wanglab/gogpt-training-data huggingface dataset:
Protein: Beta-alanine transporter (BalaT) (Q961J5)
Organism: Drosophila melanogaster (Fruit fly)
Function: Beta-alanine transporter required for the uptake of beta-alanine by the glia. Required for the recycling process of the neurotransmitter histamine in photoreceptor neurons of the compound eye and therefore for photoreceptor synaptic transmission. Following histamine release from photoreceptors and its uptake by glia, histamine is conjugated to beta-alanine by e/Ebony to form the inactive metabolite, carcinine.
Subcellular location: Cell membrane {ECO:0000269|PubMed:28806173}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MDFDEVLREVGSFGLYQKVIICSVLLPAALPCAFHAYSQLFIAATPQHFCRVPELEPWTQDYVQLVKNLSIPRNRNGAYAECSMYSRNYTDIVRYLEYRPPPDLLRQQAEDLLKLQPDTTQVVPCQHGWHYDKSIYSSTVVQEWNLVCDRSFLVTLALVVFGVGGLLGNYVFGYLVDLWGRRPSFYAYLLLEIIACAASAFAWNYYTWLGLRFVVGLTVPAILASPYVLAIELVGPERRVFCTIVSNIAYSLGLVVLAGVIYIVRDWRELSLAVSMPLLMLFSCFFVLPESPRWLMAVGKTRRAIKILKVMARVNGVRVNRDFVERLQRKLVITRAAETKSSMTTHYGILDLFRGPNMRRKTLIITLIWFANTSVYVGLSYYAPALGGDEIWNFFLAGAVELPTYLLLWPGLSYFGRRWILFISMLVGGVACVATFLYPDITLLLYCVGKMGISSSFVVLPLMASELYPTVVRGLGMSFSSVISMVGPIVIPMINHMGQQMLVLPLIVMGALLILGGFASLLLPETRNRNLPQTLEEGEAVPLSFLLCCCVESERKPNNIRASPKKRILPEAGTPVFHRVDTPVSDRVPCKIVCSICKNEMRTL
Protein: Multifunctional tryptophan biosynthesis protein [Includes: Anthranilate synthase component 2 (AS) (EC 4.1.3.27) (Anthranilate synthase, glutamine amidotransferase component); Indole-3-glycerol phosphate synthase (EC 4.1.1.48) (PRAI)] (P00937)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Chorismate synthase ARO2
- Aminodeoxychorismate synthase
- Tryptophan synthase
- Anthranilate synthase component 1
- Anthranilate phosphoribosyltransferase
- N-
- Chorismate mutase
- Pentafunctional AROM polypeptide
- Probable prephenate dehydratase
- 1-
Sequence:
MSVHAATNPINKHVVLIDNYDSFTWNVYEYLCQEGAKVSVYRNDAITVPEIAALNPDTLLISPGPGHPKTDSGISRDCIRYFTGKIPVFGICMGQQCMFDVFGGEVAYAGEIVHGKTSPISHDNCGIFKNVPQGIAVTRYHSLAGTESSLPSCLKVTASTENGIIMGVRHKKYTVEGVQFHPESILTEEGHLMIRNILNVSGGTWEENKSSPSNSILDRIYARRKIDVNEQSKIPGFTFQDLQSNYDLGLAPPLQDFYTVLSSSHKRAVVLAEVKRASPSKGPICLKAVAAEQALKYAEAGASAISVLTEPHWFHGSLQDLVNVRKILDLKFPPKERPCVLRKEFIFSKYQILEARLAGADTVLLIVKMLSQPLLKELYSYSKDLNMEPLVEVNSKEELQRALEIGAKVVGVNNRDLHSFNVDLNTTSNLVESIPKDVLLIALSGITTRDDAEKYKKEGVHGFLVGEALMKSTDVKKFIHELCE
Protein: Olfactory receptor 2T1 (Olfactory receptor 1-25) (OR1-25) (Olfactory receptor OR1-61) (O43869)
Organism: Homo sapiens (Human)
Function: Odorant receptor.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
Sequence:
MWQEYYFLNVFFPLLKVCCLTINSHVVILLPWECYHLIWKILPYIGTTVGSMEEYNTSSTDFTFMGLFNRKETSGLIFAIISIIFFTALMANGVMIFLIQTDLRLHTPMYFLLSHLSLIDMMYISTIVPKMLVNYLLDQRTISFVGCTAQHFLYLTLVGAEFFLLGLMAYDRYVAICNPLRYPVLMSRRVCWMIIAGSWFGGSLDGFLLTPITMSFPFCNSREINHFFCEAPAVLKLACADTALYETVMYVCCVLMLLIPFSVVLASYARILTTVQCMSSVEGRKKAFATCSSHMTVVSLFYGAAMYTYMLPHSYHKPAQDKVLSVFYTILTPMLNPLIYSLRNKDVTGALKRALGRFKGPQRVSGGVF
Protein: GH03216p (Q8MZ57)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MQPFSSKRVEGVGNSTVALLVRHRPGQAYITPNKPVVHVGNGVTLTCSANPPGWPVPQYRWFRDMDGDIGNTQKILAQGPQYSIPKAHLGSEGKYHCHAVNELGIGKIATIILEVHQPPQFLAKLQQHMTRRVGDVDYAVTCSAKGKPTPQIRWIKDGTEILPTRKMFDIRTTPTDAGGGVVAVQSILRFRGKARPNGNQLLPNDRGLYTCLYENDVNSANSSMHLRIEHEPIVIHQYNKVAYDLRESAEVVCRVQAYPKPEFQWQYGNNPSPLTMSSDGHYEISTRMENNDVYTSILRIAHLQHSDYGEYICRAVNPLDSIRAPIRLQPKGSPEKPTNLKILEVGHNYAVLNWTPGFNGGFMSTKYLVSYRRVATPREQTLSDCSGNGYIPSYQISSSSSNSNHEWIEFNCFKENPCKLAPLDQHQSYMFKVYALNSKGTSGYSNEILATTKVSKIPPPLHVSYDPNSHVLGINVAATCLSLIAVVESLVTRDATVPMWEIVETLTLLPSGSETTFKEAIINHVSRPAHYTTATTSGRSLGVGGGSHLGEDRTMALAETAGPGPVVRVKLCLRSNHEHCGAYANAEIGKSYMPHKSSMTTSALVAIIIASLSFVVFLGLLYAFCHCRRKHAAKKESSSVGGGVGGGNANATANPGSTGAKEYDLDLDASRRPSLSQDPQQSQQQPPPPPPYYPTGTLDSKDIGNGNGGMELTLTALHDPDEQLNMQQQQHHSNHGQYQQPKAILGIYGGVAGSGGNNSGGQHPHSNGYGYHVTSAIGVDSDSYQVLPSVANSAAGSHGHGSGHGHGLGAGE
Protein: ATP-dependent protease ATPase subunit HslU (Unfoldase HslU) (P43773)
Organism: Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Function: ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- ATP-dependent protease subunit HslV
- Chaperone protein DnaJ
- Chaperone protein HtpG
- Chaperone protein ClpB
- Co-chaperonin GroES
- Protein GrpE
- Chaperonin GroEL
- ATP-dependent Clp protease ATP-binding subunit ClpX
- Uncharacterized protein HI_1159
- Lon protease
Sequence:
MSEMTPREIVSELDQHIIGQADAKRAVAIALRNRWRRMQLQEPLRHEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEVGYVGKEVDSIIRDLTDSAMKLVRQQEIAKNRARAEDVAEERILDALLPPAKNQWGEVENHDSHSSTRQAFRKKLREGQLDDKEIEIDVSAGVSMGVEIMAPPGMEEMTNQLQSLFQNLGSDKTKKRKMKIKDALKALIDDEAAKLINPEELKQKAIDAVEQNGIVFIDEIDKICKKGEYSGADVSREGVQRDLLPLVEGSTVSTKHGMVKTDHILFIASGAFQVARPSDLIPELQGRLPIRVELTALSAADFERILTEPHASLTEQYKALMATEGVNIAFTTDAVKKIAEAAFRVNEKTENIGARRLHTVMERLMDKISFSASDMNGQTVNIDAAYVADALGEVVENEDLSRFIL
Protein: Pericentrin-like protein, isoform P (M9ND93)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|ARBA:ARBA00004300}.
Interaction partners:
Sequence:
MADQRTTTTTTTTATTATTPSSANILATTATTTTTTSSSIEEEIEEAIEISEVEEQLNTPLESLSEAAAYARPKDEQSSAKSLSSNPAEDEDADEFRIDDAQLSGGQLAQHFLVDEDESEEGSDLPAASKVEVSLSSNDDDFDISLPLEQRKPVHSLHEDDESVDQSLSNQSTTDDVSELVEEPVHEMDDKTDGSAAISASAPQETQVDESQITDEQDHSMEEIVATNESIEVTYEAEETVNTSQKQDLITDLDEESEDQVHVDNRPTSTLQALKLPALQQPQIVERKAATALTTLRLQADVLEPLELTILEMDDDENEEDDDDEESSLQLMKLRLMAMNQQMIVDNAPKLSPTEAEQTQVTSSSNNLEIKQMERVPLTEFSKDVLEDITEESERLLSMSTTMEEEQDPPSLSLDESKTLLQPGAHKTGGSSSSLVSLNMLKQLEAKVQELHTQLETKDNCLASLNLQLETARRESSAGPASARDSSSLMTNSTEYRTLQEELGGPTLDIYVEMSRRDELIAKLTDSLQQSLNVRDKLQVDADRLGGEVQNLRRQLQETLDAVKRSSAVWPDQECNPGQRISEISMDLISESDDDLDRHFLTDNEERGSRSSKERQLTQLQTNEELGLQASNPEWTPTFSKQIEQFHTYLLPTEQRIFQMVQRKFDDYLNQQITLCRDLGAQELKIARDQWESEKLTSEQNQQAAHAKQMEDLRKYFEHKCADLEKQFSDDVFSHKSQHQTGDSSSECSEVDQLPEEGAAAVSSKEPSPRKRKRAELLLSPSHRQMTPCGLDSLGENTGKTEKDNTADIADLKIFYQTHIKELKRAHEDQVRKLSDRIKFYERQQGDDDYKPATESPERTCPDQESAGGVANTSLIIIDEDELNFNNESQVIQRIIEEYEKRLQEQLALARQDIATELEQQIKSLLSENTVDDQHWPKELILLREKFTAKSQLEITQLNIKHAEEMSRLKLEFEKQLNRKNKRHLTFDAARDLEQVICERDGLRELSKSFRSVLCRLAKCVAHCEEDLNATLSEEVQRLLFHSRSQDGGDDLEATISSSLNNTKHMLRVPDVHSLLEVVEDPSLVQFIDSKSNEEPSEDFDLNDCLERLKSEASYLLHLSEDLHKQRTHDESSEHLDEPEKQEHELCCEAEDGLKTTGAVNQQVLSKFLRTNSLNDQQMGVANQRKNSNPEAGKTHSSLPPDLQEHAGNASELSFQLVQLKNRLIKSEADRQNLQQQLSRTIDRNAELGQELQALRDQLSQLNSLNHTDYNEGYGLGTMKSLQEQGLDQSSASFLALQERARHLLSSSPVKEQPSRDHGNSTVILLQMIEDFCREGDKVVEFSKKDREDLQSQIDTADKQLKDTRRFLEDQAAEREQERDEFQREIERLKAQLRDKEKEHSSYANASEELKVAKRKHYAQLESQFREVNQQLCESNAKRDKFEVELKASIDKIFVLREIISELETQVQTKALNEEVLAEKAQQLEEYVSLQMRDNDILQQEVHSLKTDIGEGYQSRIRVLEEKLKQSGPTAEQGVVLSQVAEKLRDIETTLDQKTKALESLHNSNATSNSASLSVTEDVSIHGSKEPTAVGSPSHPSLTVEGVQRVTEKLDRHTRVEEAAIKRIRDLEMQVHQMRAGCVELQHERDTLQGRMEEQTQRISTLQNRLEEQRQRAEQLHRTGTSDLNTRVHELQGEVQNLYEQLAARDKQMANMRQQLQRSKEEITRLETEVEVRTQPDRSLVNKLQAEVQQKGAEIVKLKDKIRTEMINRLAIPDLMETMLADKNDEIDHLRDQLEAKEKELQASQQEASQISSPSGAAGKQEGSGGKLSARTLSDIGSITEFPEPDVERRAAMRSLTALQMSEGAGGFLHQTMETSKEAVANLTHKRTDDLSGFIVPYPVNTFEHPHYFQALGVTAQSTDGLTPGLVPRQINFSNLTEDSKLKTTSLLMHTPELPRPTTPPEIHQLRVKLSDLQTEKQRQQSELEKKLQDLQKELEQEKEKLSRQAQTLQSYEESEAKYRLRIENLESKVLETAAQAASDRENLRKELNCVSAAHEQCENAAAARKRELEKLNSEVKVKADQLHAALRRCADLELQVLTLERDLERLKNSDNSSKQYSVDEIAQQVEKELNYSAQLDSNILKAIESEEENNLDKKLQKGVQTEEETLPGTGNGTDDENFTGERELLNQLEALRAQLAVEREQCEAMSKELLGEKQHSQDIQEQDVIIIEAMRKRLETALDAEDELHKQLDQERERCERLQTQLTSLQRAESRRNSSLLLKSPGDSPRKSPRADFESELGDRLRSEIKLLVAQNERERERSADAQRSSERERQRYEKELQERVAYCERLKQEMEKLSRDKESAETELEHFNERLTLQASEIESLEARLVTLQEAETRRANTRTRQHQENVKLQAEIHELKSKLLAAEAARDCLDQKVTQLRFDVSRSGQREAKLAEALAQANDRLAHSTDDNVPAQFMQKMKEINALLAENTQENRQMAETVQFLVGERIALQKKCEELGGAGNTNVTELEERCRQLIGRYLRVESHRKALVYQKRYLKLTLEGYQASEQLALQNLRGGAEQPPQRNIKKKFKTVALAIIAIQRIKYIGRIWHTGKRIVSKSVFTITQQRSPGLNLNVAPPQSPLPGPNSNLPTNNNNLMGRLSYAPLSPPMVNFSTVQPIMLPSDFTLQAPTTSLQTTIANNNSENTLPSLARLDWPTMQKPKRAHARHH
Protein: Transcription factor TCP3 (Q9MAH8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays a pivotal role in the control of morphogenesis of shoot organs by negatively regulating the expression of boundary-specific genes such as CUC genes, probably through the induction of miRNA (e.g. miR164). Participates in ovule develpment.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Transcription factor TCP15
- Transcription factor TCP14
- Transcription factor TCP8
- Transcription factor TCP21
- Transcription factor TCP20
- Transcription factor TCP19
- Protein ASYMMETRIC LEAVES 2
- Transcription factor TCP23
- Transcription factor TCP16
- Transcription factor TCP7
Sequence:
MAPDNDHFLDSPSPPLLEMRHHQSATENGGGCGEIVEVQGGHIVRSTGRKDRHSKVCTAKGPRDRRVRLSAPTAIQFYDVQDRLGFDRPSKAVDWLITKAKSAIDDLAQLPPWNPADTLRQHAAAAANAKPRKTKTLISPPPPQPEETEHHRIGEEEDNESSFLPASMDSDSIADTIKSFFPVASTQQSYHHQPPSRGNTQNQDLLRLSLQSFQNGPPFPNQTEPALFSGQSNNQLAFDSSTASWEQSHQSPEFGKIQRLVSWNNVGAAESAGSTGGFVFASPSSLHPVYSQSQLLSQRGPLQSINTPMIRAWFDPHHHHHHHQQSMTTDDLHHHHPYHIPPGIHQSAIPGIAFASSGEFSGFRIPARFQGEQEEHGGDNKPSSASSDSRH
Protein: Endoglucanase 3 (EC 3.2.1.4) (Cellulase 5) (AtCEL5) (Endo-1,4-beta glucanase 3) (Q2V4L8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in the sloughing (cell-cell separation) of the root cap cells from root tip.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Beta-glucosidase 12
- Beta-glucosidase 43
- Protein COFACTOR ASSEMBLY OF COMPLEX C SUBUNIT B CCB3, chloroplastic
Sequence:
MASPFFFVFLLSALSLENTYASPNYREALSKSLLFFQGQRSGRLPSDQQLSWRSSSGLSDGSSAHVDLTGGYYDAGDNVKFNFPMAFTTTMLSWSSLEYGKKMGPELQNSRVAIRWATDYLLKCARATPGKLYVGVGDPNGDHKCWERPEDMDTPRTVYSVSPSNPGSDVAAETAAALAASSMVFRKVDPKYSRLLLATAKKVMQFAIQYRGAYSNSLSSSVCPFYCSYSGYKDELLWGAAWLHRATNDPYYTNFIKSLGGGDQPDIFSWDNKYAGAYVLLSRRAVLNKDNNFELYKQAAENFMCKILPNSPSSSTKYTKGGLMYKLPQSNLQYVTSITFLLTTYAKYMKSTKQTFNCGNSLIVPNALINLSKRQVDYVLGVNPMKMSYMVGFSSNFPKRIHHRGSSLPSRAVRSNSLGCNGGFQSFRTQNPNPNILTGAIVGGPNQNDEYPDQRDDYTRSEPATYINAAFVGPLAYFAASRSP
Protein: F-box/kelch-repeat protein KIB1 (Protein KINK SUPPRESSED IN BZR1-1D 1) (Q9SU05)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins. Required for brassinosteroid (BR) signal transduction. Mediates ASK7/BIN2/SK21 inactivation both by competing with substrate binding (e.g. BZR1) and by promoting its ubiquitination and subsequent proteasomal degradation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:28575660}. Nucleus, nucleolus {ECO:0000269|PubMed:28575660}. Note=Mostly localized in the nucleolus, and, to a lower extent, in the cytoplasm. {ECO:0000269|PubMed:28575660}.
Interaction partners:
- Serine/threonine-protein phosphatase BSU1
- Shaggy-related protein kinase eta
- Serine/threonine-protein kinase BSK1
- F-box/kelch-repeat protein At1g24800
- Serine carboxypeptidase 24
- F-box/kelch-repeat protein At1g25055
- Protein BRASSINAZOLE-RESISTANT 2
- F-box protein At5g36730
- F-box protein At5g36820
- Protein BRASSINAZOLE-RESISTANT 1
Sequence:
MTHKKQKKEMSDSEKKTFNEDSKHSILAVDLVRLILERLSFVDFHRARCVSSIWYIASKTVIGVTNPTTPWLILFPKGDVEIKKDSCKLYDPHENKTYIVRDLGFDLVTSRCLASSGSWFLMLDHRTEFHLLNLFTRVRIPLPSLESTRGSDIKIGNAVLWVDEQRKDYLVVWNISSLFGYHKKGDDRWKVFKPLENERCIIAMVFKENKLYVLSVDGNVDVFYFSGNDSPVRCATLPSSPLRKGHKVVVTLSGEVLIIVAKVEPYPRTRLCFFAVYKMDPKSSRWETIKSLAGEALILDLGITVEAKVMKNCIYFSNDQFHRYNENSLWNVSNKSGVFVYHFRSANVVQLVELLTASSRTSKILFKDARCFFPTFTSKWLL
Protein: ATP-binding cassette sub-family C member 6 (EC 7.6.2.-) (EC 7.6.2.3) (MRP-like protein 1) (MLP-1) (Multidrug resistance-associated protein 6) (O88269)
Organism: Rattus norvegicus (Rat)
Function: ATP-dependent transporter of the ATP-binding cassette (ABC) family that actively extrudes physiological compounds, and xenobiotics from cells. Mediates ATP-dependent transport of glutathione conjugates such as leukotriene-c4 (LTC4) and N-ethylmaleimide S-glutathione (NEM-GS) (in vitro) (By similarity). Transports also an anionic cyclopentapeptide endothelin antagonist, BQ-123. May contribute to regulate the transport of organic compounds in testes across the blood-testis-barrier (By similarity).
Subcellular location: Basolateral cell membrane {ECO:0000269|PubMed:10692506, ECO:0000269|PubMed:28111129}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:33058196}; Multi-pass membrane protein {ECO:0000255}. Lateral cell membrane {ECO:0000269|PubMed:10692506}; Multi-pass membrane protein {ECO:0000255}. Basal cell membrane {ECO:0000250|UniProtKB:O95255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Vitamin K-dependent gamma-carboxylase
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
- Matrix Gla protein
Sequence:
MNGEHSMATPGESCAGLRVWNQTEQEPVAYHLLNLCFLRAAGSWVPPMYLWVLGPIYLLYIHRHGCCYLRMSRLFKIKMVLGFALILLYTFNAAVPLWRIHRGMPQAPELLIHPTVWLTTMSFATFLIHMERKKGVRASGLLFGYWLLCCLVPAIDTVQQASAGSFRQEPLHHLATYLCLSLVVAELVLSCLVDQPPFFSEDSKPLNPCPEAEASFPSKAMFWWASGLLWKGYRKLLGPKDLWSLERENSSEELVSQLEREWRRNFSELPGHKGHSGMGTPETEAFLQPERSQRGPLLRAIWRVFRSTFLLGTLSLVISDAFRFAVPKLLSLFLEFMGDLESSAWTGWLLAVLMFLSACLQTLFEQQYMYRVKVLQMRLRTAITGLVYRKVLVLSSGSRKSSAAGDVVNLVSVDVQRLVESILHLNGLWLLFLWIIVCFVYLWQLLGPSALTAVAVFLSLLPLNFFITKKRSFHQEEQMRQKASRARLTSSMLRTVRTIKSHGWECAFLERLLHIRGQELGALKTSAFLFSVSLVSFQVSTFLVALVVFAVHTLVAEDNAMDAEKAFVTLTVLSILNKAQAFLPFSVHCLVQARVSFDRLAAFLCLEEVDPNGMVLSPSRCSSKDRISIHNGTFAWSQESPPCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGSVAYVPQEAWVQNTSVVENVCFRQELDLPWLQEVLEACALGSDVASFPAGVHTPVGEQGMNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEVFKQVIGPSGLLQGTTRILVTHTLHVLPQADQILVLANGTIAEMGSYQDLLHRNGALVGLLDGARQPAGEGEGEAHAAATSDDLGGFSGGGTPTRRPERPRPSDAAPVKGSTSEAQMEPSLDDVEVTGLTAGEDSVQYGRVKSATYLSYLRAVGTPLCTYTLFLFLCQQVASFCQGYWLSLWADDPVVDGKQMHSALRGSIFGLLGCLQAIGLFASMAAVFLGGARASCLLFRSLLWDVARSPIGFFERTPVGNLLNRFSKETDIVDVDIPDKMRTLLTYAFGLLEVGLAVSMATPLAIVAILPLMLLYAGFQSLYVATCCQLRRLESASYSSVCSHLAETFQGSQVVRAFQAQGPFTAQHDALMDENQRISFPRLVADRWLAANLELLGNGLVFVAATCAVLSKAHLSAGLAGFSVSAALQVTQTLQWVVRSWTDLENSMVAVERVQDYVHTPKEAPWRLPSSAAQPLWPCGGQIEFRDFGLRHRPELPMAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTLRSRITIIPQDPVLFPGSLRMNLDLLQENTDEGIWAALETVQLKAFVTSLPGQLQYECSGQGDDLSVGQKQLLCLARALLRKTQILILDEATASVDPGTEIQMQAALERWFAQCTVLLIAHRLRSVMNCARVLVMDEGQVAESGSPAQLLAQKGLFYRLAQESGLA
Protein: Nucleus-vacuole junction protein 1 (P38881)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the formation of nucleus-vacuole (NV) junctions during piecemeal microautophagy of the nucleus (PMN). NV junctions are interorganelle interfaces mediated by NVJ1 in the nuclear envelope and VAC8 on the vacuole membrane. Together, NVJ1 and VAC8 form Velcro-like patches through which teardrop-like portions of the nucleus are pinched off into the vacuolar lumen and degraded by the PMN process. Acts also as an outer-nuclear membrane receptor for OSH1 and TSC13.
Subcellular location: Nucleus outer membrane {ECO:0000269|PubMed:10888680, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15367582, ECO:0000269|PubMed:16912077}; Single-pass membrane protein {ECO:0000269|PubMed:10888680, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15367582, ECO:0000269|PubMed:16912077}.
Interaction partners:
- Vacuolar protein 8
- Oxysterol-binding protein homolog 1
- Very-long-chain enoyl-CoA reductase
- Structural protein MDM1
- Nucleus-vacuole junction protein 2
- Uncharacterized protein YDR179W-A
- Membrane-anchored lipid-binding protein LAM6
- Autophagy-related protein 39
Sequence:
MTRPPLVRGIFSLGLSVAVLKGVEKTVRKHLERQGWIEPQKVDYELIFTIDRLKNLVDNKREALTAEQPDAGELSWRKVFNFISRQSSELDTRIYVLILLLSFLLPIAWTVLDGDRETTLEDKDNDCNVDLIENERRLKHYNDGERAVLQFGKNRSEPIILSYKDMNVLEGEHEFTSKEEHSNSHLTSKSENALNQVGSEDLLGCHLEKQLEEDKNEPNGEADGEDDNNREKDCSSSSEVESQSKCRKESTAEPDSLSRDTRTTSSLKSSTSFPISFKGSIDLKSLNQPSSLLHIQVSPTKSSNLDAQVNTEQAYSQPFRY
Protein: Preprofallaxidin-5 [Cleaved into: Fallaxidin-5.1] (B5LUQ6)
Organism: Litoria fallax (Eastern dwarf tree frog) (Hylomantis fallax)
Subcellular location: Secreted {ECO:0000250|UniProtKB:P82881}.
Interaction partners:
Sequence:
MASLKKSLFLVLFLGFVSLSICEEEKREDKEDEGENEEAEENHEERSEEKRFLPLLASLVGGLLGKRS
Protein: FI02826p (Q9VPF1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Protein pinocchio
- LD33695p
Sequence:
MTTPLQTRMALAEIPDRLEALRMANTPTNSNRRTPDEPTPAAIINTPNANGGLGLRVDNDVNVVQAQDFVFSPLPSPDELVIRQRGRRRFTTTYSPDKVNGGGGAGGGASGGSSMRSPFQRTPTKNFQLTSGMILRSSPRKRLTMGSTPPEPTPMDTYSPIKMATTKQLWPGTPVVKKLKMEDRPVGQTNTDATLPSLLQGLSQEQLIDLIMNNIKSASDEGEIRTQLPTPDISALEQDLHHAKRLIFKSLPTSRLCKKTDAAAYSKASMHLNEFKRVLQSQAKRLHDSTHWDALVDYVSMAWQCVASTPNWESHAHNAVRRQCFKLLACSCYAAIKHGGMRLGQLRLETLERNLREWSKDYEDVLSCVNALQRTLNSRSSL
Protein: 3'-phosphoadenosine 5'-phosphate phosphatase (PAP phosphatase) (EC 3.1.3.7) (3'(2'),5'-bisphosphate nucleotidase) (3'(2'),5-bisphosphonucleoside 3'(2')-phosphohydrolase) (D-fructose-1,6-bisphosphate 1-phosphohydrolase) (DPNPase) (Fructose-1,6-bisphosphatase) (FBPase) (EC 3.1.3.11) (Inositol-1-monophosphatase) (I-1-Pase) (IMPase) (EC 3.1.3.25) (Inositol-1-phosphatase) (P9WKJ1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Phosphatase with a broad specificity. Its primary physiological function is to dephosphorylate 3'-phosphoadenosine 5'-phosphate (PAP) and 3'-phosphoadenosine 5'-phosphosulfate (PAPS). Thus, plays a role in mycobacterial sulfur metabolism, since it can serve as a key regulator of the sulfate assimilation pathway by controlling the pools of PAP and PAPS in the cell. To a lesser extent, is also able to hydrolyze inositol 1-phosphate (I-1-P), fructose 1,6-bisphosphate (FBP) (to fructose 6-phosphate (F-6-P)) and AMP in vitro, but this might not be significant in vivo. Glucose-1-phosphate (G-1-P), p-nitrophenyl phosphate (pNPP), and beta-glycerol phosphate (beta-GP) are also good substrates, compared to I-1-P. With much lower efficiency, can also hydrolyze inositol 2-phosphate (I-2-P) and glucose-6-phosphate (G-6-P) in vitro, but not fructose-6-phosphate (F-6-P) and trehalose-6-phosphate (T-6-P).
Interaction partners:
- Bifunctional enzyme CysN/CysC
- Adenosine 5'-phosphosulfate reductase
- Bifunctional oligoribonuclease and PAP phosphatase NrnA
- Sulfate adenylyltransferase subunit 2
- Oligoribonuclease
- L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligase
- Histidinol-phosphatase
- Inositol-1-monophosphatase SuhB
Sequence:
MVSPAAPDLTDDLTDAELAADLAADAGKLLLQVRAEIGFDQPWTLGEAGDRQANSLLLRRLQAERPGDAVLSEEAHDDLARLKSDRVWIIDPLDGTREFSTPGRDDWAVHIALWRRSSNGQPEITDAAVALPARGNVVYRTDTVTSGAAPAGVPGTLRIAVSATRPPAVLHRIRQTLAIQPVSIGSAGAKAMAVIDGYVDAYLHAGGQWEWDSAAPAGVMLAAGMHASRLDGSPLRYNQLDPYLPDLLMCRAEVAPILLGAIADAWR
Protein: Fructose-bisphosphate aldolase (FBP aldolase) (EC 4.1.2.13) (Q5BAU6)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Triosephosphate isomerase
- Triosephosphate isomerase
- ATP-dependent 6-phosphofructokinase
- Glyceraldehyde-3-phosphate dehydrogenase
- Glyceraldehyde-3-phosphate dehydrogenase
- Fructose-1,6-bisphosphatase
- Transketolase
- Glucose-6-phosphate isomerase
- transketolase
- Transketolase-like pyrimidine-binding domain-containing protein
Sequence:
MPLNKPNPALSILDHASKNNYAVPAMCVYNVEGILATVRAANKKRSPAMIQLFPWALHYADGLLVHAAAEAAKSAEVPVTVSMDHAQTPEIIRRAADIGGFDSIMVDMSHYEKEENLRLTRELVAYCHERGIATEAEPGRIEGGEDGVADTAELEGLLTTPEESEEFVDTGIDWLAPAFGNVHGEYGPRGIQLEYERLKSINEKVGDRVRLVLHGADPFTEEIFRKCIECGVSKVNINKVLNNEYVKVQREKAGRVPLTQLLEEATDEMQKAVEKCMDMLGSTGRY
Protein: Probable GDP-L-fucose synthase (EC 1.1.1.271) (GDP-4-keto-6-deoxy-D-mannose-3,5-epimerase-4-reductase) (GER) (Protein FX) (Q9W1X8)
Organism: Drosophila melanogaster (Fruit fly)
Function: Catalyzes the two-step NADP-dependent conversion of GDP-4-dehydro-6-deoxy-D-mannose to GDP-fucose, involving an epimerase and a reductase reaction.
Interaction partners:
- GDP-mannose 4,6 dehydratase
- Large ribosomal subunit protein eL19
- Ubiquitin-conjugating enzyme E2-18 kDa
- Small ribosomal subunit protein eS1
- Large ribosomal subunit protein uL14
- Probable tRNA N6-adenosine threonylcarbamoyltransferase
- 40S ribosomal protein S15
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein eS4
- Small ribosomal subunit protein uS17
Sequence:
MKKVLVTGGTGLVGKALEAVIKEQSPEDEQWFFAGSKDADLTNLAATQALFAREKPTHVIHLAAMVGGLFHNMNNNLDFLRNNLLINDNVLQTAHEQGCVKVVSCLSTCIFPDKTSYPIDETMVHNGPPHPSNYGYSYAKRLIDVQNHAYHDKYGRVYTSVIPCNIFGPHDNYNPEVSHVIPGMIYRMHQLVTEKTDVPENDKVFTVFGSGMPLRQFVYSRDLAELMIWVLRNYESVEPIILSADEVQEVTIFEVAQAVAKAFNFNGRLVCDTSKSDGQYKKTASNAKLRSFLPDYAFTDLETAINASVKWYIENYDQARK
Protein: KICSTOR subunit 2 (F5H2Q3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGESIPLAAPVPVEQAVLETFFSHLGGQSFFSRKDSIRTIYTSLHNELKKVVTGRGALGGTAPHVEELLSHLSEQLCFFVQARMEIADFYEKMYTLSTQKFINAEELVGLLDAIMKKYSSRFHHPILSPLESSFQLEVDVLCHLLKAQAQVSEWKFLPSLVNLHSAHTKLQTWGQIFEKQRETKKHLFGGQSQKAVQPPHLFLWLMKLKNMLLAKFSFYFHEALSRQTTASEMKTLTAKANPDFFGKISSFIRKYDAANVSLIFDNRGSESFQGHGYHHPHSYREAPKGVDQYPAVVSLPSDRPVMHWPNVIMIMTDRTSDLNSLEKVVHFYDDKVQSTYFLTRPEPHFTIVIIFESKKSERDSHFISFLNEVSLALKNPKVFASLKPGAKG
Protein: Urea-proton symporter DUR3 (OsDUR3) (High-affinity urea active transporter DUR3) (Q7XBS0)
Organism: Oryza sativa subsp. japonica (Rice)
Function: High-affinity urea-proton symporter involved in the active transport of urea across the plasma membrane into root cells. May play an important role in urea uptake by plant cells at low external urea concentrations.
Subcellular location: Cell membrane {ECO:0000269|PubMed:22010949}; Multi-pass membrane protein {ECO:0000269|PubMed:22010949}.
Interaction partners:
- Proline dehydrogenase
- Os01g0314700 protein
- adenine phosphoribosyltransferase
- adenine phosphoribosyltransferase
- adenine phosphoribosyltransferase
- adenine phosphoribosyltransferase
- adenine phosphoribosyltransferase
Sequence:
MASGVCPPAELGFGAEYYSVVNGVCSRAGSYFGGRPVLTQAVGYAVVLGFGAFFALFTSFLVWLEKRYVGSQHTSEWFNTAGRSVKTGLIASVIVSQWTWAATILQSSNVAWQYGVSGPFWYASGATIQVLLFGVMAIEIKRKAPNAHTVCEIVRARWGTPAHLVFLTFCLLTNVIVTAMLLLGGSAVVNALTGVNVYAASFLIPLGVVVYTLAGGLKATFLASYIHSVVVHAVLVVFVFLVYTSSSKLGSPRVVYDRLMAVASAARDCSADLSRNGQACGPVAGNFKGSYLTMLSSGGLVFGIINIVGNFGTVFVDNGYWMSAIAARPSSTHKGYLLGGLVWFAVPFSLATSLGLGALALDLPLTAAEAAKGLVPPATATALMGKSGSVLLLTMLFMAVTSAGSAELVAVSSLCTYDIYRTYLNPGASGKQILRVSRAVVLGFGCFMGVLAVVLNVAGVSLGWMYLAMGVIVGSAVIPIALLLLWSKANAVGAMGGAVSGCALGVAVWLTVAKVQYGRVNLDTTGRNAPMLAGNLVSILVGGAVHAACSLLRPQHYDWGTSREMITTVESVHAALDDELKEERLVHAKRWIVRWGLVFTAVIVVAWPALSLPARRYSLGYFTLWAAVAIAWGTVGSVVIILLPVAESWTTITKVCAGMFTNDAVYDRLDDVNLRLRAIMGAMPEAEKRYRQLHETEMHPAGTHPANDDDDDNNNNQMMHS
Protein: Salivary cystatin-L2 (Sialostatin-L2) (B7PKZ1)
Organism: Ixodes scapularis (Black-legged tick) (Deer tick)
Function: Inhibitor of cysteine proteinases. Inhibits host immune responses, probably via its inhibition of host cathepsins. Contributes to the suppression of the host's immune response to tick salivary proteins and is important for successful feeding on hosts. Down-regulates TLR2-mediated host responses to infection by B.burgdorferi and the production of chemokines CCL3 and CXCL10 by host dendritic cells. Enhances infection by the tick-transmitted pathogen B.burgdorferi (in vitro). Inhibits host inflammatory responses to A.phagocytophilum infection. Inhibits papain (in vitro). Inhibits cathepsin-L (CTSL) (in vitro). Inhibits cathepsin-L2 (CTSV) (in vitro).
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MTSSLALVLVFGGAAVCAELALRGGYRERSNQDDPEYLELAHYATSTWSAQQPGKTHFDTVVEVLKVETQTVAGTNYRLTLKVAESTCELTSTYNKDTCQANANAAQRTCTTVIYRNLQGEKSISSFECAAA