wanglab/gogpt-training-data huggingface dataset:
Protein: Small ribosomal subunit protein uS8c (30S ribosomal protein S8, chloroplastic) (P0C493)
Organism: Oryza sativa subsp. indica (Rice)
Function: One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit.
Subcellular location: Plastid, chloroplast.
Interaction partners:
- Small ribosomal subunit protein uS2c
- Small ribosomal subunit protein uS12cz/uS12cy
- Small ribosomal subunit protein uS11c
- Small ribosomal subunit protein uS9
- Small ribosomal subunit protein uS7cz/uS7cy
- DNA-directed RNA polymerase subunit alpha
- 30S ribosomal protein S13
- Large ribosomal subunit protein uL14c
- Small ribosomal subunit protein uS14c
- Small ribosomal subunit protein uS17c
Sequence:
MGKDTIADLLTSIRNADMNKKGTVRVVSTNITENIVKILLREGFIESVRKHQESNRYFLVSTLRHQKRKTRKGIYRTRTFLKRISRPGLRIYANYQGIPKVLGGMGIAILSTSRGIMTDREARLNRIGGEVLCYIW
Protein: Protein SETSIP (SET pseudogene protein 18) (SET similar protein) (Similar to SET translocation protein) (P0DME0)
Organism: Homo sapiens (Human)
Function: Plays a role as a transcriptional activator involved in the early stage of somatic cell reprogramming. Promotes the differentiation of protein-induced pluripotent stem (PiPS) cells into endothelial cells and the formation of vascular-like tubes (in vitro). Involved in the transcription induction of vascular endothelial-cadherin (VE-cadherin) expression. Associates to the VE-cadherin gene promoter.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22869753}. Nucleus {ECO:0000269|PubMed:22869753}. Note=Translocated from the cytoplasm to the nucleus in protein-induced pluripotent stem (PiPS) endothelial cells.
Interaction partners:
Sequence:
MAPKRQSPLPLQKKKPRPPPALGLEETSASAGLPKKGEKEQQEAIEHIDEVQNEIDRLNEQDSEEILKVEQKYNKLRQPFFQKRSELIAKIPNFGVTTFVNHPQVSSLLGEEDEEALHYLTKVEVTEFEDIKSGYRIDFYFDENPYFENKVFSKEFHLNESGDPSSKSTKIKWKSGKDVTKRSSQTQNKASRKRQHEEPESFFTWFTDHSDAGADELEEVIKDDIWPNPLQYYLVPDMDDEEGGEDDDDDDDDGDEGEEELEDIDEGDEDEGEEDEDDDEGEEGEEDEGEDD
Protein: FK506-binding protein 1 (FKBP) (EC 5.2.1.8) (Peptidyl-prolyl cis-trans isomerase) (PPIase) (Rapamycin-binding protein) (P28870)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Subcellular location: Cytoplasm.
Interaction partners:
- Calcineurin subunit B
- Serine/threonine-protein phosphatase
- Serine/threonine-protein kinase TOR
- Calmodulin
- Mlc1p
- Ubiquitin-binding TORC1 subunit
- Eukaryotic translation initiation factor 4E
- Uncharacterized protein
- Calcium-binding protein NCS-1
- Small ribosomal subunit protein uS19
Sequence:
MSEELPQIEIVQEGDNTTFAKPGDTVTIHYDGKLTNGKEFDSSRKRGKPFTCTVGVGQVIKGWDISLTNNYGKGGANLPKISKGTKAILTIPPNLAYGPRGIPPIIGPNETLVFEVELLGVNGQ
Protein: Bifunctional UDP-glucose 4-epimerase/aldose 1-epimerase (A0A1D8PCN0)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Galactokinase
- Galactose-1-phosphate uridylyltransferase
- UTP--glucose-1-phosphate uridylyltransferase
- N-acetylglucosamine kinase 1
- Phosphotransferase
- Phosphotransferase
- Hexokinase-2
- Gal102p
- N-acetylglucosamine-6-phosphate deacetylase
- High-affinity glucose transporter 1
Sequence:
MSNEYILVTGGAGYIGSHTVIELISNGYKVVIVDNLSNSSYDAVARIEFIVKQHVPFYDVDIRNYEQLNKVFQDYKISGVIHFAALKAVGESTKIPLAYYDNNVSGTVNLLEVCKANDVKTIVFSSSATVYGDVTRFGDNSMIPIPEHCPMDPTNPYGRTKFIIESILKDIYNSDDAWKVAILRYFNPIGAHPSGLLGEDPLGIPNNLLPYLAQVAIGRREKLSIFGNDYNSRDGTPIRDYIHVVDLAKGHIAALAYLKNLQSKGLYREWNLGTGKGSTVFEVYHAFSKVVGRELPHEVVGRRAGDVLDLTAKPDRANKELQWKTELAIDDACKDLWKWTTENPFGFNIENYSWKEFDGFNNRLHSFVAGDLKVNLANRGALIQAITLKDSNMVKAYNNAEDFKSETNPFFGTTVGRYANRISNGEFKLNGKVYKLTKNEGANNLHGGANGFDKQDFFGPVVKSRDGKFFVDFLLVDKDGNDGFPGELEAIVHYTIDDSSVEIEYECQLLSGEATIVNMTNHSYFNVSNSDTIEGTEVKLITDKMLEVDSQLLPTGKFIENEKAASPIVLNENDVFDNCFIVDEECGIDTRDKPLKQVFEATSFVTNNKLKISTTEPAFQFYTGDGVNTKGFGKRCGFCVEPSRFINAINHKEWSNQVILKKGDVYGSKIKYEFQ
Protein: MOB kinase activator 1B (D6RCK3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEGATDVNESGSRSSKTFKPKKNIPEGSHQYELLKHAEATLGSGNLRMAVMLPEGEDLNEWVAVNTVDFFNQINMLYGTITDFCTEESCPVMSAGPKYEYHWADGTNIKKPIKCSAPKYIDYLMTWVQDQ
Protein: Sterigmatocystin biosynthesis regulatory protein (Sterigmatocystin biosynthesis cluster protein aflR) (P52957)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Transcription factor; part of the gene cluster that mediates the biosynthesis of sterigmatocystin (ST), a polyketide-derived furanocoumarin which is part of the most toxic and carcinogenic compounds among the known mycotoxins. Binds to the palindromic sequence 5'-TCG(N5)CGA-3'found in the promoter regions of several sterigmatocystin cluster genes to induce their expression.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
Interaction partners:
- Protein-methionine methyltransferase laeA
- Developmental and secondary metabolism regulator veA
- Versicolorin reductase stcU
Sequence:
MEPPAISQQSTPTAPGGTQGTRKLRESCISCSRSKVKCNKEKPTCSRCVRRGLPCEYMVSRRTGRTRVIGVEQPKTAPSPTTPTNTTAATTATKAGPPVTTDSAVHTPVITTAPSPKPVQIQSPPAEPDLWGAILSPNTSTSTDLSSLLSVNTNFSQLFASLSPSLLEGMDGMDAEMHAPELGALSVADPSSSMMQGLEAPNAAQPPSSNTTSHSYCLSICLDTLMRLFPNAGANCERPGHESNPGKLFTIESVIEDNKQILDTAQTILACRCAEDEYVVTLVSLIVFKVLGWYVAAARDRSSDPGREEDFNWSTAQDSRRGSVSSFEEQVLHLPTVVGSYCIDGHHQSRMAAQLVLSELYRVQRLVTQVSRRLESIRRRSSSSSSSASSNTTDSDGGMSTPLSSTTLVHLEDDLRKRLRAVSSETISILRHA
Protein: Phosphatidylinositol N-acetylglucosaminyltransferase GPI3 subunit (GPI-GlcNAc transferase complex subunit GPI3) (GPI-GnT subunit GPI3) (EC 2.4.1.198) (GlcNAc-PI synthesis protein) (P32363)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalytic subunit in the complex catalyzing the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit GPI15
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit GPI1
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit GPI19
- Phosphatidylinositol N-acetylglucosaminyltransferase GPI2 subunit
- N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
- Phosphatidylinositol N-acetylglucosaminyltransferase ERI1 subunit
- GPI-anchor transamidase
- GPI mannosyltransferase 3
- GPI mannosyltransferase 1
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
Sequence:
MGFNIAMLCDFFYPQLGGVEFHIYHLSQKLIDLGHSVVIITHAYKDRVGVRHLTNGLKVYHVPFFVIFRETTFPTVFSTFPIIRNILLREQIQIVHSHGSASTFAHEGILHANTMGLRTVFTDHSLYGFNNLTSIWVNKLLTFTLTNIDRVICVSNTCKENMIVRTELSPDIISVIPNAVVSEDFKPRDPTGGTKRKQSRDKIVIVVIGRLFPNKGSDLLTRIIPKVCSSHEDVEFIVAGDGPKFIDFQQMIESHRLQKRVQLLGSVPHEKVRDVLCQGDIYLHASLTEAFGTILVEAASCNLLIVTTQVGGIPEVLPNEMTVYAEQTSVSDLVQATNKAINIIRSKALDTSSFHDSVSKMYDWMDVAKRTVEIYTNISSTSSADDKDWMKMVANLYKRDGIWAKHLYLLCGIVEYMLFFLLEWLYPRDEIDLAPKWPKKTVSNETKEARET
Protein: Urocortin-2 (Urocortin II) (Ucn II) (Q99ML8)
Organism: Mus musculus (Mouse)
Function: Suppresses food intake, delays gastric emptying and decreases heat-induced edema. Might represent an endogenous ligand for maintaining homeostasis after stress (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:23493376}.
Interaction partners:
- Corticotropin-releasing factor receptor 2
- Corticotropin-releasing factor receptor 1
- Urocortin-3
- Corticoliberin
- Urocortin
- Corticotropin-releasing factor-binding protein
Sequence:
MMTRWALVVFVVLMLDRILFVPGTPIPTFQLLPQNSLETTPSSVTSESSSGTTTGPSASWSNSKASPYLDTRVILSLDVPIGLLRILLEQARYKAARNQAATNAQILAHVGRR
Protein: AT3G26440 protein (Transmembrane protein, putative (DUF707)) (B9DHF0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MANRADNSMRCSNSKKPNDGMMLVISIFAGIVIGFLLGISFPTLSLTKMNFPSSILPSVATVYIENEKPEKSSKTSSQNESDASHHHKIWVPSNPRGAEMLPPSFVAAESDFYLRRLWGLPKDDLPVVKPKYLVAFTVSYEQRKNIDACVKKFSDNFTIVLFHYDGKTSEYDEFEWSKRAIHVSVPKQTKWWYAKRFLHPDIIAPYEYIFIWDEDLGVENFDAEEYIKIVNKHGLEISQPAVESRKSITWKITKRIPGIEVHKEVEEKPGRCNDPHLPPCAGFIEIMAPVFSREAWRCVWHMIQNDLVHGWGLDFALRKCVEPAHEKIGVVDSQWIIHQKIPSLGSQGTAQEGKTAFQGVRERCKREWTMFQKRMTRSEQKYLKEIASASSNSTRT
Protein: Ephrin B3 (Ephrin-B3b) (Q90Z31)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MASRGCVNGLGILLIFLVDLLGITATNMEPIYWNSLNKRFSDDKGYVLYPQIGDRLDLICPSSDPPGPRAPADYEYYKLYLVSSREQADRCEVTGAPNLLLTCDKPNSDMRFTIKFQEYSPNLWGHEFKTNHDYFIIATSDGTRQGLESMRGGVCATQGMKVVLKVGQSPYGLPAKSPKPDSAGRINNPNPGTGNSTHPQIPPRGSGGENGPLPASNIAVIAGAAGGSAFLLLVTAVICVVCYRRRHAKHSESHHPPLSLSSLTSPKRGCGGGVGGGNNNGSEPSDIIIPLRTSDSAYCPHYEKVSGDYGHPVYIVQEMPPQSPANIYYKV
Protein: Small ribosomal subunit protein uS3 (40S ribosomal protein S3) (Q06559)
Organism: Drosophila melanogaster (Fruit fly)
Function: Has DNA repair activity directed towards the mutagenic lesions 8-oxoguanine and abasic sites in DNA. It can cleave DNA containing 8-oxoguanine residues efficiently. Also acts as an ap lyase, cleaving phosphodiester bonds via a beta,delta elimination reaction.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:25858587}. Nucleus {ECO:0000269|PubMed:25858587, ECO:0000269|PubMed:8641296}.
Interaction partners:
- Large ribosomal subunit protein eL18
- Small ribosomal subunit protein eS12
- Large ribosomal subunit protein bL21m
- Small ribosomal subunit protein eS1
- Large ribosomal subunit protein P1
- Elongation factor 1-gamma
- Large ribosomal subunit protein bL20m
- Small ribosomal subunit protein uS5
- Large ribosomal subunit protein uL1
- Large ribosomal subunit protein eL30
Sequence:
MNANLPISKKRKFVSDGIFKAELNEFLTRELAEDGYSGVEVRVTPSRTEIIIMATKTQQVLGEKGRRIRELTAMVQKRFNFETGRIELYAEKVAARGLCAIAQAESLRYKLTGGLAVRRACYGVLRYIMESGAKGCEVVVSGKLRGQRAKSMKFVDGLMIHSGDPCNDYVETATRHVLLRQGVLGIKVKVMLPYDPKNKIGPKKPLPDNVSVVEPKEEKIYETPETEYKIPPPSKPLDDLSEAKVL
Protein: Pentatricopeptide repeat-containing protein At1g62930, chloroplastic (Q9LQ14)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Pentatricopeptide repeat-containing protein At4g21190
- Vacuolar fusion protein MON1 homolog
Sequence:
MTSCVHLGIVASQSKKMSLAKRFAQLRKASPLFSLRGVYFSAASYDYREKLSRNVLLDLKLDDAVDLFGEMVQSRPLPSIVEFNKLLSAIAKMNKFDLVISLGERMQNLRISYDLYSYNILINCFCRRSQLPLALAVLGKMMKLGYEPDIVTLSSLLNGYCHGKRISEAVALVDQMFVMEYQPNTVTFNTLIHGLFLHNKASEAVALIDRMVARGCQPDLFTYGTVVNGLCKRGDIDLALSLLKKMEKGKIEADVVIYTTIIDALCNYKNVNDALNLFTEMDNKGIRPNVVTYNSLIRCLCNYGRWSDASRLLSDMIERKINPNVVTFSALIDAFVKEGKLVEAEKLYDEMIKRSIDPDIFTYSSLINGFCMHDRLDEAKHMFELMISKDCFPNVVTYNTLIKGFCKAKRVEEGMELFREMSQRGLVGNTVTYNTLIQGLFQAGDCDMAQKIFKKMVSDGVPPDIITYSILLDGLCKYGKLEKALVVFEYLQKSKMEPDIYTYNIMIEGMCKAGKVEDGWDLFCSLSLKGVKPNVIIYTTMISGFCRKGLKEEADALFREMKEDGTLPNSGTYNTLIRARLRDGDKAASAELIKEMRSCGFVGDASTISMVINMLHDGRLEKSYLEMLS
Protein: Feruloyl esterase A (EC 3.1.1.73) (Cinnamoyl esterase) (FAE-III) (Ferulic acid esterase A) (O42807)
Organism: Aspergillus niger
Function: Involved in degradation of plant cell walls. Hydrolyzes the feruloyl-arabinose ester bond in arabinoxylans, and the feruloyl-galactose ester bond in pectin. Binds to cellulose.
Subcellular location: Secreted {ECO:0000269|PubMed:9406381, ECO:0000269|Ref.5}.
Interaction partners:
Sequence:
MKQFSAKYALILLATAGQALAASTQGISEDLYNRLVEMATISQAAYADLCNIPSTIIKGEKIYNAQTDINGWILRDDTSKEIITVFRGTGSDTNLQLDTNYTLTPFDTLPQCNDCEVHGGYYIGWISVQDQVESLVKQQASQYPDYALTVTGHSLGASMAALTAAQLSATYDNVRLYTFGEPRSGNQAFASYMNDAFQVSSPETTQYFRVTHSNDGIPNLPPADEGYAHGGVEYWSVDPYSAQNTFVCTGDEVQCCEAQGGQGVNDAHTTYFGMTSGACTW
Protein: Contig An14c0180, genomic contig (A2R3S8)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Interaction partners:
Sequence:
MAPWILGEKFNTVYPHKGSIKALWETKWKFACEKSVYPFHDGAIEDFRPIFQKLIDENINDAYTDAYTQAFFPVAEALENKASAALNNNNVEMASDLLRRAAVVYRISRFPYVDPTREDIKKEAFNRQKKVYLKAASFWKPTIQEVIIPHKHKSATDGAYVPLFVRVPEHATAENPVPVVVLMTGLDGYRPDNSQRTHEIINRGWATVICEIPGTADSPADPSDPESADRQWTTVLDYMATRPEFDMSRVAAWGLSAGGFYAIRAAHTHRDRFVGTLAHGPGCHYFLDPEWLSRVDDHEYPFLLTPAWAKKYGYSNPEDFKKHGQKKFSLLETGILDQPSCRLLLLNGVDDGVTPIEDCLMLFNHGSPKEGRFFHGLPHMGYPHSLVPSYKWFEDVLRSPQEPLKN
Protein: Calcium-transporting ATPase (EC 7.2.2.10) (A8WI68)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|RuleBase:RU361146}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU361146}. Sarcoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004326}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004326}.
Interaction partners:
Sequence:
MAKVIRSGHHGIQMVRAKELVPGDLVEVSVGDKIPADLRLVKIYSTTIRIDQSILTGESVSVIKHTDSVPDPRAVNQDKKNCLFSGTNVASGKARGIVFGTGLTTEIGKIRTEMAETENEKTPLQQKLDEFGEQLSKVISVICVAVWAINIGHFNDPAHGGSWVKGAIYYFKIAVALAVAAIPEGLPAVITTCLALGTRRMAKKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVSKMFIAGQASGDNINFTEFAISGSTYEPVGKVSTNGREINPAAGEFESLTELAMICAMCNDSSVDYNETKKIYEKVGEATETALIVLAEKMNVFGTSKAGLSPKELGGVCNRVIQQKWKKEFTLEFSRDRKSMSAYCFPASGGSGAKMFVKGAPEGVLGRCTHVRVNGQKVPLTSAMTQKIVDQCVQYGTGRDTLRCLALGTIDTPVSVSNMNLEDSTQFVKYEQDITFVGVVGMLDPPRTEVSDSIKACNHAGIRVIMITGDNKNTAEAIGRRIGLFGENEDTTGKAYTGREFDDLPPEQQSEACRRAKLFARVEPSHKSKIVDILQSQGEITAMTGDGVNDAPALKKAEIGISMGSGTAVAKSASEMVLADDNFASIVSAVEEGRAIYNNMKQFIRYLISSNVGEVVSIFMVAALGIPEALIPVQLLWVNLVTDGLPATALGFNPPDLDIMDRHPRSANDGLISGWLFFRYLAVGTYVGVATVGASMWWFLLYEEGPQITYYQLTHWMRCEIEPDNFADLDCAVFEDNHPNAMALSVLVTIEMLNAINSLSENQSLLVMPPWKNIWLMAAISLSMSLHFVILYVDIMATIFQITPLNWVEWIAVLKISLPVLLLDEILKFIARNYIDGKPETVGAKARSAISLLAWVSVTLAYFAWMLGPYAELINHALVGPSVDPSKFDAVVTPDKLHNEL
Protein: Small ribosomal subunit protein mS35 (37S ribosomal protein S24, mitochondrial) (Mitochondrial ribosomal small subunit protein 24) (Q03976)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:11278769, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}. Note=Mitoribosomes are tethered to the mitochondrial inner membrane and spatially aligned with the membrane insertion machinery through two distinct membrane contact sites, formed by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein MBA1. {ECO:0000269|PubMed:25609543}.
Interaction partners:
- Small ribosomal subunit protein bS18m
- Small ribosomal subunit protein uS14m
- Small ribosomal subunit protein bS16m
- Small ribosomal subunit protein mS33
- Small ribosomal subunit protein mS29
- Small ribosomal subunit protein mS23
- Small ribosomal subunit protein uS5m
- Small ribosomal subunit protein uS10m
- Small ribosomal subunit protein uS9m
- Small ribosomal subunit protein bS6m
Sequence:
MKVPLGLWKVSRGNLWSTQKRVLTMSRCLNSDAGNEAKTVREGPAFSADLYMHPEKWKGLPPQRILELYWERMARLGSEYKPNKDELNALLTTSEYSNVPVNDIKKLYHRGEQGAIDIKGGNVNRDNSLRPFMFDELPSQAQELVAQHREQRFYNRLAAYELPLLAQYRQEYKRPSPESHPVTYRYTSYVGEEHPNSRKVVLSVKTKELGLEEKSLHKFRILARSRYDHTTDIFKMSSDKFEHASQNARYLHDILQRLLAESKDLTEDDFSDVPLDTRHTIAKSLRKKKRDYEFPEHWKRPEDAPKKKFDIVDQLLSTL
Protein: Anoctamin-9 (Transmembrane protein 16J) (Tumor protein p53-inducible protein 5) (p53-induced gene 5 protein) (A1A5B4)
Organism: Homo sapiens (Human)
Function: Has calcium-dependent phospholipid scramblase activity; scrambles phosphatidylserine, phosphatidylcholine and galactosylceramide (By similarity). Does not exhibit calcium-activated chloride channel (CaCC) activity. Can inhibit the activity of ANO1.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20056604, ECO:0000269|PubMed:22946059, ECO:0000269|PubMed:29604966}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum {ECO:0000269|PubMed:36520003}. Note=Shows predominantly an intracellular localization with a weak expression in the cell membrane.
Interaction partners:
Sequence:
MQGEESLRILVEPEGDSFPLMEISTCETEASEQWDYVLVAQRHTQRDPRQARQQQFLEELRRKGFHIKVIRDQKQVFFGIRADNSVFGLYRTLLLEPEGPAPHAELAAPTTIPVTTSLRIRIVNFVVMNNKTSAGETFEDLMKDGVFEARFPLHKGEGRLKKTWARWRHMFREQPVDEIRNYFGEKVALYFVWLGWYTYMLVPAALTGLLVFLSGFSLFEASQISKEICEAHDILMCPLGDHSRRYQRLSETCTFAKLTHLFDNDGTVVFAIFMALWATVFLEIWKRQRARVVLHWDLYVWDEEQEEMALQLINCPDYKLRPYQHSYLRSTVILVLTLLMICLMIGMAHVLVVYRVLASALFSSSAVPFLEEQVTTAVVVTGALVHYVTIIIMTKINRCVALKLCDFEMPRTFSERESRFTIRFFTLQFFTHFSSLIYIAFILGRINGHPGKSTRLAGLWKLEECHASGCMMDLFVQMAIIMGLKQTLSNCVEYLVPWVTHKCRSLRASESGHLPRDPELRDWRRNYLLNPVNTFSLFDEFMEMMIQYGFTTIFVAAFPLAPLLALFSNLVEIRLDAIKMVWLQRRLVPRKAKDIGTWLQVLETIGVLAVIANGMVIAFTSEFIPRVVYKYRYSPCLKEGNSTVDCLKGYVNHSLSVFHTKDFQDPDGIEGSENVTLCRYRDYRNPPDYNFSEQFWFLLAIRLAFVILFEHVALCIKLIAAWFVPDIPQSVKNKVLEVKYQRLREKMWHGRQRLGGVGAGSRPPMPAHPTPASIFSARSTDV
Protein: Calcium up-regulated protein C (Q7Z202)
Organism: Dictyostelium discoideum (Social amoeba)
Function: May play an important role in stabilizing and/or regulating the cell membrane during Ca(2+) stress or certain stages of development.
Subcellular location: Cytoplasm. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MINIEDISKSSNQSEEKQLKSTSSKTKYPFAAKSLFKGSNNITPYYLSTSNTFQCVASESIQTWLLSDDGHIFTSSGNFVLDVSSGGYFVELVQLNSNSKTQIWTIDTTNNKIQNQGNGKYLDIDNLNICVAPLNGNATQKWTTFRRAPIPTGNWGYFQSKKLDSNNNYWGLSVLNNSTSYNTSVVMNKVQAKSIGQIWQMTNDGHILSRLDGNLVLDIGPSINGSKTNYYLNTNVYKANDLMQQWGINENNQIFNQYYPNLCIGFVGELGVDSTVNCVLAQPTSAGNINFQWIANPTYSLNQIVSEVPEPFPAYTSGDLLASYQYLSNIATNGYTDDIRSLYTSINVSLEIFYVNVTNATCPSSIHSTEDFSNVQNQIKNELTYAINVRLVFDNYSDFYSKLFSQGSTNLTNLANLINVDMSSDQVVNGDYTDAITSVFYAIISEIPIGGSIIANIGESAVEFGELDAESNDSGPSTYQVTLSKLYDHLNENYENEMANAQSMKNTILQDWGMMSKTFALCFLPTNNPSSLNINGLDFQKISTIASIAYQTAMIQMLLPTNYQIYFTPAGYYAPVSSDDYSYTDSTGTYIMAEIDNCNSHPPKALTDKLWNNGVSKQEVFTSSYGWNLATSVTYYNMVGKYSGMFKLSFPTVKNFTSVPMQFVMTNGSDRVGTFNVKTHFAGLASTYYYSGALGHHYYDIAVIDINGNKVANFTVDNNLEALEGSYVSIKTNSLVVQPGYVVGNPTCNQGSFSQGFAASILIPIYKSN
Protein: Dual specificity protein phosphatase 14 (EC 3.1.3.16) (EC 3.1.3.48) (MKP-1-like protein tyrosine phosphatase) (MKP-L) (Mitogen-activated protein kinase phosphatase 6) (MAP kinase phosphatase 6) (MKP-6) (O95147)
Organism: Homo sapiens (Human)
Function: Involved in the inactivation of MAP kinases. Dephosphorylates ERK, JNK and p38 MAP-kinases.
Interaction partners:
Sequence:
MSSRGHSTLPRTLMAPRMISEGDIGGIAQITSSLFLGRGSVASNRHLLQARGITCIVNATIEIPNFNWPQFEYVKVPLADMPHAPIGLYFDTVADKIHSVSRKHGATLVHCAAGVSRSATLCIAYLMKFHNVCLLEAYNWVKARRPVIRPNVGFWRQLIDYERQLFGKSTVKMVQTPYGIVPDVYEKESRHLMPYWGI
Protein: Phosphoglucomutase-like protein 5 (Aciculin) (Phosphoglucomutase-related protein) (PGM-RP) (Q15124)
Organism: Homo sapiens (Human)
Function: Component of adherens-type cell-cell and cell-matrix junctions. Has no phosphoglucomutase activity in vitro.
Subcellular location: Cell junction, adherens junction {ECO:0000269|PubMed:8175905}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:8175905}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:Q8BZF8}. Note=Concentrated in focal contacts at the ends of actin bundles, and associated with actin filaments. {ECO:0000269|PubMed:8175905}.
Interaction partners:
- UTP--glucose-1-phosphate uridylyltransferase
- Glucose-6-phosphate isomerase
- Phosphopentomutase
- Phosphoacetylglucosamine mutase
- 1,4-alpha-glucan-branching enzyme
- Ornithine transcarbamylase, mitochondrial
- Glycogen phosphorylase, muscle form
- Glycogen phosphorylase, liver form
- Glycogen phosphorylase, brain form
- Dystrophin
Sequence:
MEGSPIPVLTVPTAPYEDQRPAGGGGLRRPTGLFEGQRNYLPNFIQSVLSSIDLRDRQGCTMVVGSDGRYFSRTAIEIVVQMAAANGIGRLIIGQNGILSTPAVSCIIRKIKAAGGIILTASHCPGGPGGEFGVKFNVANGGPAPDVVSDKIYQISKTIEEYAICPDLRIDLSRLGRQEFDLENKFKPFRVEIVDPVDIYLNLLRTIFDFHAIKGLLTGPSQLKIRIDAMHGVMGPYVRKVLCDELGAPANSAINCVPLEDFGGQHPDPNLTYATTLLEAMKGGEYGFGAAFDADGDRYMILGQNGFFVSPSDSLAIIAANLSCIPYFRQMGVRGFGRSMPTSMALDRVAKSMKVPVYETPAGWRFFSNLMDSGRCNLCGEESFGTGSDHLREKDGLWAVLVWLSIIAARKQSVEEIVRDHWAKFGRHYYCRFDYEGLDPKTTYYIMRDLEALVTDKSFIGQQFAVGSHVYSVAKTDSFEYVDPVDGTVTKKQGLRIIFSDASRLIFRLSSSSGVRATLRLYAESYERDPSGHDQEPQAVLSPLIAIALKISQIHERTGRRGPTVIT
Protein: Meiotic recombination protein dmc1 (O42634)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for meiotic recombination and cell cycle progression. Binds to single and double-stranded DNA, in the presence of magnesium, and exhibits DNA-dependent ATPase activity. Promotes DNA strand annealing and strand exchange via DNA recombinase activity and forms helical and stacked ring nucleoprotein filaments.
Subcellular location: Nucleus.
Interaction partners:
- DNA repair protein rhp57
- Meiotic recombination protein rec12
- Homologous-pairing protein 2
- DNA repair protein rhp51
- DNA repair protein rhp55
- Meiotic coiled-coil protein 7
- Meiotic recombination protein rdh54
- Swi5-dependent recombination DNA repair protein 1
- Crossover junction endonuclease mus81
- DNA repair protein rdl1
Sequence:
MEEFAEGNDDEQMIFSDIEDLTAHGIGMTDIIKLKQAGVCTVQGVHMSTKRFLLKIKGFSEAKVDKLKEAASKMCPANFSTAMEISQNRKKVWSISTGSEALNGILGGGIQSMSITEVFGEFRCGKTQMSHTLCVTAQLPRDMGGAEGKVAFIDTEGTFRPDRIKAIAERFGVDADQAMENIIVSRAYNSEQQMEYITKLGTIFAEDGQYRLLIVDSIMALFRVDYSGRGELSERQQKLNIMLARLNHISEEFNVAVFVTNQVQADPGAAMMFASNDRKPVGGHVMAHASATRLLLRKGRGEERVAKLNDSPDMPEAECSYVITPGGIADVS
Protein: KICSTOR subunit 2 (KICSTOR complex protein C12orf66) (Q96MD2)
Organism: Homo sapiens (Human)
Function: As part of the KICSTOR complex functions in the amino acid-sensing branch of the TORC1 signaling pathway. Recruits, in an amino acid-independent manner, the GATOR1 complex to the lysosomal membranes and allows its interaction with GATOR2 and the RAG GTPases. Functions upstream of the RAG GTPases and is required to negatively regulate mTORC1 signaling in absence of amino acids. In absence of the KICSTOR complex mTORC1 is constitutively localized to the lysosome and activated. The KICSTOR complex is also probably involved in the regulation of mTORC1 by glucose.
Subcellular location: Lysosome membrane {ECO:0000305|PubMed:28199306}.
Interaction partners:
- GATOR1 complex protein DEPDC5
- KICSTOR complex protein SZT2
- KICSTOR complex protein ITFG2
- GATOR1 complex protein NPRL2
- KICSTOR complex protein kaptin
- GATOR2 complex protein WDR24
- GATOR2 complex protein WDR59
- S-adenosylmethionine sensor upstream of mTORC1
- GATOR1 complex protein NPRL3
- GATOR2 complex protein MIOS
Sequence:
MGESIPLAAPVPVEQAVLETFFSHLGIFSYDKAKDNVEKEREANKSAGGSWLSLLAALAHLAAAEKVYHSLTYLGQKLGGQSFFSRKDSIRTIYTSLHNELKKVVTGRGALGGTAPHVEELLSHLSEQLCFFVQARMEIADFYEKMYTLSTQKFINAEELVGLLDAIMKKYSSRFHHPILSPLESSFQLEVDVLCHLLKAQAQVSEWKFLPSLVNLHSAHTKLQTWGQIFEKQRETKKHLFGGQSQKAVQPPHLFLWLMKLKNMLLAKFSFYFHEALSRQTTASEMKTLTAKANPDFFGKISSFIRKYDAANVSLIFDNRGSESFQGHGYHHPHSYREAPKGVDQYPAVVSLPSDRPVMHWPNVIMIMTDRTSDLNSLEKVVHFYDDKVQSTYFLTRPEPHFTIVIIFESKKSERDSHFISFLNEVSLALKNPKVFASLKPGAKG
Protein: V-type proton ATPase 16 kDa proteolipid subunit c (Vacuolar proton pump 16 kDa proteolipid subunit c) (Q9VFE3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- V-type proton ATPase subunit B
- V-type proton ATPase subunit E
- V-type proton ATPase subunit d 1
- V-type proton ATPase subunit S1
- V-type proton ATPase subunit G
- ATPase H
- V-type proton ATPase subunit H
- V-type proton ATPase subunit a
- V-type proton ATPase catalytic subunit A isoform 2
- V-type proton ATPase subunit F 1
Sequence:
MAAQIRTVVSQTFLWLFLAVATILTLYFVMTGKGERVSVGWFLASSNPYMWACLGIGLSVSLSVVGAALGIHTTGTSIVGGGVKAPRIKTKNLISVIFCEAVAIYGLITAIVLSGQLEQFSMETALSQAAIQNTNWFSGYLIFGAGLAVGLVNLFCGIAVGIVGSGAALSDAANAALFVKILIVEIFGSAIGLFGLIVGIYMTSKSKMGDKE