wanglab/gogpt-training-data huggingface dataset:
Protein: Brakeless-B (Scribbler long isoform) (Scribbler, isoform D) (Scribbler, isoform H) (Q9N693)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MEKKLAKVALNSSNVATESNIKNNKLLANLSAAGAATATTATTGTATTTTATTANQALNFNNKTKATANATAASANNRHNNNNNSSAIKKHTNTKQLAGKSPACNSSSSSLSSSSSSNSSESKDTNFEYEDEWNIGGIPELLDDLDADIEKSAHSSGGGNQATALNAKQANSSSTSSSSSSKGGASSSSSSAAATGSSSSHKSHKTTLHSNLSATSPTTIKFTRQPVAIGGANSSSSSSAAAAPSGGSANVVAKGSSSSSSSTSSSSSGKHHHHHHHHSNSSSSGSSSKGYKSALVAQLNSPSPLNSNSKSLSGSGSGSGNTNGAAGAGAGSTLSSSTFAGFSKGGSLVSSSAGAAAALAAGSGQQGSKFSAGGMSSQTGSGSGGNNTSNSNNSSSGSGGSGSGSSTGNTASGSGNNNSTSAGGPPSSQGGNNGNGSGSSSSSSSGKSSAKMSIDHQATLDKGLKMKIKRTKPGTKSSEAKHEIVKATDQQQNGALGAGSNNSANEDGSSGSSSTNASSLGSTNSSSSASSGSSSSSGSSSSSSKKHLNNASSGSGSSSSGGGSQNNASGHASGGGSSGSSQSTPQGTKRGSSGHRREKTKDKNAHSNRMSVDKSAAAASAAGEKDTPEKCSGTGAGGSPCSCNGDVGAPCSHHACIRRAAHMSNSAGNANSSAGTGQSGGSSSMSAVPPGVFTPSAGSPSTGSPSTVVPAAASLLAATGAASSSASQMASSSAGGVGGSGGGANAPGPPGKESAGSIKISSHIAAQLAAAAASNSYSGSGANTNQGQNSNAGGNGGSESKAAAAAQAKLMAPGMISATMHHTISVPAGTGTGDDDTKSPPAKRVKHEAGASGAGGGKEMVDICIGTSVGTITEPDCLGPCEPGTSVTLEGIVWHETEGGVLVVNVTWRGKTYVGTLLDCTRHDWAPPRFCDSPTEELDSRTPKGRGKRGRSAGLTPDLSNFTETRSSIYFSHAQVHSKLRNGATKGRGATRSASGNAAANSNSSSSGNGGGATPSTSPTAFLPPRPEKRKSKDEAPSPLNGDASDGASVGGIGGAGGVNMVNASGIPISASGGGLATQPQSLLNPVTGLNVQISTKKCKTASPCAISPVLLECPEQDCSKKYKHANGLRYHQSHAHGAGGGASSMDEDSMQAPEDPATPPSPGVASGTGSGASVASSAVPATAPSAGQGTVAVSPNTPLANSSNPVTNGNVAPSAPATGSVTIAAPNTTPSVVETQAPLTGPPPVTPPAPTPICAVATPGAEQSVSSVLPLGNLPLTAGPNSATQQQQPPTQQQQPQLLVPGGSAASLQQQQQQQQPVAGGSITAGISGQALSQHQQQLMGGLPAMLSDQQQQALLQQGALKAGVLRFGPPDGNPLQQQPGQASVNPQTQQSPPRPPSHVQDQQTPSAYAQQAGLKTSPGFGSVGVGAASSKQKKNRKSPGPSDFEGRVSREDVQSPAYSDISDDSTPVAEQEMLDKSVGQAVTAKHIELMGKKPTEVGVGVPPPPAPNMYVPGMYQFYPAQQQSAPPPQQQQQQPQYMVQTEPGKPPGLPPALTQAQQQQQLQPGAPPPTSQPPSHLLGPPGQQSVAAHLADYSGKNKDPPLDLMTKPQPQPGQPPSQQQQSGQLSGQENNGKDVGPPTSQPGSQPPPVNLSAVAGPPPGSLPPGLGGLSALGAAGLGGPGPGKGMPHFYPFNFIPPAYPYNVDPNFGSVSIVASEEAAKLSGHPGLPPSSQAQQLSGISIKEERLKESPSPHDQPKHMPSQQQMIASKLIKQEPMTKQEIKQEPNSNPGQQHPPPQQQPAPQPQQQQPPPPQPQQPHALHPKDLQALGAYPAIYQRHSINLAVQQAREEELRRYYMFTGRQNSAAAAAAAAAQNAASGGLPPHPGMMHKDEPGMGSAAQQQQQQQQQQMQIAQQQQQAIQQHHQHLQQQHQAQQQQQQQQHQQQQQQQQQQQQQQQQQQQQQKLKQSQAASAGANNKATNLTKDSPKQKGGDDDQPLKVKQEGQKPTMETQGPPPPPTSQYFLHPSYISPTPFGFDPNHPMYRNVLMSAAGPYNTAPYHLPIPRPYHAPEDLSRNTGTKALDALHHAASQYYTTHKIHELSERALKSPTSGSGPVKVSVSSPSIGPPQPGGPTSSGPGSGPVSGVLGPGSGSNQQPGSAPGSAGGVPLNLQPPPGGMGPSPGSKPDLSGPKGHGGVTPGSSLDGHKQSMPGGPPPNGPSGNGAVGGVGGAAGNGAAGGGGAGAADSRSPPPQRHVHTHHHTHVGLGYPMYPAPYGAAVLASQQAAAVAVINPFPPGPSK
Protein: Multisubstrate pseudouridine synthase 7 (EC 5.4.99.-) (EC 5.4.99.27) (RNA pseudouridylate synthase 7) (RNA-uridine isomerase 7) (O74343)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes pseudouridylation at position 35 in U2 snRNA stem-loop II region which induces particular conformation of the mRNA-U2 snRNA duplex and places the nucleophile in an accessible position for the first step of splicing. Also catalyzes pseudouridylation at position 56 in U2 snRNA. Catalyzes also pseudouridylation at position 50 in 5S rRNA, position 13 in cytoplasmic tRNAs, and position 35 in pre-tRNA(Tyr). Pseudouridine residues in tRNAs may stabilize the local RNA conformation, favor interactions with protein partners and play an important role in the stabilization of the codon-anticodon interaction with mRNA. Also catalyzes pseudouridylation of mRNAs in response to heat shock: mediates pseudouridylation of mRNAs with the consensus sequence 5'-UGUAR-3'.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q08647}. Cytoplasm {ECO:0000250|UniProtKB:Q08647}.
Interaction partners:
- Pseudouridylate synthase C18B11.02c
- tRNA pseudouridine synthase 4
- Putative tRNA pseudouridine synthase C16C4.06c
- Putative tRNA pseudouridine synthase C25B8.05
- tRNA
- rRNA methyltransferase 1, mitochondrial
- Large ribosomal subunit protein uL15m
- Large ribosomal subunit protein uL13m
- Mitochondrial GTPase 1
- Large ribosomal subunit protein bL17m
Sequence:
MSQENHVDVPRKRIRIDQSESSRNLERNGLEDEANAPSDLSGQKFYMTESDVGIDAFLNPNLPSIDGIIKARFTDFAVFEVDTDGNIVHLTDMEAHDPILSKATGDKETEDAKDSSNQDISNDQKAPSFKEQEPATLPILPNDLQSIIPKGIGNEFIQSLHKLSVGEITDPISLILPENTPPMDKGQRTILHQFIRNNFSGLESSTKGNGTFTVSKTTRKNQPRSRRDPRLSWKALGGEYCHFHLYKENRDSMDCLGKIARLLKVPTRTLSIAGTKDRRGVTCQRVAIHHVRASRLAQLNSGSLKNSTYGFLLGNYSYKNSNLRLGDLKGNEFHIVVRNVITPKEKVVEALNSLKEHGFINYFGLQRFGTSSVGTHTIGVRLLQSDWKGAVDLILSPRPEHTGSVKEAIDLWHSTHDAEASLRILPRRMIAESSILETWSRSGNQTDYLGAFQRIPRHLRSIYPHAYQSYVWNRVASWRIKNLGDRPVVGDLVYSTESNGLSQKSPIVDPEAPDLLEDLPVSSKLSARPIEEDEVNNFSIYDIVLPLPGRNVIYPKNETFDIYKSVMNEASLDPLNMSRKDRELSLPGDYRKLLVRPENMEFNFIKYDNMEQQLILTDKDRLENRSISVSSEVGKHTAVTLKFVLPSSAYATMALREALRTATASGDQRMLMPAVLKDSI
Protein: Enoyl-CoA delta isomerase 1 (H3BS70)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKFKNPPVNSLSLEFLTELVISLEKLENDKSFRGVILTSDRPGVFSAGLDLTEMCGRSPAHYAGYWKAVQELWLRLYQSNLVLVSAINGACPAGGCLVALTCDYRILADNPRYCIGLNETQLGIIAPFWLKDTLENTIGHRAAERALQLGLLFPPAEALQVGIVDQVVPEEQVQSTALSAIAQWMAIPDHARQLTKAMMRKATASRLVTQRDADVQNFVSFISK
Protein: Peptidyl-prolyl cis-trans isomerase (PPIase) (EC 5.2.1.8) (Cyclophilin) (CPH) (Cyclosporin A-binding protein) (PPI-II) (Rotamase) (P14832)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in histone deacetylase complexes, suggesting a function in chromatin. Imports fructose-1,6-bisphosphatase (FBPase) into the intermediate vacuole import and degradation (Vid) vesicles. Regulates the meiotic gene program via the Set3C histone deacetylase complex to promote efficient sporulation, and the prolyl-isomerase activity is required for this function.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15643056}. Nucleus {ECO:0000269|PubMed:15643056}. Mitochondrion intermembrane space {ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:22984289}.
Interaction partners:
- Probable DNA-binding protein SNT1
- Protein HOS4
- SIR4-interacting protein SIF2
- Probable histone deacetylase HOS2
- SET domain-containing protein 3
- FK506-binding protein 1
- Ran-specific GTPase-activating protein 1
- Peptidyl-prolyl cis-trans isomerase FPR2
- Peptidyl-prolyl cis-trans isomerase ESS1
- NAD-dependent protein deacetylase HST1
Sequence:
MSQVYFDVEADGQPIGRVVFKLYNDIVPKTAENFRALCTGEKGFGYAGSPFHRVIPDFMLQGGDFTAGNGTGGKSIYGGKFPDENFKKHHDRPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGEVVDGYDIVKKVESLGSPSGATKARIVVAKSGEL
Protein: Zinc finger protein 57 (Zfp-57) (Q8C6P8)
Organism: Mus musculus (Mouse)
Function: Transcription regulator required to maintain maternal and paternal gene imprinting, a process by which gene expression is restricted in a parent of origin-specific manner by epigenetic modification of genomic DNA and chromatin, including DNA methylation. Acts by controlling DNA methylation during the earliest multicellular stages of development at multiple imprinting control regions (ICRs). Acts together with ZNF445, but ZFP57 plays the predominant role in imprinting maintenance. In contrast, in humans, ZNF445 seems to be the major factor early embryonic imprinting maintenance. Required for the establishment of maternal methylation imprints at SNRPN locus. Acts as a transcriptional repressor in Schwann cells. Binds to a 5'-TGCCGC-3' consensus sequence and recognizes the methylated CpG within this element.
Subcellular location: Nucleus {ECO:0000269|PubMed:15070898, ECO:0000269|PubMed:18854139, ECO:0000269|PubMed:8120052}. Note=Binds various differentially methylated regions (DMR), including the Snrpn DMR.
Interaction partners:
- Transcription intermediary factor 1-beta
- DNA
- Histone-lysine N-methyltransferase SETDB1
- Developmental pluripotency-associated protein 3
- Small nuclear ribonucleoprotein-associated protein N
- DNA
Sequence:
MAARKQSSQPSRTPVSYEDVAVSFTQEEWEYLTSTQKTLYQKVMSETFKNLTFVGSKKKPQEPSSDLQDKNEEQEKSSSCTGVFKGGPFFFCLTCGKCFKKNTFLFNHQFPVRSRRLAVTNPQSRKGKGYKAQHRGERPFFCNFCGKTYRDASGLSRHRRAHLGYRPRSCPECGKCFRDQSEVNRHLKVHQNKPAASNQAGNQASNQRLKSRVPPTTPRSQAPALKYVKVIQGPVARAKARNSGASTLNVRSNSITVVRSREKISCPYCHITFTMRTCLLTHLKIHFRRQPNQHFCCKESAHSSNTLRMQKIYTCPVCDSSFRGKESLLDHLCCQRPIRFSKCWEILGHLLGYLHEPVVLGNIFKVRDSSGKRMESRRRRRKRACTENPETEGLSGKGRVAPWEMEGATSPESPVTEEDSD
Protein: serine C-palmitoyltransferase (EC 2.3.1.50) (Q9V3F2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Serine palmitoyltransferase 1
- ORM1-like protein
- 3-dehydrosphinganine reductase
- Sphingolipid delta
- LD18904p
- Ceramide kinase, isoform A
- ceramide glucosyltransferase
- Sphingosine-1-phosphate lyase
- sphingosine kinase
- Neutral ceramidase
Sequence:
MGNFDGDSGTVFEQSYATTNGNGKVPNGNGAADLSAPEKQELLRKFSAPAYTEIRTRRCQPKPANDAQSPSSINYHPEKKSIPNGHASILDQESKPNQAEGKLSPELEHFQKTSFEEVPLHTACLTYLGFYLLMILGYINQLLFVPKVATEKGRDGYVALYDAFESFYSRYVYRRIKDCWNRPICSVPGDELTLKDRVTDDYGWSFKFTGTETRCLNLGSYNYLGFAAATGQCADDSEESARSSGLAYCSSRCELGDNEQLQELEALTARYFGVEDAIVFGMGFATNALNLPSLLGPNSLVISDEKNHASIILGLRLSGATTKVFKHNNMRDLERVLRQGVCYGNPKKGGQPWDKVMILVEGIFSMEGSIVRLPEVIALKKKYKAYLYLDEAHSVGAMGSRGRGVTDYFNVDPKEVDILMGTFTKSFGSAGGYLAGSKKLIDFLRTNSHAHCYAASISPPIAQQILTSMKTIMGEDGTDIGRKKIHQLARNTRYFRRRLAQLGVITYGHEDSPVVPMLVYLFSKIGAVVRTLTTRHIAAVGAGFPATPIMEGRIRFCLSAAHTKEQLDFALEAIDEIADDLGLKYSRKPRDPNPVIY
Protein: Serrate RNA effector molecule homolog (Arsenite-resistance protein 2 homolog) (Q9V9K7)
Organism: Drosophila melanogaster (Fruit fly)
Function: Acts as a mediator between the cap-binding complex (CBC) and RNA-mediated gene silencing (RNAi). Involved in innate immunity via the short interfering RNAs (siRNAs) processing machinery by restricting the viral RNA production. Also involved microRNA (miRNA)-mediated silencing by contributing to the stability and delivery of primary miRNA transcripts to the primary miRNA processing complex containing drosha and pasha.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Nuclear cap-binding protein subunit 2
- Nuclear cap-binding protein subunit 1
- Phosphorylated adapter RNA export protein
- RNA helicase
- Nuclear cap-binding protein subunit 1
- LD24793p
- ATP-dependent RNA helicase WM6
- RNA helicase
- Pre-mRNA-splicing factor CWC22 homolog
- Microfibrillar-associated protein 1
Sequence:
MGDSDDEYDRKRRDKFRGERESYRTERRDDRRPVGGSAGARDEWAERNPFRGGASAGGGGARHRPDYSDYRGPGARPRYGSPVRDLPPAKRMRPDWGDGDVRANPRFGGYDPYLMQAWNDHYQSMHSAYSHGGHAPPVRESIGGGGGDTLTQPAMLNLKQFLDTQDENISDSEVMRKYTEYKTDFKRQQLNEFFVAHKDEEWFKNKYHPEDSVKRSEEQRGFLQRRTDVFMELLENGTIGSVKVDSSQADALIRVLDTCVIKLEGGTDEDLKVLDEKPKDPVVYERKAEQMQSVKEVEKTINSPKEEMSEADPVSTQRKPVRPVNSDGENWDDDDAENSAPKKELAEDSKDSDSKPEDKQLNKKKTKKRKRNSSDDDSSSSESSSSSDEEKLKEKYDVEDGLRAEQKTEAEKDRQEATKAKQGPQSPKLDEDEGNENTEPKGLDSKINTYEEIDNTLKSPEISSNPIKNTDNGDGSKVEEDGEKPSVGKDKVVETETIDLDKVKDGQPRALHRTSSIFLRNLAPSITRSEIEAVCNRFSGYLRVAIADPLVERRWYRRGWITFMRDVNIKEICWGLNNQRLRDCEMGAIVNRDLSRRVRPANGITAHKQVVRSDIKLCAKIALNLDEKFRLWAEGPKDDSNSARANESSENGSGSTYGFNSQNPVLQNITDYLIEEASAEEEELLGLTGENKDTEGEPIERDEQLISVLDRLVLYLRIVHSVDYYNHCEYPYEDEMPNRCGIIHARGPPPVRVTNNDVQEYIKIYESKLQQFLTKTVPLSDEEIKNLGAKDAETEVEKFVQANTQELAKDKWLCPLSGKKFKGPEFIRKHIFNKHEEKVDEVRKEVQYFNNYLRDPKRPQLPEHPGTSKRPESESARGGGGGYRPPMYPPFSAMPYGFGPPMMGGGRGGRNFPPARRELPLEHQRRLIGYHDLDAPANSDMFD
Protein: Nicotinic acetylcholine receptor alpha6, isoform H (M9PFD8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00034104}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00034104}.
Interaction partners:
Sequence:
MDSPLPASLSLFVLLIFLAIIKESCQGPHEKRLLNHLLSTYNTLERPVANESEPLEVKFGLTLQQIIDVDEKNQILTTNAWLNLEWNDYNLRWNETEYGGVKDLRITPNKLWKPDVLMYNSADEGFDGTYHTNIVVKHNGSCLYVPPGIFKSTCKIDITWFPFDDQHCEMKFGSWTYDGNQLDLVLNSEDGGDLSDFITNGEWYLLAMPGKKNTIVYACCPEPYVDITFTIQIRRRTLYYFFNLIVPCVLISSMALLGFTLPPDSGEKLTLGVTILLSLTVFLNLVAESMPTTSDAVPLIGTYFNCIMFMVASSVVLTVVVLNYHHRTADIHEMPPWIKSVFLQWLPWILRMGRPGRKITRKTILLSNRMKELELKERSSKSLLANVLDIDDDFRHTISGSQTAIGSSASFGRPTTVEEHHTAIGCNHKDLHLILKELQFITARMRKADDEAELIGDWKFAAMVVDRFCLIVFTLFTIIATVTVLLSAPHIIVQ
Protein: Homeobox protein ESX1 (Extraembryonic, spermatogenesis, homeobox 1) [Cleaved into: Homeobox protein ESX1-N; Homeobox protein ESX1-C] (Q8N693)
Organism: Homo sapiens (Human)
Function: May coordinately regulate cell cycle progression and transcription during spermatogenesis. Inhibits degradation of polyubiquitinated cyclin A and cyclin B1 and thereby arrests the cell cycle at early M phase. ESXR1-N acts as a transcriptional repressor. Binds to the sequence 5'-TAATGTTATTA-3' which is present within the first intron of the KRAS gene and inhibits its expression. ESXR1-C has the ability to inhibit cyclin turnover.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15235584}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:15235584}. Note=ESXR1-N localizes specifically to the nucleus while ESXR1-C localizes specifically to the cytoplasm.
Interaction partners:
- Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit beta
- LIM/homeobox protein Lhx4
- LIM/homeobox protein Lhx3
- Pituitary-specific positive transcription factor 1
- ETS-related transcription factor Elf-3
- Transcription factor SOX-3
Sequence:
MESLRGYTHSDIGYRSLAVGEDIEEVNDEKLTVTSLMARGGEDEENTRSKPEYGTEAENNVGTEGSVPSDDQDREGGGGHEPEQQQEEPPLTKPEQQQEEPPLLELKQEQEEPPQTTVEGPQPAEGPQTAEGPQPPERKRRRRTAFTQFQLQELENFFDESQYPDVVARERLAARLNLTEDRVQVWFQNRRAKWKRNQRVLMLRNTATADLAHPLDMFLGGAYYAAPALDPALCVHLVPQLPRPPVLPVPPMPPRPPMVPMPPRPPIAPMPPMAPVPPGSRMAPVPPGPRMAPVPPWPPMAPVPPWPPMAPVPTGPPMAPVPPGPPMARVPPGPPMARVPPGPPMAPLPPGPPMAPLPPGPPMAPLPPGPPMAPLPPRSHVPHTGLAPVHITWAPVINSYYACPFF
Protein: DNA-directed RNA polymerase II subunit 4 (15.9 kDa subunit of RNA polymerase II) (DNA-directed RNA polymerase II subunit D) (O48890)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Second largest component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- DNA-directed RNA polymerases II and V subunit 8A
- DNA-directed RNA polymerases II and V subunit 6B
- DNA-directed RNA polymerases II, IV and V subunit 6A
- DNA-directed RNA polymerases II, IV and V subunit 10
- DNA-directed RNA polymerases II, IV and V subunit 9B
- DNA-directed RNA polymerases II, IV and V subunit 8B
- DNA-directed RNA polymerases II, IV and V subunit 11
- Pentatricopeptide repeat-containing protein At4g30825
- DNA-directed RNA polymerases II, IV and V subunit 3
- DNA-directed RNA polymerase II subunit RPB1
Sequence:
MSGEEEENAAELKIGDEFLKAKCLMNCEVSLILEHKFEQLQQISEDPMNQVSQVFEKSLQYVKRFSRYKNPDAVRQVREILSRHQLTEFELCVLGNLCPETVEEAVAMVPSLKTKGRAHDDEAIEKMLNDLSLVKRFE
Protein: NADP-dependent oxidoreductase domain-containing protein (Q20127)
Organism: Caenorhabditis elegans
Interaction partners:
- Nsp1_C domain-containing protein
- Nuclear pore complex protein 15
- Nuclear pore complex protein 5
- AMP-binding domain-containing protein
- Protein SEC13 homolog
- Intraflagellar transport protein 46 homolog
- Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein
- Alanine--glyoxylate aminotransferase
- beta-ketoacyl-[acyl-carrier-protein] synthase I
- Papilin
Sequence:
MQSHTFTRSRGVPIYMNGSVSHQRLYDRLSEPSTSRQLPRSISLAPTGHHRTGSTRIDREQVDTSLPVTYIPRFHDESAVRRMNYRQIPGTDIRMSKIGFGAAAIGGMFGNVEDSIIKIVETAIKQGINYIDTGYWYSQSRSESILGKALSKIPRKAYYISTKVGRFELDYARTFDFRADKILESLTNSLKRLQLTYIDICYVQIHDADFAPNESIVLYETLQALEMAKSSGKIRHIGLTGYPLGKLVQLVDCSATKIDFVMTYCKGTLNNNALGQFTAWFQTRNIAVINSGALCWGLLTEKGPPPWHPASDEIKEACLAATTYCSSKNISISKLALDYALNFPNVICCLVGMDSVQQVLDNLELSNFSRITDVEQRVRDRIMRRYLDRLENAGWEGVDVAQYWKKLKKLGLTALATHRHSSVESLASTLNGFSLYSSNSSSELRTPRRRRPF
Protein: TGF-beta activated kinase 1/MAP3K7 binding protein 1 (D4A6C6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MEQQPSWTDDLPLCHFSGVGSASNRSYSADGKGTESHPPEDNWLKFRSENNCFLYGVFNGYDGNRVTNFVAQRLSAELLLGQLNTEHTDADVRRVLLQAFDVVERSFLESIDDALAEKASLQSQLPEGVPQHQLLPQYQKILERLKALEKEISGGAMAVVAVLLNNKLYVANVGTNRALLCRSTVDGLQVTQLNVDHTAENEDELFRLSQLGLDAGKIKQVGVICGQESTRRIGDYKVKYGYTDIDLLSTAKSKPIIAEPEIHGAQPLDGVTGFLVLMSEGLYKALEAAHGPGQANQEVAAMIDTEFAKQTSLDAVAQAVVDRVKRIHSDTFASGGERAKFCPRHEDMTLLVRNFGYPLGEMSQPTPTPAPGGRVYPVSVPYSSAQSTSKTSVTLSLVMPSQGQMVNGSHSASTLDEATPTLTNQSPTLTLQSTNTHTQSSSSSSDGGLFRSRPAHSLPPGEDGRVEPYVDFAEFYRLWSVDHGEQSVMTAP
Protein: WbcK protein (Q56914)
Organism: Yersinia enterocolitica
Interaction partners:
Sequence:
MDNKKLLSLIIPVFNAEQYLDACLSSVFVQWDNTLEIIVINDGSTDNSANIIQKYSEKYDFVYISQENTGISVVRNMGLSVSTGEYITFLDADDIWCNEIYSSIKKIVLENSPDGMVFNYSEVLDDKEHVFELIKVNKFTVDRLEHVKLKIAESEMFYVWRCVFKKNIFSGMVFDVGRRFEDQLLLPILIDKCKSIFECKDLIVKYRQISSSITKNLNISDLDDSEFGLIRFRDKYAEYKNKYWAVVLASVFMSHISKCARIYHFNKIRALDSFNKSYAIVSMKPILHSGKLKPILYYIVKYKLFYRLVSAVEKEVRK
Protein: Allantoate amidohydrolase (AAH) (EC 3.5.3.9) (Allantoate deiminase) (P77425)
Organism: Escherichia coli (strain K12)
Function: Involved in the anaerobic nitrogen utilization via the assimilation of allantoin. Catalyzes specifically the hydrolysis of allantoate to yield CO2, NH3 and S-ureidoglycine, which is unstable and readily undergoes a second deamination by S-ureidoglycine aminohydrolase AllE to yield S-ureidoglycolate and NH3. In vivo, the spontaneous release of S-ureidoglycolate and ammonia from S-ureidoglycine appears to be too slow to sustain an efficient flux of nitrogen.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- (S)-ureidoglycine aminohydrolase (UGHY) (UGlyAH)
- Allantoinase
- Ureidoglycolate dehydrogenase
- Diaminopropionate ammonia-lyase
- Ureidoglycolate lyase
- Oxamate carbamoyltransferase subunit AllF
- Putative allantoin permease
- Oxamate carbamoyltransferase subunit AllG
- NAD-dependent dihydropyrimidine dehydrogenase subunit PreA
Sequence:
MITHFRQAIEETLPWLSSFGADPAGGMTRLLYSPEWLETQQQFKKRMAASGLETRFDEVGNLYGRLNGTEYPQEVVLSGSHIDTVVNGGNLDGQFGALAAWLAIDWLKTQYGAPLRTVEVVAMAEEEGSRFPYVFWGSKNIFGLANPDDVRNICDAKGNSFVDAMKACGFTLPNAPLTPRQDIKAFVELHIEQGCVLESNGQSIGVVNAIVGQRRYTVTLNGESNHAGTTPMGYRRDTVYAFSRICHQSVEKAKRMGDPLVLTFGKVEPRPNTVNVVPGKTTFTIDCRHTDAAVLRDFTQQLENDMRAICDEMDIGIDIDLWMDEEPVPMNKELVATLTELCEREKLNYRVMHSGAGHDAQIFAPRVPTCMIFIPSINGISHNPAERTNITDLAEGVKTLALMLYQLAWQK
Protein: Protein shisa-6 (Cystine-knot AMPAR modulating protein of 52 kDa) (CKAMP52) (Shisa family member 6) (Q3UH99)
Organism: Mus musculus (Mouse)
Function: Involved in maintenance of high-frequency synaptic transmission at hippocampal CA3-CA1 synapses. Regulates AMPA-type glutamate receptor (AMPAR) immobilization at postsynaptic density keeping the channels in an activated state in the presence of glutamate and preventing synaptic depression. May play a role in self-renewal and differentiation of spermatogonial stem cells by inhibiting canonical Wnt signaling pathway.
Subcellular location: Postsynaptic density membrane {ECO:0000269|PubMed:26931375}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Disks large homolog 4
- Voltage-dependent calcium channel gamma-3 subunit
- Glutamate receptor 2
- Voltage-dependent calcium channel gamma-2 subunit
- Glutamate receptor 1
- Glutamate receptor 3
- Noelin
- Disks large homolog 3
- von Willebrand factor C domain-containing protein 2-like
- Glutamate receptor 4
Sequence:
MALRRLLLPPLLLSLLLSLASLHLPPGADAARGRSGNRTLNAGAVGGRRAGGALARGGRELNSTARASGVPEAGSRRGQSAAAAAAAAAAASATVTYETCWGYYDVSGQYDKEFECNNSESGYLYCCGTCYYRFCCKKRHEKLDQRQCTNYQSPVWVQTPSTKVVSPGPENKYDPEKDKTNFTVYITCGVIAFVIVAGVFAKVSYDKAHRPPREMNIHRALADILRQQGPIPIAHCERETISAIDTSPKENTPVRSTSKNHYTPVRTAKQTPGDRQYNHPILSSATQTPTHEKPRMNNILTSATEPYDLSFSRSYQNLAHLPPSYESAVKTNPSKYSSLKRLTDKEADEYYMRRRHLPDLAARGTLPLNVIQMSQQKPLPRERPRRPIRAMSQDRVLSPRRGLPDEFGMPYDRILSDEQLLSTERLHSQDPLLSPERTAFPEQSLSRAISHTDVFVSTPVLDRYRMTKMHSHPSASNNSYATLGQSQTAAKRHAFASRRHNTVEQLHYIPGHHTCYTASKTEVTV
Protein: FI12701p (Myosuppressin receptor 1, isoform A) (Q9W025)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MASGNNETEPLYCGSGMDNFHTSYKNMHGYVSLVVCILGTIANTLNIIVLTRREMRSPTNAILTGLAVADLAVMLEYIPYTIHDYILTDSLPREEKLSYSWACFIKFHSIFAQVLHTISIWLTVTLAVWRYIAVGYPQKNRVWCGMRTTIITITTAYVVCVLVVSPSLYLITAITEYVDQLDMNGKVINSIPMTQYVIDYRNELLSARTAALNATPTSAPLNETVWLNASTLLTSTTTAAPPTPSPVVRNVTVYRLYHSDLALHNASLQNATFLIYSVVIKLIPCIALTILSVRLILALLEAKRRRKKLTSKPATPGASNGTKSPANGKAADRPRKNSKTLEKEKQTDRTTRMLLAVLLLFLITEFPQGIMGLLNAVLGDVFYLQCYLRLSDLMDILALINSSINFILYCSMSKQFRTTFTLLFRPKFLDKWLPVAQDEMAAARAERSAVAPVLEKGRQQPQVVMASTTTNITQVTNL
Protein: Peroxidase 22 (Atperox P22) (EC 1.11.1.7) (ATPEa) (Basic peroxidase E) (P24102)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Subcellular location: Secreted {ECO:0000305}. Vacuole {ECO:0000305}. Note=Carboxy-terminal extension appears to target the protein to vacuoles.
Interaction partners:
- Heavy metal-associated isoprenylated plant protein 4
- Dirigent protein 14
- Beta-glucosidase 32
- NAC domain containing protein 38
- Protein indeterminate-domain 6
- Dirigent protein 13
Sequence:
MGFSPSFSCSAIGALILGCLLLQASNSNAQLRPDFYFGTCPFVFDIIGNIIVDELQTDPRIAASLLRLHFHDCFVRGCDASILLDNSTSFRTEKDAAPNANSARGFNVIDRMKVALERACPGRVSCADILTIASQISVLLSGGPWWPVPLGRRDSVEAFFALANTALPSPFFNLTQLKTAFADVGLNRTSDLVALSGGHTFGRAQCQFVTPRLYNFNGTNSPDPSLNPTYLVELRRLCPQNGNGTVLVNFDVVTPDAFDSQYYTNLRNGKGLIQSDQELFSTPGADTIPLVNQYSSDMSVFFRAFIDAMIRMGNLRPLTGTQGEIRQNCRVVNPRIRVVENDDGVVSSI
Protein: cAMP-regulated phosphoprotein 19 (ARPP-19) (P56211)
Organism: Homo sapiens (Human)
Function: Protein phosphatase inhibitor that specifically inhibits protein phosphatase 2A (PP2A) during mitosis. When phosphorylated at Ser-62 during mitosis, specifically interacts with PPP2R2D (PR55-delta) and inhibits its activity, leading to inactivation of PP2A, an essential condition to keep cyclin-B1-CDK1 activity high during M phase. May indirectly enhance GAP-43 expression.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Serine/threonine-protein kinase greatwall
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B delta isoform
- Misshapen-like kinase 1
- cAMP-regulated phosphoprotein 21
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
- Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform
- Protein phosphatase 1 regulatory subunit 1B
- Cyclin-dependent kinase 1
Sequence:
MSAEVPEAASAEEQKEMEDKVTSPEKAEEAKLKARYPHLGQKPGGSDFLRKRLQKGQKYFDSGDYNMAKAKMKNKQLPTAAPDKTEVTGDHIPTPQDLPQRKPSLVASKLAG
Protein: 60S acidic ribosomal protein P2, putative (Q38BQ9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- 60S acidic ribosomal protein P2, putative
- 60S acidic ribosomal protein, putative
- 60S acidic ribosomal protein P0
- GST N-terminal domain-containing protein
- 40S ribosomal protein S15a, putative
- 60S ribosomal protein L5, putative
- 60S ribosomal protein L29
- 60S ribosomal protein L7a
- 60S ribosomal protein L27a
- 60S ribosomal subunit protein L31, putative
Sequence:
MAQSINPADTLACTYASLMLSDAGLPITAESINSACKAAGLEVRDTLPILFARFLEKKPIESLLAAAAAVAPQEGALPAAPAAAAAGGAAPAAADDKKKEEEEDDDDMGFGLFD