wanglab/gogpt-training-data huggingface dataset:
Protein: Palladin (P0C5E3)
Organism: Rattus norvegicus (Rat)
Function: Cytoskeletal protein required for organization of normal actin cytoskeleton. Roles in establishing cell morphology, motility, cell adhesion and cell-extracellular matrix interactions in a variety of cell types. May function as a scaffolding molecule with the potential to influence both actin polymerization and the assembly of existing actin filaments into higher-order arrays. Binds to proteins that bind to either monomeric or filamentous actin. Localizes at sites where active actin remodeling takes place, such as lamellipodia and membrane ruffles. Different isoforms may have functional differences. Plays a role in neurite outgrowth and in the establishment of polarity during neuronal morphogenesis. Participates in the acquisition of the reactive astrocyte morphology.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16125169, ECO:0000269|PubMed:16868024}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q8WX93}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:11553711, ECO:0000269|PubMed:16125169}. Cell projection, ruffle {ECO:0000269|PubMed:16868024}. Cell projection, podosome {ECO:0000269|PubMed:16868024}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q8WX93}. Cell projection, axon {ECO:0000269|PubMed:11438925, ECO:0000269|PubMed:11553711}. Cell projection, growth cone {ECO:0000269|PubMed:11438925, ECO:0000269|PubMed:11553711}. Note=Localizes to stress fibers (PubMed:11553711, PubMed:16125169, PubMed:16868024, PubMed:22659164). Localizes to Z lines (PubMed:11553711, PubMed:16125169, PubMed:16868024). Preferentially expressed in the excitatory presynaptic terminals (PubMed:11438925). {ECO:0000269|PubMed:11438925, ECO:0000269|PubMed:11553711, ECO:0000269|PubMed:16125169, ECO:0000269|PubMed:16868024, ECO:0000269|PubMed:22659164}.
Interaction partners:
Sequence:
PEEICTLVIAESFPEDAGIFTCSARNDYGSVTSTAQLVVTSANTENCSYDSMGEPNSDHFQHFPPPPPILETGSYELASQKPSEIQQVNTPNLGFNMAALQMQFNSAERETNGVHPSHGVNGLINGKAYGNKSPPTPAALLSPTKEPPPLLAKPKLGFPKKASRTARIASDEEIQGTKDAVIQDLERKLRFKEDLLNNGQPRLTYEERMARRLLGADSANVFNIQEPEETAANQEYKVSSCEQRLISEIEYRLERSPVEESGDEVQEAEVPVENAAAPFFEMKLKHYKIFEGMPVTFTCRVAGSPKPKIYWFKDGKQISPKSDHYTIQRDVDGTCSLHTTASTLDDDGNYTIMAANTQGRVSCTGRLMVQAVNQRGRSPRSPPGHPHARRPRSRSRDSGDENEPIQERFFRPHFLQAPGDLTVQEGKLCRMDCKVSGLPTPDLSWQLDGKPIRPDSAHKMLVRENGVHSLIIEPVTSRDAGIYTCIATNRAGQNSFNLELVVAAKEAHKAPVFIEKLQNTGVADGYPVRLECRVSGVPPPQIFWKKENESLTHSTDRVSMHQDNHGYICLLIQGATKEDAGWYTVSAKNEAGIVSCTARLDVY
Protein: Transmembrane 4 L6 family member 18 (Q96CE8)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MGSRKCGGCLSCLLIPLALWSIIVNILLYFPNGQTSYASSNKLTNYVWYFEGICFSGIMMLIVTTVLLVLENNNNYKCCQSENCSKKYVTLLSIIFSSLGIAFSGYCLVISALGLVQGPYCRTLDGWEYAFEGTAGRFLTDSSIWIQCLEPAHVVEWNIILFSILITLSGLQVIICLIRVVMQLSKILCGSYSVIFQPGII
Protein: Uncharacterized protein (Q38AX2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MMSRRPPVGVFCVDVEELLKATAKLKIDREKVDDRSPTFSTSGPRGSSTKRSSARNSGGRGDCPHSVRPGSMSSAGGAHSPRSSAGRRRMRSRKAKNRGLKAGVEDYTPLGKERGEDGHAVARPLFDFPSPNIVNTTTCSTSRTPICGGFRDPACMQTGDACNDTISCWKNGDQAIRGPESDCTFSSQLQLTIPPGADEDSVGPEQEEKFRLHDGTETAAPPITPERVDPVISNVMQAMQNRLLGVSAALCHRDAAPRDGGTGFTSSEKVSCGQRISNGTNNVAQFSRKVNDSVFLSQPSIYGTEDSKKAAGSWGPPQSLQAARTPRKLAAIGKHGVKEYGQPPRLRDARGVERVLITGVVTKVPKRATSSLGAPQLAKPLLTPVFQNIARNFAEKSKRPKRF
Protein: Protein transport protein SEC13 (Q04491)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Functions as a component of the nuclear pore complex (NPC) and the COPII coat. It is one of 5 proteins constituting the COPII coat, which is involved in anterograde (ER to Golgi) double-membrane transport vesicle formation. First the small GTPase SAR1, activated by and binding to the integral ER membrane protein SEC12, exchanges GDP for GTP and recruits the heterodimer SEC23/24, which in turn recruits the heterotetramer SEC13-SEC31. The polymerization of COPII coat complexes then causes physically the deformation (budding) of the membrane, leading to the creation of a transport vesicle. The COPII complex is dissociated upon SAR1-GTP hydrolysis to SAR1-GDP. SEC23 functions as the SAR1 GTPase activating protein, whose activity is stimulated in the presence of SEC13/31. SEC13 is directly or indirectly required for normal ER membrane and nuclear envelope morphology. It also 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. SEC13 is required for efficient mRNA export from the nucleus to the cytoplasm and for correct nuclear pore biogenesis and distribution. Component of the SEA complex which coats the vacuolar membrane and is involved in intracellular trafficking, autophagy, response to nitrogen starvation, and amino acid biogenesis.
Subcellular location: Cytoplasmic vesicle, COPII-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus, nuclear pore complex {ECO:0000269|PubMed:10684247}. Vacuole membrane; Peripheral membrane protein.
Interaction partners:
- Nucleoporin NUP145
- Restriction of telomere capping protein 1
- Nucleoporin NUP84
- SED5-binding protein 3
- Protein transport protein SEC24
- Small COPII coat GTPase SAR1
- COPII coat assembly protein SEC16
- Maintenance of telomere capping protein 5
- Protein transport protein SEC31
- Nucleoporin NUP85
Sequence:
MVVIANAHNELIHDAVLDYYGKRLATCSSDKTIKIFEVEGETHKLIDTLTGHEGPVWRVDWAHPKFGTILASCSYDGKVLIWKEENGRWSQIAVHAVHSASVNSVQWAPHEYGPLLLVASSDGKVSVVEFKENGTTSPIIIDAHAIGVNSASWAPATIEEDGEHNGTKESRKFVTGGADNLVKIWKYNSDAQTYVLESTLEGHSDWVRDVAWSPTVLLRSYLASVSQDRTCIIWTQDNEQGPWKKTLLKEEKFPDVLWRASWSLSGNVLALSGGDNKVTLWKENLEGKWEPAGEVHQ
Protein: Nociceptin receptor (K3 opiate receptor) (Kappa-type 3 opioid receptor) (KOR-3) (ORGC) (Orphanin FQ receptor) (P35377)
Organism: Mus musculus (Mouse)
Function: G-protein coupled opioid receptor that functions as receptor for the endogenous neuropeptide nociceptin. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Signaling via G proteins mediates inhibition of adenylate cyclase activity and calcium channel activity. Arrestins modulate signaling via G proteins and mediate the activation of alternative signaling pathways that lead to the activation of MAP kinases. Plays a role in modulating nociception and the perception of pain. Plays a role in the regulation of locomotor activity by the neuropeptide nociceptin.
Subcellular location: Cell membrane; Multi-pass membrane protein. Cytoplasmic vesicle {ECO:0000250}. Note=Ligand binding leads to receptor internalization into cytoplasmic vesicles, decreasing the amount of available receptor at the cell surface. Internalization requires phosphorylation at Ser-360. Can recycle to the cell membrane (By similarity). {ECO:0000250}.
Interaction partners:
- Prepronociceptin
- Proenkephalin-A
- Pro-opiomelanocortin
- Proenkephalin-B
- Prolactin
- Prolactin-6A1
- Pro-neuropeptide Y
Sequence:
MESLFPAPFWEVLYGSHFQGNLSLLNETVPHHLLLNASHSAFLPLGLKVTIVGLYLAVCIGGLLGNCLVMYVILRHTKMKTATNIYIFNLALADTLVLLTLPFQGTDILLGFWPFGNALCKTVIAIDYYNMFTSTFTLTAMSVDRYVAICHPIRALDVRTSSKAQAVNVAIWALASVVGVPVAIMGSAQVEDEEIECLVEIPAPQDYWGPVFAICIFLFSFIIPVLIISVCYSLMIRRLRGVRLLSGSREKDRNLRRITRLVLVVVAVFVGCWTPVQVFVLVQGLGVQPGSETAVAILRFCTALGYVNSCLNPILYAFLDENFKACFRKFCCASALHREMQVSDRVRSIAKDVGLGCKTSETVPRPA
Protein: Integrin beta (F1QG85)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|RuleBase:RU000633}; Single-pass type I membrane protein {ECO:0000256|RuleBase:RU000633}. Cell projection, invadopodium membrane {ECO:0000256|ARBA:ARBA00004297}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004297}. Cell projection, lamellipodium {ECO:0000256|ARBA:ARBA00004510}. Cell projection, ruffle membrane {ECO:0000256|ARBA:ARBA00004199}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004199}. Melanosome {ECO:0000256|ARBA:ARBA00004223}.
Interaction partners:
- Scaffold protein ILK
- Integrin alpha-5 precursor
- Integrin alpha-6 isoform X1
- Protein tyrosine kinase 2ab
- Talin 1.
- Integrin, alpha 6b
- Integrin, alpha 6,-like
- Integrin, alpha 8
- Integrin, alpha V
- Integrin alpha-4
Sequence:
MDLKLLFISALLGIISCSHAQQEGNECIKANALSCGECIQVGDKCGWCTDAEFLKQGEPTSARCDELESLKKRGCAEDKIENPHGSQRILKNTPVTNRKKGAEKLRPEDITQIQPQKLSLQLRSGEPQNIKLKFKRAEDYPIDLYYLMDLSYSMKDDLENVKNLGTSLMKEMSKITSDFRIGFGSFVEKTVMPYISTTPAKLLNPCTGDQNCTSPFSYKNVLKLTSNGQRFNSLVGQQQISGNLDSPEGGFDAIMQVAVCGEHIGWRNVTRLLVFSTDAGFHFAGDGKLGGIVLPNDGRCHLENDMYTMSHYYDYPSIAHLVQKLSENNIQTIFAVTEEFQPVYKELKNLIPKSAVGTLSANSSNVINLIVDAYNSLSSEVILENSKLPEGVTITYQSRCKNGVVNEGESGRKCSNISIGDEVSFNINITAQGCPKQGKTETIKIKPLGFTEEVEITLSFICECECHKHAMKNSPLCHNGNGSFECGACRCNKGRVGRQCECRKDEVSTEDLDKNCRKDNGTDICSNNGECVCGTCECKKRENPEERYSGKYCECDNFNCDRSNNKLCGGHGRCECRVCVCDANYTGSACDCSLDTSTCLASNKQICNGRGICECGTCRCTDPKFQGPTCEICPTCPGVCTEHKECVQCRAFGTGEKKDTCKRDCSYFNLIEVEDRDKLPQPVQAFPLMHCKERDARDCWFYYTYAVNNNTEKEVHVVKTMECPPGPDIIPIVAGVVAGIVLIGLALLLIWKLLMIIHDRREFAKFEKEKMNAKWDTGENPIYKSAVTTVINPKYEGK
Protein: Agamous-like MADS-box protein AGL13 (Q38837)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251}.
Interaction partners:
- Agamous-like MADS-box protein AGL103
- Floral homeotic protein APETALA 3
- AGAMOUS-like 96
Sequence:
MGRGKVEVKRIENKITRQVTFSKRKSGLLKKAYELSVLCDAEVSLIIFSTGGKLYEFSNVGVGRTIERYYRCKDNLLDNDTLEDTQGLRQEVTKLKCKYESLLRTHRNLVGEDLEGMSIKELQTLERQLEGALSATRKQKTQVMMEQMEELRRKERELGDINNKLKLETEDHDFKGFQDLLLNPVLTAGCSTDFSLQSTHQNYISDCNLGYFLQIGFQQHYEQGEGSSVTKSNARSDAETNFVQ
Protein: Histone H1.8 (Histone H1oo) (Oocyte-specific histone H1) (Oocyte-specific linker histone H1) (Q3HNG7)
Organism: Bos taurus (Bovine)
Function: May play a key role in the control of gene expression during oogenesis and early embryogenesis, presumably through the perturbation of chromatin structure. Essential for meiotic maturation of germinal vesicle-stage oocytes. The somatic type linker histone H1c is rapidly replaced by H1oo in a donor nucleus transplanted into an oocyte. The greater mobility of H1oo as compared to H1c may contribute to this rapid replacement and increased instability of the embryonic chromatin structure. The rapid replacement of H1c with H1oo may play an important role in nuclear remodeling (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16470586}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00837, ECO:0000269|PubMed:16470586}. Chromosome {ECO:0000255|PROSITE-ProRule:PRU00837, ECO:0000269|PubMed:16470586}. Note=In the 1-, 2- and 4-cell embryo, it is uniformly spread within the cytoplasm, while it is concentrated onto the chromatin in the nucleus. In the 8- to 16-cell embryo, its presence diminishes in the cytoplasm, although it is still strongly expressed in the nucleus.
Interaction partners:
- H1.9 linker histone
- Bone morphogenetic protein 15
- Importin subunit beta-1
Sequence:
MAPGSIASSDTSSSTSSSSTSSASSASAEGSSRPLGSEKPGLARGAVRAPRRHPPVLRMVLEALQAGERRRGTSVAAIKVYILQKYPTVDALRLNHLLKQALATGLHRGLLIRPVNSKAKGATGSFKLVPKDKRKIPPRKTAPRMPGQAEGKDPKKPSESKKDPANTVEVKKGSRKPREERAAPSKPGAAKKAPKKGTQTKDPEPRLGEAKKSSRRPDKAAQAPPSAGGPGGKSKVKERGSRQADTKAHRKTQPGSQSSKSTVTKGENGAPLAKKKMGGKVPKEAAGEGPKAKAPVPPKGAGSKKEPGPLAGKAEASKGPRKPGIPTKSSVSKAASKKAEAEG
Protein: Disease resistance protein RRS1 (Disease resistance protein RCH2) (Disease resistance protein SLH1) (Probable WRKY transcription factor 52) (Protein RPS4-homolog) (Protein SENSITIVE TO LOW HUMIDITY 1) (Resistance to Colletotrichum higginsianum 2 protein) (Resistance to Ralstonia solanacearum 1 protein) (WRKY DNA-binding protein 52) (P0DKH5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor. Interacts specifically with the W box (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis-acting element. Acts also as a disease resistance protein involved in resistance to fungal and bacterial pathogens, including R.solanacearum, P.syringae pv. tomato and C.higginsianum. Heterodimerization with RPS4 is required to form a functional complex to recognize AvrRps4 and PopP2. Contributes to temperature-conditioned RPS4 auto-immunity.
Subcellular location: Nucleus {ECO:0000269|PubMed:12788974}. Cytoplasm {ECO:0000305|PubMed:12788974}. Note=The nuclear localization is only detected upon interaction with PopP2. {ECO:0000269|PubMed:12788974}.
Interaction partners:
- Disease resistance protein RPS4
- Cysteine protease RD19A
- Toll/interleukin-1 receptor-like protein
- Protein EDS1
- Probable cysteine protease RD19C
- Probable cysteine protease RD19B
- Probable cysteine protease RD19D
- LRR protein
- Lipase-like PAD4
- Disease resistance protein ADR1
Sequence:
MTNCEKDEEFVCISCVEEVRYSFVSHLSEALRRKGINNVVVDVDIDDLLFKESQAKIEKAGVSVMVLPGNCDPSEVWLDKFAKVLECQRNNKDQAVVSVLYGDSLLRDQWLSELDFRGLSRIHQSRKECSDSILVEEIVRDVYETHFYVGRIGIYSKLLEIENMVNKQPIGIRCVGIWGMPGIGKTTLAKAVFDQMSSAFDASCFIEDYDKSIHEKGLYCLLEEQLLPGNDATIMKLSSLRDRLNSKRVLVVLDDVRNALVGESFLEGFDWLGPGSLIIITSRDKQVFCLCGINQIYEVQGLNEKEARQLFLLSASIKEDMGEQNLQELSVRVINYANGNPLAISVYGRELKGKKKLSEMETAFLKLKRRPPFKIVDAFKSTYDTLSDNEKNIFLDIACFFQGENVNYVIQLLEGCGFFPHVEIDVLVDKCLVTISENRVWLHKLTQDIGREIINGETVQIERRRRLWEPWSIKYLLEYNEHKANGEPKTTFKRAQGSEEIEGLFLDTSNLRFDLQPSAFKNMLNLRLLKIYCSNPEVHPVINFPTGSLHSLPNELRLLHWENYPLKSLPQNFDPRHLVEINMPYSQLQKLWGGTKNLEMLRTIRLCHSHHLVDIDDLLKAENLEVIDLQGCTRLQNFPAAGRLLRLRVVNLSGCIKIKSVLEIPPNIEKLHLQGTGILALPVSTVKPNHRELVNFLTEIPGLSEELERLTSLLESNSSCQDLGKLICLELKDCSCLQSLPNMANLDLNVLDLSGCSSLNSIQGFPRFLKQLYLGGTAIREVPQLPQSLEILNAHGSCLRSLPNMANLEFLKVLDLSGCSELETIQGFPRNLKELYFAGTTLREVPQLPLSLEVLNAHGSDSEKLPMHYKFNNFFDLSQQVVNDFLLKTLTYVKHIPRGYTQELINKAPTFSFSAPSHTNQNATFDLQSGSSVMTRLNHSWRNTLVGFGMLVEVAFPEDYCDATDVGISCVCRWSNKEGRSCRIERKFHCWAPWQVVPKVRKDHTFVFSDVNMRPSTGEGNDPDIWAGLVVFEFFPINQQTKCLNDRFTVRRCGVRVINVATGNTSLENIALVLSLDPVEVSGYEVLRVSYDDLQEMDKVLFLYIASLFNDEDVDFVAPLIAGIDLDVSSGLKVLADVSLISVSSNGEIVMHSLQRQMGKEILHGQSMLLSDCESSMTENLSDVPKKKKKHSESRVKKVVSIPAIDEGDLWTWRKYGQKDILGSRFPRGYYRCAYKFTHGCKATKQVQRSETDSNMLAITYLSEHNHPRPTKRKALADSTRSTSSSIC
Protein: ATP-dependent (S)-NAD(P)H-hydrate dehydratase (EC 4.2.1.93) (ATP-dependent NAD(P)HX dehydratase) (Carbohydrate kinase domain-containing protein) (NAD(P)HX dehydratase) (Q8IW45)
Organism: Homo sapiens (Human)
Function: Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ATP, which is converted to ADP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration.
Subcellular location: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03157}.
Interaction partners:
- NAD
- NADH dehydrogenase 1 alpha subcomplex subunit 13
- YjeF N-terminal domain-containing protein 3
- Enhancer of mRNA-decapping protein 3
Sequence:
MVTRAGAGTAVAGAVVVALLSAALALYGPPLDAVLERAFSLRKAHSIKDMENTLQLVRNIIPPLSSTKHKGQDGRIGVVGGCQEYTGAPYFAAISALKVGADLSHVFCASAAAPVIKAYSPELIVHPVLDSPNAVHEVEKWLPRLHALVVGPGLGRDDALLRNVQGILEVSKARDIPVVIDADGLWLVAQQPALIHGYRKAVLTPNHVEFSRLYDAVLRGPMDSDDSHGSVLRLSQALGNVTVVQKGERDILSNGQQVLVCSQEGSSRRCGGQGDLLSGSLGVLVHWALLAGPQKTNGSSPLLVAAFGACSLTRQCNHQAFQKHGRSTTTSDMIAEVGAAFSKLFET
Protein: Ethionine resistance-conferring protein 1 (P38767)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Probable transporter involved in ethionine resistance. Overproduction leads to accumulation of S-adenosylmethionine.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Uncharacterized transporter YDR338C
- Squalene synthase ERG9
- TATA-box-binding protein
- tRNA
Sequence:
MSKQFSHTTNDRRSSIIYSTSVGKAGLFTPADYIPQESEENLIEGEEQEGSEEEPSYTGNDDETEREGEYHSLLDANNSRTLQQEAWQQGYDSHDRKRLLDEERDLLIDNKLLSQHGNGGGDIESHGHGQAIGPDEEERPAEIANTWESAIESGQKISTTFKRETQVITMNALPLIFTFILQNSLSLASIFSVSHLGTKELGGVTLGSMTANITGLAAIQGLCTCLDTLCAQAYGAKNYHLVGVLVQRCAVITILAFLPMMYVWFVWSEKILALMIPERELCALAANYLRVTAFGVPGFILFECGKRFLQCQGIFHASTIVLFVCAPLNALMNYLLVWNDKIGIGYLGAPLSVVINYWLMTLGLLIYAMTTKHKERPLKCWNGIIPKEQAFKNWRKMINLAIPGVVMVEAEFLGFEVLTIFASHLGTDALGAQSIVATIASLAYQVPFSISVSTSTRVANFIGASLYDSCMITCRVSLLLSFVCSSMNMFVICRYKEQIASLFSTESAVVKMVVDTLPLLAFMQLFDAFNASTAGCLRGQGRQKNRWVHQPSRILLPRCAHGICVSIPVSSGCRRLMVGYN
Protein: Lanosterol 14-alpha demethylase (EC 1.14.14.154) (CYPLI) (Cytochrome P450 51) (Cytochrome P450-14DM) (Cytochrome P450-LIA1) (Sterol 14-alpha demethylase) (P50859)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Function: Catalyzes C14-demethylation of lanosterol which is critical for ergosterol biosynthesis. It transforms lanosterol into 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol (By similarity).
Subcellular location: Membrane {ECO:0000305}.
Interaction partners:
- Delta
- Terpene cyclase/mutase family member
- Candida glabrata strain CBS138 chromosome K complete sequence
- Squalene synthase
- Sterol 24-C-methyltransferase
- 3-keto-steroid reductase
- Delta
- C-8 sterol isomerase
- Squalene monooxygenase
- Sterol-4-alpha-carboxylate 3-dehydrogenase ERG26, decarboxylating
Sequence:
MSTENTSLVVELLEYVKLGLSYFQALPLAQRVSIMVALPFVYTITWQLLYSLRKDRPPLVFYWIPWVGSAIPYGTKPYEFFEDCQKKYGDIFSFMLLGRIMTVYLGPKGHEFIFNAKLADVSAEAAYSHLTTPVFGKGVIYDCPNHRLMEQKKFVKGALTKEAFVRYVPLIAEEIYKYFRNSKNFKINENNSGIVDVMVSQPEMTIFTASRSLLGKEMRDKLDTDFAYLYSDLDKGFTPINFVFPNLPLEHYRKRDHAQQAISGTYMSLIKERREKNDIQNRDLIDELMKNSTYKDGTKMTDQEIANLLIGVLMGGQHTSAATSAWCLLHLAERPDVQEELYQEQMRVLNNDTKELTYDDLQNMPLLNQMIKETLRLHHPLHSLFRKVMRDVAIPNTSYVVPRDYHVLVSPGYTHLQEEFFPKPNEFNIHRWDGDAASSSAAGGDEVDYGFGAISKGVSSPYLPFGGGRHRCIGELFAYCQLGVLMSIFIRTMKWRYPTEGETVPPSDFTSMVTLPTAPAKIYWEKRHPEQKY
Protein: Anion exchange transporter (Solute carrier family 26 member 7) (Q8TE54)
Organism: Homo sapiens (Human)
Function: Acts as a sodium-independent DIDS-sensitive anion exchanger mediating bicarbonate, chloride, sulfate and oxalate transport. May play a role in the maintenance of the electrolyte and acid-base homeostasis in the kidney, by acting as a distal excretory segment-specific anion exchanger. Plays a major role in gastric acid secretion.
Subcellular location: Basolateral cell membrane {ECO:0000269|PubMed:16524946, ECO:0000269|PubMed:30333321, ECO:0000269|PubMed:32119864}; Multi-pass membrane protein {ECO:0000255}. Recycling endosome membrane {ECO:0000269|PubMed:16524946}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:31372509}; Multi-pass membrane protein {ECO:0000255}. Lateral cell membrane {ECO:0000269|PubMed:31372509}; Multi-pass membrane protein {ECO:0000255}. Note=Expressed in the cytoplasm in recycling endosomes of medullary collecting duct cells and in acid-secreting gastric parietal cells. Targeted to the basolateral membrane in hypertonicity and potassium depletion. {ECO:0000269|PubMed:16524946}.
Interaction partners:
- Anion exchange protein 2
Sequence:
MTGAKRKKKSMLWSKMHTPQCEDIIQWCRRRLPILDWAPHYNLKENLLPDTVSGIMLAVQQVTQGLAFAVLSSVHPVFGLYGSLFPAIIYAIFGMGHHVATGTFALTSLISANAVERIVPQNMQNLTTQSNTSVLGLSDFEMQRIHVAAAVSFLGGVIQVAMFVLQLGSATFVVTEPVISAMTTGAATHVVTSQVKYLLGMKMPYISGPLGFFYIYAYVFENIKSVRLEALLLSLLSIVVLVLVKELNEQFKRKIKVVLPVDLVLIIAASFACYCTNMENTYGLEVVGHIPQGIPSPRAPPMNILSAVITEAFGVALVGYVASLALAQGSAKKFKYSIDDNQEFLAHGLSNIVSSFFFCIPSAAAMGRTAGLYSTGAKTQVACLISCIFVLIVIYAIGPLLYWLPMCVLASIIVVGLKGMLIQFRDLKKYWNVDKIDWGIWVSTYVFTICFAANVGLLFGVVCTIAIVIGRFPRAMTVSIKNMKEMEFKVKTEMDSETLQQVKIISINNPLVFLNAKKFYTDLMNMIQKENACNQPLDDISKCEQNTLLNSLSNGNCNEEASQSCPNEKCYLILDCSGFTFFDYSGVSMLVEVYMDCKGRSVDVLLAHCTASLIKAMTYYGNLDSEKPIFFESVSAAISHIHSNKNLSKLSDHSEV
Protein: U11/U12 small nuclear ribonucleoprotein 25 kDa protein (U11/U12 snRNP 25 kDa protein) (U11/U12-25K) (Minus-99 protein) (Q9BV90)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000269|PubMed:15146077}.
Interaction partners:
- U11/U12 small nuclear ribonucleoprotein 35 kDa protein
- U11/U12 small nuclear ribonucleoprotein 48 kDa protein
- Zinc finger matrin-type protein 5
- Programmed cell death protein 7
- PHD finger-like domain-containing protein 5A
- Zinc finger CCHC-type and RNA-binding motif-containing protein 1
- Splicing factor 3B subunit 6
- RNA-binding region-containing protein 3
- Small nuclear ribonucleoprotein F
- Small nuclear ribonucleoprotein Sm D2
Sequence:
MDVFQEGLAMVVQDPLLCDLPIQVTLEEVNSQIALEYGQAMTVRVCKMDGEVMPVVVVQSATVLDLKKAIQRYVQLKQEREGGIQHISWSYVWRTYHLTSAGEKLTEDRKKLRDYGIRNRDEVSFIKKLRQK
Protein: 4-alpha-glucanotransferase DPE2 (EC 2.4.1.25) (Amylomaltase) (Disproportionating enzyme) (D-enzyme) (Protein DISPROPORTIONATING ENZYME 2) (Q8RXD9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Cytosolic alpha-glucanotransferase essential for the cytosolic metabolism of maltose, an intermediate on the pathway by which starch is converted to sucrose in leaves at night. Metabolizes maltose exported from the chloroplast and is specific for beta-maltose. May play a role in freezing tolerance. Temperature drop induces inactivation of DPE2 that leads to rapid accumulation of maltose, a solute that protects cells from freezing damage.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:14996213, ECO:0000269|PubMed:16596410, ECO:0000269|PubMed:20700743}.
Interaction partners:
- Alpha-glucan phosphorylase 2, cytosolic
- Alpha-glucan phosphorylase 1
- Isoamylase 3, chloroplastic
- 1,4-alpha-glucan-branching enzyme 3, chloroplastic/amyloplastic
- Isoamylase 2, chloroplastic
- 1,4-alpha-glucan-branching enzyme 2-1, chloroplastic/amyloplastic
- 1,4-alpha-glucan-branching enzyme 2-2, chloroplastic/amyloplastic
- Alpha-amylase 3, chloroplastic
- Isoamylase 1, chloroplastic
- Starch synthase 3, chloroplastic/amyloplastic
Sequence:
MMNLGSLSLSTSKSSKPMVSISFWIPYFTHWGESLLVCGSAPGLGSGNVKKGLLLKPSQQDDQLIWSGSVSVPPGFSSDYCYYVVDDSKSVLRSEFGMKRKLVVPETLTGGESVHLRDLWQSGDQALPFRSAFKDVIFHHSFDVKVEKPLGVFMNKSDQDDSVVVQFKICCPDIGEGTSVYVLGTPEKLGNWKVENGLRLNYVDDSIWEADCLIPKADFPIKYRYCKVQKEDSIGFESGGNRELSLHSIGSKQEYIVMSDGLFRAMPWRGAGVAVPMFSVRSEDDVGVGEFLDLKLLVDWAVDSGLHLVQLLPVNDTSVHKMWWDSYPYSSLSVFALHPLYLRVQALSERLPEDIKEEIQKAKNQLDKNDVDYEATMETKLSIAKKIFDIEKDQTLNSSTFQKFFSENEGWLKPYAAFCFLRDFFETSDHSQWGTFSDYTDDKLEKLISKDNLHYNTICFHYYIQYHLHVQLSAAAEYARKKGVVLKGDLPIGVDRNSVDTWVYRNLFRMNTSTGAPPDYFDKNGQNWGFPTYNWEEMSKDNYAWWRARLTQMGKYFTAYRIDHILGFFRIWELPAHAMTGLVGKFRPSIPLSQEELEKEGIWDFDRLSKPYIQKKFLEEKFGDFWPFIASNFLNETQKDMYEFKEDCNTEKKIVAKLKSLAEKSLLLENEDKVRRDVFDILRNVVLIKDPEDARKFYPRFNIEDTSSFQDLDDHSKNVLKRLYYDYYFQRQEDLWRKNALKTLPALLNSSNMLACGEDLGLIPSCVHPVMQELGLVGLRIQRMPSESDVKFGIPSNYDYMTVCAPSCHDCSTLRAWWEEDEERRQQYFKEVIGVDGIPPSQCIPEITHFILRQHVEAPSMWAIFPLQDMMALKEEYTTRPATEETINDPTNPKHYWRYRVHVTLDSLLKDTDLKSTIKNLVSSSGRSVPANVSGEDINKSRGEVIANGSTKPNP
Protein: LD20793p (Peritrophin A) (Peritrophin A, isoform B) (O17452)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MQRFQVCSVLILAWIACGHALAVGSPECPEKYGVQAYAHTENCDQFFLCTNGTLTLETCENGLLFDGKGAVHNHCNYNWAVDCKGRQWDPTPISTPACEYQFGLYAVSKDCSTTYIKCAHGEPHEQDCDAGLAYDERIHGCNWPDQLLEHCNPEAVVGFKCPTKVDPNSVAARFWPFPRFPVAGDCHRLITCVEGHPRLISCGEDKVFDEHTLTCEDPEYASGSCANYGK
Protein: Placenta-expressed transcript 1 protein (Antigen mAgK114) (Q8VEN2)
Organism: Mus musculus (Mouse)
Function: Modulates leading keratinocyte migration and cellular adhesion to matrix proteins during a wound-healing response and promotes wound repair. May play a role during trichilemmal differentiation of the hair follicle.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:20130590}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:20130590}. Note=Localized at the apical membrane of the most differentiated keratinocytes of the outer root sheath (ORS), clustered mainly in planar regions of the plasma membrane at the base of microvilli.
Interaction partners:
Sequence:
MLSLRSLLPHLGLFLCLALHLSPSLSASDNGSCVVLDNIYTSDILEISTMANVSGGDVTYTVTVPVNDSVSAVILKAVKEDDSPVGTWSGTYEKCNDSSVYYNLTSQSQSVFQTNWTVPTSEDVTKVNLQVLIVVNRTASKSSVKMEQVQPSASTPIPESSETSQTINTTPTVNTAKTTAKDTANTTAVTTANTTANTTAVTTAKTTAKSLAIRTLGSPLAGALHILLVFLISKLLF