wanglab/gogpt-training-data huggingface dataset:
Protein: MAGE-like protein 2 (Protein nS7) (Q9QZ04)
Organism: Mus musculus (Mouse)
Function: Probably enhances ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases, possibly through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex. Acts as a regulator of retrograde transport via its interaction with VPS35. Recruited to retromer-containing endosomes and promotes the formation of 'Lys-63'-linked polyubiquitin chains at 'Lys-220' of WASHC1 together with TRIM27, leading to promote endosomal F-actin assembly (By similarity). Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-BMAL1 heterodimer. Significantly promotes the cytoplasmic accumulation of CLOCK.
Subcellular location: Early endosome. Cytoplasm {ECO:0000269|PubMed:22208286}. Nucleus {ECO:0000269|PubMed:22208286}. Note=Recruited to retromer-containing endosomes via interaction with VPS35. Colocalizes with CLOCK and BMAL1 in the cytoplasm, and with PER2 in the cytoplasm and nucleus. {ECO:0000250|UniProtKB:Q9UJ55, ECO:0000269|PubMed:22208286}.
Interaction partners:
- Zinc finger protein RFP
- Ubiquitin carboxyl-terminal hydrolase 7
- Vacuolar protein sorting-associated protein 35
- Sorting nexin-8
- Vacuolar protein sorting-associated protein 26A
- Vacuolar protein sorting-associated protein 29
- Small nuclear ribonucleoprotein-associated protein N
- Sorting nexin-27
- Sorting nexin-3
- Sorting nexin-1
Sequence:
MSQLSTNLGDSSPPESPVPAVHSRPTVLMRAPPASSRAPPVPWDPPPVDLQAPMAAWQAPQPAWEAPEGQLPAPVAQLAQPPGLGAPMVQAPPLGGGMAKPPTPGVLMVHQPPPGAPMAQSSTPGVLMLHPSVTGAPLAHPPPPGTPMTHPPGTSMAHPPPPPPPPPPPPPPGTPMTHPPPPGTPMGHHPPPGNPMTHPPPGNPMVHPLTHGAPMVHGGPHGTPMPHVPITGTPIAQQPTPGVLMAQQLTPGVLMVQPPAPGAPMVQPPPQAALMTQPAPSITPMAKPPGPGVVMIHPPGARGPIIQTPVSGAPMAQTVLPPGQPLATWAPQGQPLILQIQSQVIRAPPQVPSVPQAPQVQLATPPGWQATTPNWQVTPQGWPATPLTWQATQVTWQAPTIAWQATQPGRQGHSTIRTGHTPIRPGPAPLLRQIPPMIRQIQPVMRQAPPLIRQVPIRPAPHGIASQPQLWQVLPPPPPLRQAPQARLLLPRVPGTGQVSTVPPVAQIHLVPQSGPQVPQTVLPAQLSIPIPVPQAAAQSAPRTVHCPPIIWQAPKGQAPVPQELPVPQELPVPQELPVPQEVPVPQEIPVPQEIPVPQELPVPQELPVPQELPVPQELPVPQELPVPQELPVPQELPVPQELPVPLEFQEVQQAQAVGWRAPKVPPHFWQPVSAQEAQEQATQIAHVEQQQPFQGAPASSKALQTQLPTHQAQASGLQAELPSVQLQPSWQGPLPMLQAQPGASATLANFPRGSTRSRMAPSGEPGPSSLEPRGPPRERRAPARDKKGPPKERMFIGATFCAPRGASASRAYVPTAWKNLPATSETFPATSRVFPSTSHFQPASSNAFRGPSAASESPKSLPFALQDPYACVEALPAVPWVPYPDGNASSACKSVPAILMVAAAAPQASATAAEASKSSEPPRRPGKATRKKKHLEPKEDNCGHRLSSRDWRGPRTWGNPSHSDWEIQRAMQLLGDRESLYTPQGLNDWGCPNTSRMPRSLEGPSTSRDQEFCGDSGGSQTWMASEVPSVSRGSSAAQEDPDRESQPLSPLDERANALVQFLLVKDQAKVPVQLSEMVNVVIREYKDDSLDIINRANTKLECTFGCQLKEVDTKTHTYIIVNKMAYPQCNLLASYLERPKFSLLMVVLSLIFMKGYCIRENLLFSFLFQLGLDVQETSGLFRITKKLITSVFVRHRYLEYRQIPFTEPAEYELLWGPRAFLETNRVHILRFLAALYENQPQIWSCQYLDSLAELEYKDANAAAEESHDSDDDAHDPTSSPHPH
Protein: NAD(P)H-quinone oxidoreductase subunit 1, chloroplastic (EC 7.1.1.-) (NAD(P)H dehydrogenase subunit 1) (NDH subunit 1) (NADH-plastoquinone oxidoreductase subunit 1) (Q37165)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01350}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01350}.
Interaction partners:
- NAD
- NAD
- NAD
- NAD
- NAD
- NAD
- NAD
- NAD
- NAD
- NAD
Sequence:
MIIYATAVQTINSFVKLESLKEVYGLIWIFVPIFSLVLGIITGVLVIVWLEREISAGIQQRIGPEYAGPLGILQALADGTKLLFKENLRPSRGNTPLFSIGPSIAVISILLSYSVIPFSNHLVLADLNIGIFLWIAISSIAPIGLLMSGYGSNNKYSFLGGLRAAAQSISYEIPLTLCVLSISLLSNSLSTVDIVEAQSKYGFWGWNLWRQPIGFIIFLISSLAECERLPFDLPEAEEELIAGYQTEYSGIKFGLFYVASYLNLLISSLFVTVLYLGGWNISIPYISILELFQRDQIFGTTIGIFITLAKTYLFLFVSIATRWTLPRLRMDQLLNLGWKFLLPISLGNLLLTTSFQLFSL
Protein: Mothers against decapentaplegic homolog 1 (MAD homolog 1) (Mothers against DPP homolog 1) (JV4-1) (Mad-related protein 1) (SMAD family member 1) (SMAD 1) (Smad1) (hSMAD1) (Transforming growth factor-beta-signaling protein 1) (BSP-1) (Q15797)
Organism: Homo sapiens (Human)
Function: Transcriptional modulator activated by BMP (bone morphogenetic proteins) type 1 receptor kinase. SMAD1 is a receptor-regulated SMAD (R-SMAD). SMAD1/OAZ1/PSMB4 complex mediates the degradation of the CREBBP/EP300 repressor SNIP1. May act synergistically with SMAD4 and YY1 in bone morphogenetic protein (BMP)-mediated cardiac-specific gene expression.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15647271, ECO:0000269|PubMed:9335504}. Nucleus {ECO:0000269|PubMed:15647271, ECO:0000269|PubMed:22781750, ECO:0000269|PubMed:9335504}. Note=Cytoplasmic in the absence of ligand. Migrates to the nucleus when complexed with SMAD4 (PubMed:15647271). Co-localizes with LEMD3 at the nucleus inner membrane (PubMed:15647271). Exported from the nucleus to the cytoplasm when dephosphorylated (By similarity). {ECO:0000250|UniProtKB:P70340, ECO:0000269|PubMed:15647271}.
Interaction partners:
- E3 ubiquitin-protein ligase SMURF1
- Mothers against decapentaplegic homolog 4
- Mothers against decapentaplegic homolog 6
- Inner nuclear membrane protein Man1
- Mothers against decapentaplegic homolog 2
- Activin receptor type-1
- Bone morphogenetic protein receptor type-1A
- Mitogen-activated protein kinase 1
- Transcriptional coactivator YAP1
- Mothers against decapentaplegic homolog 3
Sequence:
MNVTSLFSFTSPAVKRLLGWKQGDEEEKWAEKAVDALVKKLKKKKGAMEELEKALSCPGQPSNCVTIPRSLDGRLQVSHRKGLPHVIYCRVWRWPDLQSHHELKPLECCEFPFGSKQKEVCINPYHYKRVESPVLPPVLVPRHSEYNPQHSLLAQFRNLGQNEPHMPLNATFPDSFQQPNSHPFPHSPNSSYPNSPGSSSSTYPHSPTSSDPGSPFQMPADTPPPAYLPPEDPMTQDGSQPMDTNMMAPPLPSEINRGDVQAVAYEEPKHWCSIVYYELNNRVGEAFHASSTSVLVDGFTDPSNNKNRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYAECLSDSSIFVQSRNCNYHHGFHPTTVCKIPSGCSLKIFNNQEFAQLLAQSVNHGFETVYELTKMCTIRMSFVKGWGAEYHRQDVTSTPCWIEIHLHGPLQWLDKVLTQMGSPHNPISSVS
Protein: FMR1 autosomal homolog 1 (E9PFF5)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000256|ARBA:ARBA00004331}. Postsynapse {ECO:0000256|ARBA:ARBA00034110}.
Interaction partners:
Sequence:
MAELTVEVRGSNGAFYKVYSRANDQEPCGWWLAKVRMMKGEFYVIEYAACDATYNEIVTFERLRPVNQNKTVKKNTFFKCTVDVPEDLREACANENAHKDFKKAVGACRIFYHPETTQLMILSASEATVKRVNILSDMHLRSIRTKLMLMSRNEEATKHLECTKQLAAAFHEEFVVREDLMGLAIGTHGSNIQQARKVPGVTAIELDEDTGTFRIYGESADAVKKARGFLEFVEDFIQVPRNLVGKVIGKNGKVIQEIVDKSGVVRVRIEGDNENKLPREDGMVPFVFVGTKESIGNVQVLLEYHIAYLKEVEQLRMERLQIDEQLRQIGSRSYSGRGRGRRGPNYTSGYGTNSELSNPSETESERKDELSDWSLAGEDDRDSRHQRDSRRRPGGRGRSVSGGRGRGGPRGGKSSISSVLKDPDSNPYSLLDNTESDQTADTDASESHHSTNRRRRSRRRRTDEDAVLMDGMTESDTASVNENGLGKRCD
Protein: Jun dimerization protein 2 (Q8WYK2)
Organism: Homo sapiens (Human)
Function: Component of the AP-1 transcription factor that represses transactivation mediated by the Jun family of proteins. Involved in a variety of transcriptional responses associated with AP-1 such as UV-induced apoptosis, cell differentiation, tumorigenesis and antitumogeneris. Can also function as a repressor by recruiting histone deacetylase 3/HDAC3 to the promoter region of JUN. May control transcription via direct regulation of the modification of histones and the assembly of chromatin.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Transcription factor Jun
- Transcription factor JunD
- Transcription factor JunB
- ADP-ribosylation factor-like protein 4C
- Cyclic AMP-dependent transcription factor ATF-2
- Basic leucine zipper transcriptional factor ATF-like
- CCAAT/enhancer-binding protein gamma
- Progesterone receptor
- Cyclic AMP-dependent transcription factor ATF-3
- Protein c-Fos
Sequence:
MMPGQIPDPSVTTGSLPGLGPLTGLPSSALTVEELKYADIRNLGAMIAPLHFLEVKLGKRPQPVKSELDEEEERRKRRREKNKVAAARCRNKKKERTEFLQRESERLELMNAELKTQIEELKQERQQLILMLNRHRPTCIVRTDSVKTPESEGNPLLEQLEKK
Protein: Sarcomere length short, isoform B (Sarcomere length short, isoform C) (Q9VGN4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Protein Obscurin
- Z band alternatively spliced PDZ-motif protein 66, isoform E
Sequence:
MPFVTPRAGTSSASSAPGGRTTFRPPWVKDDGGTSGTSSTTKPTATPWAKKTATTTTASPATKENGEKPTVAKPKATATTTAAARKTSTPEPAKKTIEPVKKSSLATSTTAAKKTPEPVNTKKAPEPIKKVAPTVGPKKPVATTSALKKKKEPTPPPESSSEEEESEEEEETEEETESEEEESEEESESEEEESEEEDTTVDEKVPEHVKKAAQLRPTTVNKKPEPESELTQRFTMEKPKLRSVVVKRDKSLKKMATEDDDEAEEGETEEERDRRRRFKLEKPKLRHVKREEKPLPSKSTDDLAKIRPVLKKVPKIDELLKEPKEEPKPEFTTKTLRKASIKREPSIKSVPAPPPLPSLVPKAPPPPPPPLAPGEKRVLSSTQKETLEKLRTRPRRRPDWSEMMKEVESGKKLRHVACNDRSQPILTCKSITKLDDKFIYETEKGNSHNKLLKQIQGGIKLKPTKTNDRSKPVLDGLRKFRRQMTIEEQLQKSQSKINMLSEAPSSHALGPGSATALGAGGSRPSIVSAMSIDEESPDELDDIDKIRDDLQSTKQMLALELRNREAQDRENKKLLAKIRTLETELEREKSREKNLEYGSNVIVATMDPTPTAEQTYVNSLKREVEDARKVSKEVEQNYQSTAEQLVEAKTEIEEQRRQIQLLERKLAAALQATPSTNRPHISNCFAYDDDDYDDCFHYDHYHAARHQGGGSLDGSRRPSDANFGRDSSPELEPEVSESDPDEPEEKKVERRERRSGKELKILRSKLTKLKVKEEAAKKEKDALKQAMKKNQSILKEENKKFKKLEKEVQKMAASMKLDEDDVDGEEKDEDEEEAEEEHASEEEEESDDESEESESEESEAETGSESEPEDSPNSAKKANVEPRVKKHESRFAAMKKCNVLLQANVDNLQDQIVQVRSRATNLQDELDAVIADLGF
Protein: Proteasome 26S subunit, ATPase 6 (G3V6W6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Proteasome subunit alpha type-5
- 26S proteasome regulatory subunit 4
- Proteasome
- 26S proteasome non-ATPase regulatory subunit 11
- 26S proteasome non-ATPase regulatory subunit 13
- Proteasome subunit alpha type-3
- 26S proteasome non-ATPase regulatory subunit 12
- 26S proteasome regulatory subunit 6B
- Proteasome subunit alpha type-1
- 26S proteasome non-ATPase regulatory subunit 6
Sequence:
MALPGIPYERRLLIMADPRDKALQDYRKKLLEHKEIDGRLKELREQLKELTKQYEKSENDLKALQSVGQIVGEVLKQLTEEKFIVKATNGPRYVVGCRRQLDKSKLKPGTRVALDMTTLTIMRYLPREVDPLVYNMSHEDPGNVSYSEIGGLSEQIRELREVIELPLTNPELFQRVGIIPPKGCLLYGPPGTGKTLLARAVASQLDCNFLKVVSSSIVDKYIGESARLIREMFNYARDHQPCIIFMDEIDAIGGRRFSEGTSADREIQRTLMELLNQMDGFDTLHRVKMIMATNRPDTLDPALLRPGRLDRKIHIDLPNEQARLDILKIHAGPITKHGEIDYEAIVKLSDGFNGADLRNVCTEAGMFAIRADHDFVVQEDFMKAVRKVADSKKLESKLDYKPV
Protein: Delta-guaiene synthase 2 (EC 4.2.3.87) (EC 4.2.3.93) (D0VMR7)
Organism: Aquilaria crassna (Eagle wood)
Function: Sesquiterpene synthase involved in the biosynthesis of delta-guaiene (53.7%) and alpha-guaiene (44.6%), two structures composed of five- and seven-membered rings. Produces also 1.7% of alpha-humulene.
Interaction partners:
Sequence:
MSSAKLGSASEDVSRRDANYHPTVWGDFFLTHSSNFLENNDSILEKHEELKQEVRNLLVVETSDLPSKIQLTDEIIRLGVGYHFETEIKAQLEKLHDHQLHLNFDLLTTSVWFRLLRGHGFSIPSDVFKRFKNTKGEFETEDARTLWCLYEATHLRVDGEDILEEAIQFSRKRLEALLPKLSFPLSECVRDALHIPYHRNVQRLAARQYIPQYDAEQTKIESLSLFAKIDFNMLQALHQSELREASRWWKEFDFPSKLPYARDRIAEGYYWMMGAHFEPKFSLSRKFLNRIVGITSLIDDTYDVYGTLEEVTLFTEAVERWDIEAVKDIPKYMQVIYIGMLGIFEDFKDNLINARGKDYCIDYAIEVFKEIVRSYQREAEYFHTGYVPSYDEYMENSIISGGYKMFIILMLIGRGEFELKETLDWASTIPEMVKASSLIARYIDDLQTYKAEEERGETVSAVRCYMREFGVSEEQACKKMREMIEIEWKRLNKTTLEADEISSSVVIPSLNFTRVLEVMYDKGDGYSDSQGVTKDRIAALLRHAIEI
Protein: Pre-mRNA-splicing factor SYF1 (PRP19-associated complex protein 90) (Synthetic lethal with CDC40 protein 1) (Q04048)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in pre-mRNA splicing and cell cycle control. As a component of the NTC complex (or PRP19-associated complex), associates to the spliceosome to mediate conformational rearrangement or to stabilize the structure of the spliceosome after U4 snRNA dissociation, which leads to spliceosome maturation.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Pre-mRNA-splicing factor 8
- Pre-mRNA-processing factor 17
- Pre-mRNA-splicing factor ATP-dependent RNA helicase-like protein PRP2
- Pre-mRNA-splicing factor PRP21
- Small nuclear ribonucleoprotein Sm D1
- Pre-mRNA-splicing factor CEF1
- Small nuclear ribonucleoprotein G
- Small nuclear ribonucleoprotein Sm D2
- Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP16
- Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP22
Sequence:
MSAYIAMKGVITNVDENIRNDEDVAFEYEIQKTPQNILTWKRYIEYWKEEGRTDKQIRWLYERFCSQFVTDTSIWEDYIRWESTKEVVETSRIFWLFQRCLKSCVRDCDRICLSYLELAIEQYDLAMIRHALASSLMKMEREMHRKVWDPVIKFVEEKVLPLTQLDSTQEDEEESTDEAELINVLLVKGFTKGGFISEEISENGSRGDIWSSHILERYLKVAPQQKRNESLATLALTRDNITIKSVYEKYLPQDENSGKYLPSSELPFELNFNYLASLEKLGLDNQYEEFMRQMNGIYPDKWLFLILSLAKYYISRGRLDSCGDLLKKSLQQTLRYSDFDRIYNFYLLFEQECSQFILGKLKENDSKFFNQKDWTEKLQAHMATFESLINLYDIYLNDVALRQDSNLVETWMKRVSLQKSAAEKCNVYSEAILKIDPRKVGTPGSFGRLWCSYGDLYWRSNAISTARELWTQSLKVPYPYIEDLEEIYLNWADRELDKEGVERAFSILEDALHVPTNPEILLEKYKNGHRKIPAQTVLFNSLRIWSKYIDYLEAYCPKDANSSDKIFNKTKMAYNTVIDLRLITPAMAENFALFLQNHYEVMESFQVYEKTIPLFPPEIQYELWIEYLEVATSHQLSSLSPEHIRFLFEKALKNLCSNGIDCKTIFIAYSVFEERISGLISKSIEILRRGAVIGTVSVSTHLESRLQLWRMCISKAESTLGPSVTRELYQECIQILPNSKAVEFVIKFSDFESSIGETIRAREILAYGAKLLPPSRNTELWDSFEIFELKHGDKETYKDMLKMKKVLESNMLIDSASVSHEEGNINFVAAATSHAPNSHTLTQSTSSYSINPDEIELDI
Protein: Cerberus (Q9PWB0)
Organism: Gallus gallus (Chicken)
Function: Cytokine that acts as a regulator of the activity of Nodal/BMP pathways during the establishment of bilateral asymmetry in the head and trunk of the embryo.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Protein Wnt
- Protein Wnt-11
- Protein Wnt
- Protein Wnt-3a
- Protein Wnt
- Protein Wnt
- Protein Wnt-4
- Protein Wnt-9a
- Protein Wnt-8c
- Protein Wnt
Sequence:
MSLLLLQLLVLSCLGDTEPQPDSQQRKRRPLQHLFYLDRNLLESQSFHELVGENPVGVKETQEEPSFFIAFPQTAGESQKQGEKKMSRFILPNAELYAHQDLRTWAAPKEISPVENFSPSYYSNKRDVEPPYRKDAKKFWDHFMLRKNSASEEVVLPIKTNEMHQETCRTLPFSQSVAHESCEKVIVQNNLCFGKCSSFHVPGPDDRLYTFCSKCLPTKFSMKHLDLNCTSSVPVVKKVMIVEECNCETQKIEDPLLGSRQSDFLGNLPEHN
Protein: Protein Wnt (D4A9J2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498, ECO:0000256|RuleBase:RU003500}.
Interaction partners:
- Low-density lipoprotein receptor-related protein
- LDL receptor related protein 5
- Frizzled-1
- Frizzled-2
- Frizzled-8
- Frizzled-9
- Protein-serine O-palmitoleoyltransferase porcupine
- Frizzled-4
- Frizzled class receptor 7
- Frizzled-5
Sequence:
MGLWALLPSWVSATLLLALTALPAALGANSSGRWWGIVNIASSTNLLTDSKSLQLVLEPSLQLLSRKQRRLIRQNPGILHSVSGGLQSAVRECKWQFRNRRWNCPTAPGPHLFGKIVNRGCRETAFIFAITSAGVTHSVARSCSEGSIESCTCDYRRRGPGGPDWHWGGCSDNIDFGRLFGREFVDSGEKGRDLRFLMNLHNNEAGRTTVFSEMRQECKCHGMSGSCTVRTCWMRLPTLRAVGDVLRDRFDGASRVLYGNRGNNRASRAELLRLEPEDPAHKPPSPHDLVYFEKSPNFCTYSGRLGTAGTAGRACNSSSPALDGCELLCCGRGHRTRTQRVTERCNCTFHWCCHVSCRNCTHTRVLHECL
Protein: Killer cell lectin-like receptor subfamily A member 18 (Q4Z8P6)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
Interaction partners:
Sequence:
MTEQKDTFSAVRFHKSSGLQNEMRLKETRKPRKAGLRVCSVPWQFIVIALGILISLRLVIVAVLMTNIFQYGQQKHELQEFLKHHNNCSIMQSDINLKDELLKNKSIECNLLESINRDQNRLYNKTKTVLDSLQHTGRGVKVYWFCYGMKCYYFIMDRKPWSRCKQSCQNSSLTLLKIDNEDELKFLQLVVPSDSCWIGLSYDNKKKDWAWIDNRPSKLALNTTKYNIRDGGCMFLSKTRLDNNYCDQSFICIWGKRLDKFPH
Protein: ATP binding cassette subfamily A member 1 (A0A8I5ZLK5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MACWSQLRLLLWKNLTFRRRQTCQLLLEVAWPLFIFLILISVRLSYPPYEQHECHFPNKAMPSAGTLPWVQGIICNANNPCFRYPTPGEAPGVVGNFNKSIVSRLFSDAQRILLYSQKDTSIRDMHKVLRTLQQIKHPNSNLKLQDFLVDNETFSGFLQHSLSLPRSAVDNLLQADVSLQKVFLQGYQLHLASLCNGSKLEEIIRLGDLEVSALCSLPREKLDAAERELRSNMDILKPVMTKLNSTSLLPTQHLAEATTTLLDSLGGLAQELFSTKSWSDMRQEVMFLTNVNNSGSSTQIYQAVSRIVCGHPEGGGLKIKSLNWYEDNNYKALFGGNGTEEDTDTFYDNSTTPYCNDLMKNLESSPLSRIIWKALKPLLIGKILYTPDTPATRQVMAEVNKTFQELALFHDLEGMWEELSPQIWTFMESSQEMDLVRTMLDSRGNDQFWERKLDGLDWTAQDIMAFLAKNPEDVQSPNGSVYTWREAFNETNQAIQTISRFMECVNLNKLEPIPTEVRLINKSMELLDERKFWAGIVFTGITPDSVELPHHVKYKIRMDIDNVERTNKIKDGYWDPGPRADPFEDMRYVWGGFAYLQDVVEQAIIRVLTGTEKKTGVYVQQMPYPCYVDDIFLRVMSRSMPLFMTLAWIYSVAVIIKSIVYEKEARLKETMRIMGLDNGILWFSWFISSLIPLLVSAGLLVIILKLGDLLPYSDPSVVFVFLSVFAVVTILQCFLISTLFSRTNLAAACGGIIYFTLYLPYVLCVAWQDYVGFSIKIFASLLSPVAFGFGCEYFALFEEQGIGVQWDNLFKSPVEEDGFNLTTSVSMMLFDTFIYGVMTWYIEAVFPGQYGIPRPWYFPCTKSYWFGEEIDEKSHPGSSQKGASEICMEEEPTHLKLGVSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMNSIRQNLGVCPQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLPPSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGSSLFLKNQLGTGYYLTLVKKDVESSLSSCRNSSSTVSCLKKVVPELPAAGQSGGRGGEVQRLVALTQDVSAISNLIRKHVSEARLVEDIGHELTYVLPYEAAKEGAFVELFHEIDDRLSDLGISSYGISETTLEEIFLKVAEESGVDAETSDGTLPARRNRRAFGDKQSCLHPFTEDDAVDPNDSDLDPESRETDLLSGMDGKGSYQLKGWKLTQQQFVALLWKRLLIARRSRKGFFAQIVLPAVFVCIALVFSLIVPPFGKYPNLELQPWMYNEQYTFVSNDAPEDMGTQELLNALTKDPGFGTRCMEGNPIPNTPCLVGEEDWTTGPVPQTLMDLFQNGNWTMKNPSPSCQCSSDKIKKMLPVCPPGAGGLPPPQRKQKTADILQNLTGRNISDYLVKTYVQIIAKSLKNKVWVNEFRYGGFSLGVSDSQALPPSQEVNNAIKQMKKLLKLTKDSSADRFLSSLGRFMTGLDTKNNVKVWFNNKGWHAISSFLNVINNAILRANLQKGENPSQYGITAFNHPLNLTKQQLSEVALMTTSVDVLVSICVIFAMSFVPASFVVFLIQERVSKAKHLQFICGVKPVIYWLSNFVWDMCNYVVPATLVVIIFICFQQKSYVSSTNLPVLALLLLLYGWSITPLMYPASFVFKIPSTAYVVLTSVNLFIGINGSVATFVLELFTNNKFNDINDILKSVFLIFPHFCLGRGLIDMVKNQAMADALERFGENRFVSPLSWDLVGRNLFAMAVEGVVFFLVTVLIQYRFFIRPRPVKARLPPLNDEDEDVRRERQRILEGGGQNDILEIKELTKIYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKTSTFKMLTGDTAVTRGDALLNKNSILSNIHEVHQNMGYCPQFDAITELLTGREHLEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYASNYSGGNKRKLSTAIALIGGPPVVFLDEPTTGMDPKARRFLWNCALSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNRFGDGYTIVVRIAGSNPDLKPVQEFFGLAFPGSVLKEKHRNMLQYQLPSSLSSLARIFSILSQSKKRLHIEDYSVSQTTLDQVFVNFAKDQSDDDHLKDLSLHKNQTVVDVAVLTSFLQDEKVKESYV
Protein: Probable uridine nucleosidase 2 (EC 3.2.2.3) (Inosine nucleosidase) (EC 3.2.2.2) (Nucleoside hydrolase 2) (Uridine ribohydrolase 2) (Xanthosine nucleosidase) (EC 3.2.2.-) (Q8LAC4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in pyrimidine breakdown, especially in response to dark stress. In the presence of URH1, exhibits efficient inosine and xanthosine hydrolytic activities. Support inosine breakdown especially during the late phase of senescence.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:21235647}.
Interaction partners:
- Uracil phosphoribosyltransferase, chloroplastic
- Dihydropyrimidine dehydrogenase
- Guanosine deaminase
- Dihydroorotate dehydrogenase
- Beta-ureidopropionase
- Dihydropyrimidinase
- Bifunctional D-cysteine desulfhydrase/1-aminocyclopropane-1-carboxylate deaminase, mitochondrial
Sequence:
MAIGDRKKIIIDTDPGIDDAMAIFVALNSPEVDVIGLTTIFGNVYTTLATRNALHLLEVAGRTDIPVAEGTHKTFLNDTKLRIADFVHGKDGLGNQNFPPPKGKPIEKSGPEFLVEQAKLCPGEITVVALGPLTNLALAVQLDPEFSKNVGQIVLLGGAFAVNGNVNPASEANIFGDPEAADIVFTCGADIIAVGINVTHQVIMTADDKDKLASSKGKLAQYLCKILDVYYDYHLTAYEIKGVYLHDPATILAAFLPSLFTYTEGVARVQTSGITRGLTLLYNNLKRFEEANEWSDKPTVKVAVTVDAPAVVKLIMDRLMES
Protein: Lysine--tRNA ligase, cytoplasmic (EC 6.1.1.6) (Lysyl-tRNA synthetase) (LysRS) (P15180)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasm.
Interaction partners:
- Isoleucine--tRNA ligase, cytoplasmic
- Leucine--tRNA ligase, cytoplasmic
- Glutamine--tRNA ligase
- Leucine--tRNA ligase, mitochondrial
- Arginine--tRNA ligase, cytoplasmic
- Arginine--tRNA ligase, mitochondrial
- Isoleucine--tRNA ligase, mitochondrial
- Putative proline--tRNA ligase YHR020W
- Methionine--tRNA ligase, cytoplasmic
- Glutamate--tRNA ligase, cytoplasmic
Sequence:
MSQQDNVKAAAEGVANLHLDEATGEMVSKSELKKRIKQRQVEAKKAAKKAAAQPKPASKKKTDLFADLDPSQYFETRSRQIQELRKTHEPNPYPHKFHVSISNPEFLAKYAHLKKGETLPEEKVSIAGRIHAKRESGSKLKFYVLHGDGVEVQLMSQLQDYCDPDSYEKDHDLLKRGDIVGVEGYVGRTQPKKGGEGEVSVFVSRVQLLTPCLHMLPADHFGFKDQETRYRKRYLDLIMNKDARNRFITRSEIIRYIRRFLDQRKFIEVETPMMNVIAGGATAKPFITHHNDLDMDMYMRIAPELFLKQLVVGGLDRVYEIGRQFRNEGIDMTHNPEFTTCEFYQAYADVYDLMDMTELMFSEMVKEITGSYIIKYHPDPADPAKELELNFSRPWKRINMIEELEKVFNVKFPSGDQLHTAETGEFLKKILVDNKLECPPPLTNARMLDKLVGELEDTCINPTFIFGHPQMMSPLAKYSRDQPGLCERFEVFVATKEICNAYTELNDPFDQRARFEEQARQKDQGDDEAQLVDETFCNALEYGLPPTGGWGCGIDRLAMFLTDSNTIREVLLFPTLKPDVLREEVKKEEEN
Protein: Ankyrin 2, isoform M (Q7KU95)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MVTENGAQGDGNTSFLRAARAGNLERVLEHLKNNIDINTSNANGLNALHLASKDGHIHVVSELLRRGAIVDSATKKGNTALHIASLAGQEEVVKLLLEHNASVNVQSQNGFTPLYMAAQENHDAVVRLLLSNGANQSLATEDGFTPLAVAMQQGHDKVVAVLLESDTRGKVRLPALHIAAKKDDVKAATLLLDNDHNPDVTSKSGFTPLHIASHYGNQNIANLLIQKGADVNYSAKHNISPLHVAAKWGKTNMVSLLLEKGGNIEAKTRDGLTPLHCAARSGHEQVVDMLLERGAPISAKTKNGLAPLHMAAQGEHVDAARILLYHRAPVDEVTVDYLTALHVAAHCGHVRVAKLLLDRNADANARALNGFTPLHIACKKNRLKVVELLLRHGASISATTESGLTPLHVAAFMGCMNIVIYLLQHDASPDVPTVRGETPLHLAARANQTDIIRILLRNGAQVDARAREQQTPLHIASRLGNVDIVMLLLQHGAQVDATTKDMYTALHIAAKEGQDEVAAVLIENGAALDAATKKGFTPLHLTAKYGHIKVAQLLLQKEADVDAQGKNGVTPLHVACHYNNQQVALLLLEKGASPHATAKNGHTPLHIAARKNQMDIATTLLEYGALANAESKAGFTPLHLSSQEGHAEISNLLIEHKAAVNHPAKNGLTPMHLCAQEDNVNVAEILEKNGANIDMATKAGYTPLHVASHFGQANMVRFLLQNGANVDAATSIGYTPLHQTAQQGHCHIVNLLLEHKANANAQTVNGQTPLHIARKLGYISVLDSLKTITKEDETAAAPSQAEEKYRVVAPEAMHESFMSDSEEEGGEDNMLSDQPYRYLTVDEMKSLGDDSLPIDVTRDERMDSNRMTQSAEYASGVPPTIGEEVISPHKTQVYGSSPKATVDGVYIANGSGHDEPPHVGRKLSWKSFLVSFLVDARGGAMRGCRHSGVRMIIPSRSTCQPTRVTCRYVKPQRTMHPPQLMEGEALASRVLELGPCSTKFIGPVVMEVPHFASLRGKEREIIILRSDNGETWREHTIDNSEEIIHDVLQQCFEPEEIAQLEEQAGNHVCRFVTYDFPQYFAVVSRIRQEVHAIGPEGGMVSSTVVPQVQAVFPQGALTKKIKVGLQAQPVDPDLTAKLLGRGVAVSPIVTVEPRRRKFHKAITLSMPAPKAHSQGMINQYSGNTPTLRLLCSITGGPSRAQWEDVTGSTPLTFVNDCVSFTTTVSARFWLMDCRNISDATKMATELYKEVIHVPFIAKFVVFAKKVEPFEAKLRVFCMTDDREDKTLEKHELYTEVAKSRDVEVLEGKPQYIEMAGNLVPVTKSGDQLQVQFKAFRENRLPFTVRVKDQHADIVGRTLFMKEPKVAKGEPPQQPICILNIVLPEAVIPDSTTAFSDRVTSAYRTSMFSLSKHQNDHYIGDIRIVDLSNLLGKDWIQLAPEIGINGEEIDEIINQNTDSIARQAQSMIRLYKDKPNYDILSLETALKNIGRDDIMKKCKSGRLSHSREFDEADLMKNSESVEELVRRESKRIQQINEREEVKYSAEEKEVEESESDEEAAKRTVAERREKIVKRLSIERSIPASTQKKEITREITEIKRKSLIEDKKAHHESEILMQLPADNVIIKTTTVPDQVIKMKMGKMDSTEVSKSEFDKELTHKFKTSGRSSEEEDQPSYPDQTDKIVQDISAAEKKEKDGVTFSRVTTITRQEARDITEDFLEIEKRSQLPATSTTATVHEKFVEEIKEKTSPLASVPQETVKEVQQVISEVTEIASKKVENIISSFESSKSVDATTVLPTQPSVESTKVSETIKNLEDAKAVSAEQVKTVHVVESSSIEETIAEFEAKKVKYDFHGGEPKTQIPKFTRKPSDDSMKPTAAPRATVESETESVLETKAEKPISKIPVKTIPTEAQKVSEVDARKITQDFLQGEKLAAEPKPSPAASKIPKVEPRKSVDKQVDRESKILDDVVASTATIMTAGLGDEQLKDQLVDHSEIIAKSETVAEKVTELLDTFHKIEEKVTKSEKTSEISSKVEELVKIEEKPLSQVQPKEDKVAEKVAEVIETFHKIEEKITTADARELTRDFLSMEQQNQLPSMPQAAEKPLESSLTSTSASEPESIVTVKPSPPASKIPVVEPRKIVFDESTKPLIEPEPVKTTEKKPLNERQLTADFLSMEQQTQLVSEPAKSLVEEVMKSAEQMVEQPKQQKSLNERQLTEDFLLMEQQTQLPSDIVKPTDKLIDGIESAAPVGDEASPFHTPKLTTSVVTQEPQQLASEYDSDTFGKQATIPLGDSKIDQGLIAPVSMEPRKSLTDAEFCKSVGETITKKMSVGVIEISDELKKIESEIPHSQTPPPTPSDNKTDKQNEEPELISLERDYLADTVTTLHTTTESTLERVSAITKIGKCKS
Protein: Uridine phosphorylase (EC 2.4.2.3) (Q499V1)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Thymidine phosphorylase
- Cytidine deaminase
- Uridine-cytidine kinase
- Uridine-cytidine kinase
- Purine nucleoside phosphorylase
- Uracil phosphoribosyltransferase homolog.
- Uridine monophosphate synthetase, isoform CRA_a.
- 5'-nucleotidase
- Thymidine kinase, cytosolic
- 5',3'-nucleotidase, mitochondrial
Sequence:
MAATGTEAKDLENHHNSDCLVQLSNPNIATMKEDVLYHFNLSTSTHDFPAMFGDVKFVCVGGSSSRMSAFIKYVAAELGLDHPGKEYPNICAGTDRYAMYKAGPVLSVSHGMGIPSIGIMLHELIKMLYHARCSNITIIRIGTSGGIGLEPGSVVITQQAVDECFKPEFEQIVLGKRVTRNTSLDAQLVQELMQCSSDLNEFPTVVGNTMCTLDFYEGQGRLDGALCSYTEKDKQAYLRAAHAAGVRNIEMESSVFATMCSACGLKAAVVCVTLLDRLQGDQINTPHNVLVEYQQRPQRLVGHFIKKRLGRA
Protein: Sporulation-specific protein 19 (Q03029)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in sporulation. Essential for completion of the nuclear division.
Subcellular location: Secreted, cell wall {ECO:0000305|PubMed:10383953}. Membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
Interaction partners:
Sequence:
MKKQILIVAAQSILCSTVFGERSNVGLSTEELGGDSILYFNEDPIVIEIDKKAIDKKTLEQLASTRDVVLTDLPDTLEFIDFNEYAKMKSKSDMLLEYINEYEFDDFERSSEGGLEEEEEEDLIYDFNAQAEDLGKLGSNIYEVVEEKNIVNTYDGNLINASTTESTTTIRPFVTSHSYVASSTPYSNISSLNEDYDNASNFLTPTTVALAVLLTILLFIQAY