSIPEPVLTESPRQHLQPFDYDGEVYIGAPQETPVFPEEEEVEEEEEEDTENQLEDEELTSRGDVFSQDDFVSFYQSELELKEIQAAPLKERFLTDCDFDRGACEWVQDNADDLDWTIKYHPDGREYYLALEGPVGNRREQARMKLLLEDHMRQSSFCLRFDFRIEGPQTGVLRVKLDNSAISIWERKQSQKQSWQSEQISISWTDSNPEAVVFEAERGRSGTGEIALDHVLLISGECSEDKTLDF
Protein: Protein PAXX (Paralog of XRCC4 and XLF) (Q8K0Y7)
Organism: Mus musculus (Mouse)
Function: Non-essential DNA repair protein involved in DNA non-homologous end joining (NHEJ); participates in double-strand break (DSB) repair and V(D)J recombination. May act as a scaffold required for accumulation of the Ku heterodimer, composed of XRCC5/Ku80 and XRCC6/Ku70, at double-strand break sites and promote the assembly and/or stability of the NHEJ machinery. Involved in NHEJ by promoting the ligation of blunt-ended DNA ends (By similarity). Together with NHEJ1/XLF, collaborates with DNA polymerase lambda (POLL) to promote joining of non-cohesive DNA ends (By similarity). Constitutes a non-essential component of classical NHEJ: has a complementary but distinct function with NHEJ1/XLF in DNA repair.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9BUH6}. Chromosome {ECO:0000250|UniProtKB:Q9BUH6}. Note=Predominantly localizes to the nucleus. Accumulates at sites of DNA damage generated by laser microirradiation. {ECO:0000250|UniProtKB:Q9BUH6}.
Interaction partners:
- Non-homologous end-joining factor 1
- DNA repair protein XRCC4
- X-ray repair cross-complementing protein 6
- X-ray repair cross-complementing protein 5
- DNA-dependent protein kinase catalytic subunit
- DNA ligase 4
- TP53-binding protein 1
- Serine-protein kinase ATM
- E3 ubiquitin-protein ligase RNF168
- DNA repair protein XRCC1
Sequence:
MAPPLLSLPLCILPPGSGSPRLVCYCERDSGGDGDRDDFNLYVTDAAELWSTCFSPDSLARLKARFGLSGAEDIHSRFRAACQQQAVTVSLQEDRALITLSGDTPALAFDLSKVPSPEAAPRLQALTLSLAEHVCNLERRLAAAEETITSPKKNTQPAGTQFLPELDHQRGSSGPGVRRRCPGESLINPGFKSKKPAAGVDFDET
Protein: Uncharacterized protein At4g18630 (Q8GYP4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MEGKKLNLYAPLPSIRRIPSMIERSSELENKKTTITRPELRSCPSTKQETPVFVLPDQSFDHLTEPASIPFMWEQIPGKPKDDMATLIQESGLLETDDEEEDEVDEDLDTVSSNVSFSVNCSTSGVSEIEKTGERSDCDEKSRESLDLMMSRFLPAAKAMALQTHQKHQSSYNSSEQKLITQNREALVARQRSQLVAEHEHFAIVQSLYDDLNIDDDTEDDENDDDGDDYGHVDHKIYPAEVTKKACGFLPRLCAKNSFKFLNPVPLDSVSNRSMKHSGDQTSLPNWSTRRLSGFISPYRTSCSDSGFLGTPEKPESFKRLNRGISKSQELYPTRTRREVLPNYSNSGEIKMFRNSISTPSRIQRTTIHDSRFLVEEVNRRRNNKSGNLQQTSSEYTPALSPPPLPETPSRSWLGRTLLPPVNPRPYGVVLGQVGIKKLNQEVLESTKWETIVKTSYVHNDHARYSQELIVYPSRQQNT
Protein: Probable 26S proteasome non-ATPase regulatory subunit 3 (26S proteasome subunit S3) (Diphenol oxidase A2 component) (DOX-A2) (Regulatory particle non-ATPase 3) (P25161)
Organism: Drosophila melanogaster (Fruit fly)
Function: Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.
Interaction partners:
- 26S proteasome regulatory complex subunit p50
- 26S proteasome regulatory subunit 7
- 26S proteasome non-ATPase regulatory subunit 1
- 26S proteasome non-ATPase regulatory subunit 11
- 26S proteasome non-ATPase regulatory subunit 4
- 26S proteasome regulatory subunit 8
- 26S proteasome non-ATPase regulatory subunit 8
- 26S proteasome regulatory subunit 8
- 26S proteasome non-ATPase regulatory subunit 7
- 26S proteasome regulatory subunit 4
Sequence:
MTNATDIGANDVEMEVDPTAETLADEKKNQDVAAVQEIREQIRQIEKGVASKESRFILRVLRNLPNTRRKLNGVVFRNLAQSIYPAGADREAAVALMPAVEKDATELPDVPKKQVATKAPIAEVDAYFYLLLLVKLIDASDLKRAGISADALMAKISIQNRRTLDLIGAKSYFYFSRVAELKNSLEGIRSFLHARLRTATLRNDFEGQAVLINCLLRNYLHYALYDQADKLVKKSVYPESASNNEWARFLYYLGRIKAAKLEYSDAHKHLVQALRKSPQHAAIGFRQTVQKLIIVVELLLGNIPERVVFRQAGLRQSLGAYFQLTQAVRLGNLKRFGDVVSQYGPKFQLDHTFTLIIRLRHNVIKTAIRSIGLSYSRISPQDIAKRLMLDSAEDAEFIVSKAIRDGVIEATLDPAQNFMRSKESTDIYSTREPQLAFHERISFCLNLHNQSVKAMRYPPKSYGKDLESAEERREREQQDLELAKEMAEDDEDGF
Protein: Small ribosomal subunit protein eS27z (40S ribosomal protein S27-1) (O64650)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Small ribosomal subunit protein eS28x
- Small ribosomal subunit protein uS15z
- Small ribosomal subunit protein eS10z
- Small ribosomal subunit protein uS15y
- Small ribosomal subunit protein uS14z/uS14y/uS14x
- Small ribosomal subunit protein uS3z
- Small ribosomal subunit protein eS30z/eS30y/eS30x
- Small ribosomal subunit protein uS13z/uS13y/uS13x
- Small ribosomal subunit protein eS6z
- Small ribosomal subunit protein eS21z
Sequence:
MVLQNDIDLLNPPAELEKRKHKLKRLVQSPNSFFMDVKCQGCFNITTVFSHSQTVVMCGNCQTLLCTPTGGKAKLTEGCSFRKK
Protein: Zinc finger protein 541 (Q9H0D2)
Organism: Homo sapiens (Human)
Function: Component of some chromatin remodeling multiprotein complex that plays a role during spermatogenesis.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q0GGX2, ECO:0000255|PROSITE-ProRule:PRU00512, ECO:0000255|PROSITE-ProRule:PRU00624}.
Interaction partners:
- Deoxynucleotidyltransferase terminal-interacting protein 1
Sequence:
MDQYSLGDEGALPSEMHLPSFSESQGLNCSDTLNRDLGPNTRGFLYAGLSGLDPDPSLPTPDMSSEVLEDNLDTLSLYSGKDSDSVKLLEEYADSESQASLQDLGLGVLKAKEADEGGRATSGSARKGKRQHSSPQNPLLDCSLCGKVFSSASSLSKHYLTHSQERKHVCKICSKAFKRQDHLTGHMLTHQKTKPFVCIEQGCSKSYCDYRSLRRHYEVHHGLCILKEAPPEEEACGDSPHAHESAGQPPPSSLRSLVPPEARSPGSLLPHRDLLRRIVSSIVHQKTPSPGPAPAGASDSEGRNTACPCPASSGSSSCTPAGPHAAPAALDTELPEEPCLPQKEPATDVFTAPNSRAAENGAPDPPEPEPDTALLQARSTAECWPEGGSVPACLPLFRGQTVPASSQPSSHSFQWLRNLPGCPKSKGNNVFVVHKPSAVPSREGSESGPGPSSGSPSEESPPGPGGGLEDALPFPAALLRVPAEAPSDPRSASGEDDPCAPKKVKVDCDSFLCQNPGEPGLQEAQKAGGLPADASPLFRQLFLKSQEPLVSHEQMQVFQMITKSQRIFSHAQVAAVSSQLPAPEGKPAALRPLQGPWPQQPPPLAPAVDSLHAGPGNPEAEGSPARRRKTTPGVPREASPGSTRRDAKGGLKVAAVPTPLAAPSLDPSRNPDISSLAKQLRSSKGTLDLEDIFPSTGQRQTQLGGEEPPGASLPGKQAPAENGAASRITKGEKGPACSRGGGYRLLGNPRAPRFSGFRKEKAKMDMCCAASPSQVAMASFSSAGPPADPSKSKLTIFSRIQGGNIYRLPHPVKEENVAGRGNQQNGSPTDWTKPRSTFVCKNCSQMFYTEKGLSSHMCFHSDQWPSPRGKQEPQVFGTEFCKPLRQVLRPEGDRHSPPGTKKPLDPTAAAPLVVPQSIPVVPVTRHIGSMAMGQEKDGEERDSKESSQQRKRKKRPPPSTAGEPGPAGCHQSRLRSPMFLVDCLLKGLFQCSPYTPPPMLSPIREGSGVYFNTLCSTSTQASPDQLISSMLDQVDGSFGICVVKDDTKISIEPHINIGSRFQAEIPELQERSLAGTDEHVASLVWKPWGDMMISSETQDRVTELCNVACSSVMPGGGTNLELALHCLHEAQGNVQVALETLLLRGPHKPRTHLLADYRYTGSDVWTPIEKRLFKKAFYAHKKDFYLIHKMIQTKTVAQCVEYYYIWKKMIKFDCGRAPGLEKRVKREPEEVERTEEKVPCSPRERPSHHPTPKLKTKSYRRESILSSSPNAGSKRTPELLGSAESQGIFPCRECERVFDKIKSRNAHMKRHRLQDHVEPIIRVKWPVKPFQLKEEELGADIGPLQW
Protein: Fumarylacetoacetase (FAA) (EC 3.7.1.2) (Beta-diketonase) (Fumarylacetoacetate hydrolase) (P16930)
Organism: Homo sapiens (Human)
Interaction partners:
- Maleylacetoacetate isomerase
- 4-hydroxyphenylpyruvate dioxygenase
- Oxaloacetate tautomerase FAHD1, mitochondrial
- Homogentisate 1,2-dioxygenase
- Tyrosine aminotransferase
- Fumarate hydratase, mitochondrial
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Succinate dehydrogenase cytochrome b560 subunit, mitochondrial
- Succinate dehydrogenase cytochrome b small subunit, mitochondrial
Sequence:
MSFIPVAEDSDFPIHNLPYGVFSTRGDPRPRIGVAIGDQILDLSIIKHLFTGPVLSKHQDVFNQPTLNSFMGLGQAAWKEARVFLQNLLSVSQARLRDDTELRKCAFISQASATMHLPATIGDYTDFYSSRQHATNVGIMFRDKENALMPNWLHLPVGYHGRASSVVVSGTPIRRPMGQMKPDDSKPPVYGACKLLDMELEMAFFVGPGNRLGEPIPISKAHEHIFGMVLMNDWSARDIQKWEYVPLGPFLGKSFGTTVSPWVVPMDALMPFAVPNPKQDPRPLPYLCHDEPYTFDINLSVNLKGEGMSQAATICKSNFKYMYWTMLQQLTHHSVNGCNLRPGDLLASGTISGPEPENFGSMLELSWKGTKPIDLGNGQTRKFLLDGDEVIITGYCQGDGYRIGFGQCAGKVLPALLPS
Protein: Protein windbeutel (Erp29 homolog) (O44342)
Organism: Drosophila melanogaster (Fruit fly)
Function: Probable chaperone protein involved in dorsoventral axis patterning in early embryos. Probably acts by folding and targeting pipe (pip) into the Golgi.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138}.
Interaction partners:
- Protein disulfide-isomerase A6 homolog
- Thioredoxin domain-containing protein 5 homolog
- Protein disulfide-isomerase
- Ero1-like protein
- IP08350p
Sequence:
MMHILVTLLLVAIHSIPTTWAVTCTGCVDLDELSFEKTVERFPYSVVKFDIAYPYGEKHEAFTAFSKSAHKATKDLLIATVGVKDYGELENKALGDRYKVDDKNFPSIFLFKGNADEYVQLPSHVDVTLDNLKAFVSANTPLYIGRDGCIKEFNEVLKNYANIPDAEQLKLIEKLQAKQEQLTDPEQQQNARAYLIYMRKIHEVGYDFLEEETKRLLRLKAGKVTEAKKEELLRKLNILEVFRVHKVTKTAPEKEEL
Protein: Prenylated Rab acceptor protein 1 (PRA1 family protein 1) (Prenylin) (Q9Z0S9)
Organism: Mus musculus (Mouse)
Function: General Rab protein regulator required for vesicle formation from the Golgi complex. May control vesicle docking and fusion by mediating the action of Rab GTPases to the SNARE complexes. In addition it inhibits the removal of Rab GTPases from the membrane by GDI1 (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:O35394}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:O35394}. Golgi apparatus {ECO:0000250|UniProtKB:O35394}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250|UniProtKB:O35394}. Note=According to PubMed:11535589, it is an integral membrane protein, while other authors showed that it is cytoplasmic and membrane-associated to Golgi and synaptic vesicles. {ECO:0000250|UniProtKB:O35394}.
Interaction partners:
- Plasminogen
- Protein YIF1A
Sequence:
MAAQKDQQKDAEGEGLSATTLLPKLIPSGAGREWLERRRATIRPWGTFVDQQRFSRPRNVGELCQRLVRNVEYYQSNYVFVFLGLILYCVVTSPMLLVALAVFFGACYILYLRTLQSKLVLFGREVSPAHQYALAGGVSFPFFWLAGAGSAVFWVLGATLVLIGSHAAFHQMEPADGEELQMEPV
Protein: CDGSH iron-sulfur domain-containing protein 1 (Cysteine transaminase CISD1) (EC 2.6.1.3) (MitoNEET) (Q91WS0)
Organism: Mus musculus (Mouse)
Function: L-cysteine transaminase that catalyzes the reversible transfer of the amino group from L-cysteine to the alpha-keto acid 2-oxoglutarate to respectively form 2-oxo-3-sulfanylpropanoate and L-glutamate (By similarity). The catalytic cycle occurs in the presence of pyridoxal 5'-phosphate (PLP) cofactor that facilitates transamination by initially forming an internal aldimine with the epsilon-amino group of active site Lys-55 residue on the enzyme (PLP-enzyme aldimine), subsequently displaced by formation of an external aldimine with the substrate amino group (PLP-L-cysteine aldimine). The external aldimine is further deprotonated to form a carbanion intermediate, which in the presence of 2-oxoglutarate regenerates PLP yielding final products 2-oxo-3-sulfanylpropanoate and L-glutamate. The proton transfer in carbanion intermediate is suggested to be controlled by the active site lysine residue, whereas PLP stabilizes carbanion structure through electron delocalization, also known as the electron sink effect (By similarity). Plays a key role in regulating maximal capacity for electron transport and oxidative phosphorylation. May be involved in iron-sulfur cluster shuttling and/or in redox reactions. Can transfer the [2Fe-2S] cluster to an apo-acceptor protein only when in the oxidation state, likely serving as a redox sensor that regulates mitochondrial iron-sulfur cluster assembly and iron trafficking upon oxidative stress (By similarity).
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:17376863}; Single-pass type III membrane protein {ECO:0000269|PubMed:17376863}.
Interaction partners:
- CDGSH iron-sulfur domain-containing protein 3, mitochondrial
- NADH dehydrogenase iron-sulfur protein 5
Sequence:
MGLSSNSAVRVEWIAAVTFAAGTAALGYLAYKKFYAKENRTKAMVNLQIQKDNPKVVHAFDMEDLGDKAVYCRCWRSKKFPFCDGAHIKHNEETGDNVGPLIIKKKET
Protein: PAMP-induced secreted peptide 1 (Q1PE40)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Endogenous secreted peptide that acts as elicitor of immune response and positive regulator of defense response. Amplifies the immune response triggered by flg22, the active epitope of bacterial flagellin. Acts as negative regulator of root growth.
Subcellular location: Secreted, extracellular space, apoplast {ECO:0000269|PubMed:25188390}.
Interaction partners:
- Receptor-like protein kinase 7
- Probable aquaporin PIP1-4
- Aquaporin PIP1-2
- Probable aquaporin PIP2-8
- Probable aquaporin PIP2-5
- Probable aquaporin PIP1-5
- At2g23270
- Leucine-rich repeat receptor-like protein kinase PEPR2
- NAC domain-containing protein 91
- PAMP-induced secreted peptide 2
Sequence:
MRRVSWSTVLIVVVMVSLFFVEHVVVPAAAGRVLTEKSGDGSATMTVEKMKSTVDSWFQRLASGPSPRGRGH
Protein: Sulochrin halogenase gedL (EC 1.14.19.-) (Flavin-dependent halogenase gedL) (Geodin synthesis protein L) (Q0CCX4)
Organism: Aspergillus terreus (strain NIH 2624 / FGSC A1156)
Function: Sulochrin halogenase; part of the gene cluster that mediates the biosynthesis of geodin, an intermediate in the biosynthesis of other natural products. The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) gedC. The atrochrysone carboxyl ACP thioesterase gedB then breaks the thioester bond and releases the atrochrysone carboxylic acid from gedC. The atrochrysone carboxylic acid is then converted to atrochrysone which is further transformed into emodinanthrone. The next step is performed by the emodinanthrone oxygenase gedH that catalyzes the oxidation of emodinanthrone to emodin. Emodin O-methyltransferase encoded probably by gedA then catalyzes methylation of the 8-hydroxy group of emodin to form questin. Ring cleavage of questin by questin oxidase gedK leads to desmethylsulochrin via several intermediates including questin epoxide. Another methylation step probably catalyzed by methyltransferase gedG leads to the formation of sulochrin which is further converted to dihydrogeodin by the sulochrin halogenase gedL. Finally, the dihydrogeodin oxidase gedJ catalyzes the stereospecific phenol oxidative coupling reaction converting dihydrogeodin to geodin.
Interaction partners:
Sequence:
MSVPNKTTVLVIGGGPAGSYAAAVLARENVDTVLLEAEKFPRYHIGESMLASMRFFLRFIDLEEQFDAYGFQKKYGATFKINSKREAYTDFSASLGPGGYAWNVIRSEADDLIFRYAGEQGAHIFDGTKVDDIEFLSYDGADGANFTPAAFLVNPGRPVAATWSRKDGTRGRIKFDYLIDASGRAGIISTKYLKNRTVNEGLRNIANWSYWKGAKVYGEGSDQQGSPFFEALTDGSGWCWAIPLHNGTLSVGVVMRQDLFFGKKKAAGSPGSLEMYKLCLQSVPGISGLLEDAEIVSDVKMASDWSYSASAYAGPHFRVAGDAGCFIDPYFSSGVHLALVGGLSAATTIQAVRRGETSEFSAAKWHSSKVTEGYTRFLLVVMAVLRQLRKQNAAVITDDKEEGFDTAFGLIQPVIQGQADTGESEQQRMVAGVQFSLERFGQATPEAQRALLDKVQFAGQNAEELEKLTADELAVLHNIIGRQLKMTKVEKNLDNFTRDVIDGWAPRVERGKLGLQRADTSIMTAEMKDLFQLNRSLDSTKAGIQLPA
Protein: GEX Interacting protein (Q7K7J0)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- Chloride channel CLIC-like protein 1
- Torsin-like protein
Sequence:
MTPRKNSGTMGMEFNKKTQYYSQCQFCTLKIWSNTEIVLAGGNVICNLCIAEKSHAVQFDRKYMIKTLSKTFSRKWEISNNLIMTLLILLLSALFFISQGTFSMLQNEPNQDRNPYQNYIESVRSFVNSDFSDISKENRNLLRLIGEQMFLHPDEHAPLVIVIAGLKANEFSEKLNKAIQNSKSETNSNNLPIEIGNQLERGELHAILNNALASQMTPRTAVLTNIDLLAWDAVLVLHAFADHGTFPIPKTVLLLAVSTEETTYSGNSCDGKILKLVTNRWIENGGNYDNIPPIVARISYFMCL
Protein: GDP-mannose 4,6 dehydratase 1 (EC 4.2.1.47) (Bacillus thuringiensis toxin-resistant protein 1) (Bt toxin-resistant protein 1) (GDP-D-mannose dehydratase) (GMD) (Q18801)
Organism: Caenorhabditis elegans
Function: Catalyzes the conversion of GDP-D-mannose to GDP-4-dehydro-6-deoxy-D-mannose. Involved in susceptibility to pore-forming crystal toxins in conjunction with bre-2, bre-3, bre-4, and bre-5. Involved in susceptibility to the nematotoxic C.cinerea galectin Cgl2, likely by contributing to the synthesis of N-glycans to which Cgl2 binds. Has a role in determining brood size.
Interaction partners:
- GDP-L-fucose synthase
- Mannose-1-phosphate guanylyltransferase catalytic subunit beta
- Nucleotidyl transferase domain-containing protein
- GDP-mannose 4,6 dehydratase 2
- Alpha-
- Dolichol-phosphate mannosyltransferase subunit 1
- Chitobiosyldiphosphodolichol beta-mannosyltransferase
- Alpha-
- Beta-1,4-galactosyltransferase galt-1
- Alpha-
Sequence:
MPTGKSESSDISEVVGNMEISKVEGLEACIGMSHEVSTTPAAELAAFRARKVALITGISGQDGSYLAELLLSKGYKVHGIIRRSSSFNTARIEHLYSNPITHHGDSSFSLHYGDMTDSSCLIKLISTIEPTEVYHLAAQSHVKVSFDLPEYTAEVDAVGTLRLLDAIHACRLTEKVRFYQASTSELYGKVQEIPQSEKTPFYPRSPYAVAKMYGYWIVVNYREAYNMFACNGILFNHESPRRGETFVTRKITRSVAKISLGQQESIELGNLSALRDWGHAREYVEAMWRILQHDSPDDFVIATGKQFSVREFCNLAFAEIGEVLQWEGEGVEEVGKNKDGVIRVKVSPKYYRPTEVETLLGNAEKAKKTLGWEAKVTVPELVKEMVASDIILMKSNPMA
Protein: UDP-sulfoquinovose synthase, chloroplastic (EC 3.13.1.1) (SoSQD1) (Sulfite:UDP-glucose sulfotransferase) (Sulfolipid biosynthesis protein) (Q84KI6)
Organism: Spinacia oleracea (Spinach)
Function: Involved in the biosynthesis of sulfolipids found in thylakoid membranes. Converts UDP-glucose and sulfite to the sulfolipid head group precursor UDP-sulfoquinovose. The sulfite is delivered to the reaction center by the FMN-binding domain of FdGOGAT.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:12706349}.
Interaction partners:
Sequence:
MAHLLSTSCSMKVSPSEKLSSKCWNIGSTKYPMSFTQQTSKSAFKSLVHQRNNTQKLTVVRATTVPLNQETKAESGTSSFENNGNTSGRKRVMVIGGDGYCGWATALHLSKKNYDVCIVDNLVRRLFDHQLGLDSLTPIASIQNRIRRWQGLTGKTIDLHVGDICDFEFLAETFKSFEPDTVVHFGEQRSAPYSMIDRSRAVYTQQNNVIGTINVLFAIKEFSEECHLVKLGTMGEYGTPNIDIEEGFITITHNGRTDTLPYPKQASSFYHLSKVHDSHNIAFTCKAWGIRATDLNQGVVYGVMTEETAMHEELCNRFDYDAVFGTALNRFCVQAAVGHPLTVYGKGGQTRGYLDIRDTVQCVELAIANPAKLGEFRVFNQFTEQYSVRDLAALVTKAGEKLGLNVETISVPNPRVEAEEHYYNAKHTKLAELGLKPHLLSDSLLDSVLNFAVQYKDRVDTKQIMPSVSWKKIGVKPQTLRA
Protein: Class E basic helix-loop-helix protein 22 (bHLHe22) (Class B basic helix-loop-helix protein 5) (bHLHb5) (Trinucleotide repeat-containing gene 20 protein) (Q8NFJ8)
Organism: Homo sapiens (Human)
Function: Inhibits DNA binding of TCF3/E47 homodimers and TCF3 (E47)/NEUROD1 heterodimers and acts as a strong repressor of Neurod1 and Myod-responsive genes, probably by heterodimerization with class a basic helix-loop-helix factors. Despite the presence of an intact basic domain, does not bind to DNA (By similarity). In the brain, may function as an area-specific transcription factor that regulates the postmitotic acquisition of area identities and elucidate the genetic hierarchy between progenitors and postmitotic neurons driving neocortical arealization. May be required for the survival of a specific population of inhibitory neurons in the superficial laminae of the spinal cord dorsal horn that may regulate pruritis. Seems to play a crucial role in the retinogenesis, in the specification of amacrine and bipolar subtypes. Forms with PRDM8 a transcriptional repressor complex controlling genes involved in neural development and neuronal differentiation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- PR domain zinc finger protein 8
- AP-3 complex subunit beta-1
Sequence:
MERGMHLGAAAAGEDDLFLHKSLSASTSKRLEAAFRSTPPGMDLSLAPPPRERPASSSSSPLGCFEPADPEGAGLLLPPPGGGGGGSAGSGGGGGGGVGVPGLLVGSAGVGGDPSLSSLPAGAALCLKYGESASRGSVAESSGGEQSPDDDSDGRCELVLRAGVADPRASPGAGGGGAKAAEGCSNAHLHGGASVPPGGLGGGGGGGSSSGSSGGGGGSGSGSGGSSSSSSSSSKKSKEQKALRLNINARERRRMHDLNDALDELRAVIPYAHSPSVRKLSKIATLLLAKNYILMQAQALEEMRRLVAYLNQGQAISAASLPSSAAAAAAAAALHPALGAYEQAAGYPFSAGLPPAASCPEKCALFNSVSSSLCKQCTEKP
Protein: Multidrug resistance protein MexB (Multidrug-efflux transporter MexB) (P52002)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: The inner membrane transporter component of the MexAB-OprM efflux system that confers multidrug resistance. Also functions as the major efflux pump for n-hexane and p-xylene efflux. Over-expression of the pump increases antibiotic and solvent efflux capacities. Implicated in the secretion of the siderophore pyoverdine.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Multidrug resistance protein MexA
- Outer membrane protein OprM
- Outer membrane protein OprJ
- Resistance-Nodulation-Cell Division
- Resistance-Nodulation-Cell Division
- Multidrug efflux outer membrane protein OprN
- Resistance-Nodulation-Cell Division
- Probable secretion protein
- Probable Resistance-Nodulation-Cell Division
- Protein CyaE
Sequence:
MSKFFIDRPIFAWVIALVIMLAGGLSILSLPVNQYPAIAPPAIAVQVSYPGASAETVQDTVVQVIEQQMNGIDNLRYISSESNSDGSMTITVTFEQGTDPDIAQVQVQNKLQLATPLLPQEVQRQGIRVTKAVKNFLMVVGVVSTDGSMTKEDLSNYIVSNIQDPLSRTKGVGDFQVFGSQYSMRIWLDPAKLNSYQLTPGDVSSAIQAQNVQISSGQLGGLPAVKGQQLNATIIGKTRLQTAEQFENILLKVNPDGSQVRLKDVADVGLGGQDYSINAQFNGSPASGIAIKLATGANALDTAKAIRQTIANLEPFMPQGMKVVYPYDTTPVVSASIHEVVKTLGEAILLVFLVMYLFLQNFRATLIPTIAVPVVLLGTFGVLAAFGFSINTLTMFGMVLAIGLLVDDAIVVVENVERVMAEEGLSPREAARKSMGQIQGALVGIAMVLSAVFLPMAFFGGSTGVIYRQFSITIVSAMALSVIVALILTPALCATMLKPIEKGDHGEHKGGFFGWFNRMFLSTTHGYERGVASILKHRAPYLLIYVVIVAGMIWMFTRIPTAFLPDEDQGVLFAQVQTPPGSSAERTQVVVDSMREYLLEKESSSVSSVFTVTGFNFAGRGQSSGMAFIMLKPWEERPGGENSVFELAKRAQMHFFSFKDAMVFAFAPPSVLELGNATGFDLFLQDQAGVGHEVLLQARNKFLMLAAQNPALQRVRPNGMSDEPQYKLEIDDEKASALGVSLADINSTVSIAWGSSYVNDFIDRGRVKRVYLQGRPDARMNPDDLSKWYVRNDKGEMVPFNAFATGKWEYGSPKLERYNGVPAMEILGEPAPGLSSGDAMAAVEEIVKQLPKGVGYSWTGLSYEERLSGSQAPALYALSLLVVFLCLAALYESWSIPFSVMLVVPLGVIGALLATSMRGLSNDVFFQVGLLTTIGLSAKNAILIVEFAKELHEQGKGIVEAAIEACRMRLRPIVMTSLAFILGVVPLAISTGAGSGSQHAIGTGVIGGMVTATVLAIFWVPLFYVAVSTLFKDEASKQQASVEKGQ