wanglab/gogpt-training-data huggingface dataset:
Protein: Actin-binding LIM protein 3 (abLIM-3) (Actin-binding LIM protein family member 3) (Q69ZX8)
Organism: Mus musculus (Mouse)
Function: May act as scaffold protein. May stimulate ABRA activity and ABRA-dependent SRF transcriptional activity.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Actin-binding LIM protein 1
- Cell division control protein 42 homolog
- Ras-related C3 botulinum toxin substrate 2
- Ras-related C3 botulinum toxin substrate 3
- Actin-binding Rho-activating protein
Sequence:
MNTSIPYQQSPYSPRGGSNVIQCYRCGDTCKGEVVRVHNNHFHIRCFTCQVCGCGLAQSGFFFKNQEYICTQDYQQLYGTRCDSCRDFITGEVISALGRTYHPKCFVCSLCRKPFPIGDKVTFSGKECVCQTCSQSMTSSKPIKIRGPSHCAGCKEEIKHGQSLLALDKQWHVSCFKCQTCSVILTGEYISKDGVPYCESDYHSQFGIKCETCDRYISGRVLEAGGKHYHPTCARCVRCHQMFTEGEEMYLTGSEVWHPICKQAARAEKKLKHRRTSETSISPPGSSIGSPNRVICAKVDNEILNYKDLAALPKVKSIYEVQRPDLISYEPHSRYTSDEMLERCGYGESLGTLSPYSQDIYENLDLRQRRASSPGYIDSPTYSRQGMSPTFSRSPHYYRSGPESGRSSPYHSQLDVRSSTPTSYQAPKHFHIPAGESNIYRKPPIYKRHGDLSTATKSKTSEDISQASKYSPAYSPDPYYASESEYWTYHGSPKVPRARRFSSGGEEEDFDRSMHKLQSGIGRLILKEEMKARSSSYADPWTPPRSSTSSREALHTTGYEMSFNGSPRSHYLADSDPLISKSASLPAYRRNGLHRTPSADLFHYDSMNAVNWGMREYKIYPYELLLVTTRGRNRLPKDVDRTRLERHLSQEEFYQVFGMTISEFERLALWKRNELKKQARLF
Protein: Uncharacterized protein UNK4.09 (O14074)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
Sequence:
MQMNSLNDPKHLVKAVVRGEIKCLDVRAQSKYEISHLRKSVNIPSEKISKCWYQLPAKQEELFVVEDQGDKIETEETGTCAQQLKKRGWNIAGHFMFSHKIWEDLSLPQNELLESGPNRNLLFEPCPYLKEVMPVVEKGIKTNNARVLDIGCGSGRDLAWICFRESGKHWMVSALDAEKRAIQRFSELFSGLGLEDRIEGKKVAKVDASGLWKLYTRDGKQEPNATAISLADMLADFQNVPEGDVYKYDLVLQIRFLNRALLRQSSSLLRNNGFLFLCTFVNDGVHQYEHPRGSDHRFEKGEAAAIVSESDGRIRVLKDEIGFIEDGRPVQILLAQKVE
Protein: 3',5'-cyclic-AMP phosphodiesterase 4C (EC 3.1.4.53) (DPDE1) (cAMP-specific phosphodiesterase 4C) (P14644)
Organism: Rattus norvegicus (Rat)
Function: Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes.
Subcellular location: Cell projection, cilium {ECO:0000250|UniProtKB:Q3UEI1}.
Interaction partners:
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit beta
- Adenosine kinase
- Adenine phosphoribosyltransferase
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
- GTP:AMP phosphotransferase AK3, mitochondrial
- Deoxycytidine kinase
- Adenylosuccinate lyase
- Adenylate cyclase type 5
Sequence:
NSSRTSSAASDLHGEDMIVTPFAQVLASLRTVRSNVAALAHGAGSATRQALLGTPPQSSQQAAPAEESGLQLAQETLEELDWCLEQLETLQTRRSVGEMASNKFKRMLNRELTHLSETSRSGNQVSEYISQTFLDQQAEVELPAPPTEDHPWPMAQITGLRKSCHTSLPTAAIPRFGVQTDQEEQLAKELEDTNKWGLDVFKVAELSGNRPLTAVIFRVLQERDLLKTFQIPADTLLRYLLTLEGHYHSNVAYHNSIHAADVVQSAHVLLGTPALEAVFTDLEVLAAIFACAIHDVDHPGVSNQFLINTNSELALMYNDSSVLENHHLAVGFKLLQGENCDIFQNLSTKQKLSLRRMVIDMVLATDMSKHMSLLADLKTMVETKKVTSLGVLLLDNYSDRIQVLQSLVHCADLSNPAKPLPLYRQWTERIMAEFFQQGDRERESGLDISPMCDKHTASVEKSQVGFIDYIAHPLWETWADLVHPDAQELLDTLEDNREWYQSRVPCSPPHAIGPDRFKFELTLEETEEEEEEDERH
Protein: Serine repeat antigen 4 (EC 3.4.22.-) (O96164)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Uncharacterized protein
Sequence:
MKIHIFLIATIYVLFSEKLIKWTTASTTQGGDTDTHPGTPPGEGSDVSQGAGQDASQGAGQDANPDPTLPKPPSPPADDTKDTGSQGDADSSSSKIEIPPLVKPENHKTIVSAMLKNYKGVKVTGTCGADFGLFLVPHIYVHVKSEDTEIELSSELAPPEMQTKFDKTQLKKFCVKDDTKKFDFIAYIYKDILVFKWKVYEEGLSKEQDVDEMKYLLPNLKQPITSIQVHSWTGTKESYILESKDYVLGEGMPEKCDAIATDCFLSGFTDIGKCFQCKLLMQEKNINDSCFKYVSSNQKELIKKQLKITAQDDEESSEYHLSESIKNLLKNIYKKNNDDNKKKELLHFENVNSALKSELLNYCNLLKEVNMNGVLKDHQLGNVQDVFNNLTKLLEEHKEENDNVLYHKMKNEALCLKNVNDWMKNKTGLLLPQLSYDLTYKNNNFTEFTQNKSYTSQNIVDKLYCNHEYCNRLKDHNNCISKINVEDQKNCALSWAFASKYHLETIKCMKGYEPLNASVLYVTNCLKNKNKDVCTEGSNPLVFLETIEEKGFLPTESNYPYDQSKVGDICPQLQNDWDNVFENTKVLDYNNGPFSVGTKGYIAYESEAFQKDMHSFVKLVKDEIMNKGSVIAYVKAENVLGYELNGKKVQNLCGDKTPDHVVNIVGYGNYINNKGEKKSYWIVRNSWGKYWGDDGYFKVDMYGPSTCEDNFIHTVVVFNVQVPINEKFDKKEHDIYNYYLKTSPEFYHNLYYKTFNSNKEEKSMNKNSYVYGQDTTPVENEAPRSGVQKPTELSSTESQTVSPPNESQTESLLSGGSQVTNPTLTQSTSSSSGQQETGPLSTQGLSPATGDPKGKEQEASPAEGLSGVLNPTKEVTSEEKIQIIHLLKHIKNSKIRRGLVKYNHEFEVGDNSCSRSTSKNAEMHDECVNICEKYWPECRGTAVPGYCLSTHDDKNECDFCYV
Protein: Calsenilin (A-type potassium channel modulatory protein 3) (DRE-antagonist modulator) (DREAM) (Kv channel-interacting protein 3) (KChIP3) (Q9JM47)
Organism: Rattus norvegicus (Rat)
Function: Calcium-dependent transcriptional repressor that binds to the DRE element of genes including PDYN and FOS. Affinity for DNA is reduced upon binding to calcium and enhanced by binding to magnesium. Seems to be involved in nociception (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12006572}. Cell membrane {ECO:0000269|PubMed:12006572, ECO:0000269|PubMed:16123112}; Lipid-anchor {ECO:0000269|PubMed:12006572}. Endoplasmic reticulum {ECO:0000269|PubMed:12006572}. Golgi apparatus {ECO:0000269|PubMed:12006572}. Nucleus {ECO:0000250|UniProtKB:Q9Y2W7}. Note=Also membrane-bound, associated with the plasma membrane. In the presence of PSEN2 associated with the endoplasmic reticulum and Golgi. The sumoylated form is present only in the nucleus. {ECO:0000250|UniProtKB:Q9Y2W7}.
Interaction partners:
- A-type voltage-gated potassium channel KCND3
- Potassium voltage-gated channel subfamily A member 4
- Voltage-gated potassium channel KCNC1
- A-type voltage-gated potassium channel KCND1
- Inactive dipeptidyl peptidase 10
- A-type potassium channel modulatory protein DPP6
Sequence:
MQRTKEAMKASDGSLLGDPGRIPLSKREGIKWQRPRFTRQALMRCCLIKWILSSAAPQGSDSSDSELELSTVRHQPEGLDQLQAQTKFTKKELQSLYRGFKNECPTGLVDEDTFKLIYSQFFPQGDATTYAHFLFNAFDADGNGAIHFEDFVVGLSILLRGTVHEKLKWAFNLYDINKDGYITKEEMLAIMKSIYDMMGRHTYPILREDAPLEHVERFFQKMDRNQDGVVTIDEFLETCQKDENIMSSMQLFENVI
Protein: Uncharacterized protein YoaJ (C1P603)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane {ECO:0000305|PubMed:19121005, ECO:0000305|PubMed:21778229}; Single-pass membrane protein {ECO:0000269|PubMed:19121005, ECO:0000269|PubMed:21778229}. Note=Some protein is also seen in the soluble fraction of the cell extracts.
Interaction partners:
- Uncharacterized membrane protein YoaK
- Uncharacterized membrane protein YkgR
- Uncharacterized protein YqfG
- Diguanylate cyclase DgcP
- Uncharacterized protein YthA
Sequence:
MKKTTIIMMGVAIIVVLGTELGWW
Protein: F1F0 ATP synthase subunit i (A0A1D8PG50)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- ATP synthase subunit delta, mitochondrial
- ATP synthase subunit d
- ATP synthase subunit a
- F1F0 ATP synthase subunit h
- ATP synthase subunit 4
- F1F0 ATP synthase subunit f
- ATP synthase subunit alpha
- ATP synthase subunit beta
- ATP synthase subunit 9, mitochondrial
- F1F0 ATP synthase subunit k
Sequence:
MGSLPRYPFPVLKTYWPYAIGAGITYYLVYKGSIASANSDEFINDPRNPRFAKGGKYIDLDKRD
Protein: Putative glycosyl transferase (Q9RN61)
Organism: Streptomyces nogalater
Interaction partners:
Sequence:
MRVPGSCRTGGIMRALFITSPGLSHILPTVPLAQALRALGHEVRYATGGDIRAVAEAGLCAVDVSPGVNYAKLFVPDDTDVTDPMHSEGLGEGFFAEMFARVSAVAVDGALRTARSWRPDLVVHTPTQGAGPLTAAALQLPCVELPLGPADSEPGLGALIRRAMSKDYERHGVTGEPTGSVRLTTTPPSVEALLPEDRRSPGAWPMRYVPYNGGAVLPDWLPPAAGRRRIAVTLGSIDALSGGIAKLAPLFSEVADVDAEFVLTLGGGDLALLGELPANVRVVEWIPLGALLETCDAIIHHGGSGTLLTALAAGVPQCVIPHGSYQDTNRDVLTGLGIGFDAEAGSLGAEQCRRLLDDAGLREAALRVRQEMSEMPPPAETAAKLVALAG
Protein: Carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase (A0A8I5Y665)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MVPPLTCMVPPLTLPAACAVAVVLQLTTLRAPACRSRLLSSAPRSEPRGPTPARGVCLVPVGLAAPPASRCSPCLSSDPMAALVLEDGSVLQGRPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPSDEEDEFGLSKWFESSEIHVAGLVVGECCPTPSHWSATCTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKLVQKGTEPSALPFVDPNARPLAPEVSIKTPRVFNAGGAPRIFAVDCGLKYNQIRCLCQLGAEVTVVPWNHELDSRKYDGLFLSNGPGDPASYPGVVSTLNRVLSEPNPRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGTGRCFLTSQNHGFAVDADSLPAGWAPLFTNANDCSNEGIVHDNLPFFSVQFHPEHRAGPSDMELLFDVFLETVRDTVAGNAEGRTVRERLAQRLCPPELPIPGSGLPPPRKVLILGSGGLSIGQAGEFDYSGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLPITPHYVTQVIRNERPDGILLTFGGQTALNCGVELTKAGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASTKEELSALVAPAFAHTSQVLIDKSLKGWKEIEYEVVRDAYGNCVTVCNMENLDPLGIHTGESIVVAPSQTLNDREYQLLRRTAIKVTQHLGIVGECNVQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLPELRNSVTGGTAAFEPSLDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKALRMVDENCVGFDHTVKPVSDVELETPTDKRIFVVAAALWAGYSVERLYELTRIDCWFLHRMKRIVTHAKLLEQHRGRPLPQDLLHQAKCLGFSDKQIALAVLSTELVVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTYWGNTHDLDFRTPHVLVLGSGVYRIGSSVEFDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGGQLPNNMAMALHRQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVAYTDGDLERFLSSAAAVSKEHPVVISKFIQEAKEIDVDAVACDGIVSAIAISEHVENAGVHSGDATLVTPPQDITPKTLERIKAIVHAVGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRIIMGEKVESVGLMTGSGVVGVKVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPKKNILLTIGSYKNKSELLPTVRLLESLGYSLYASLGTADFYTEHGVKVTAVDWHFEEAVDGECPPQRSILDQLAENHFELVINLSMRGAGGRRLSSFVTKGYRTRRLAADFSVPLIIDIKCTKLFVEALGQIGPAPPLKVHVDCMTSQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGVTMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFTLFLGASSENAGTLGAVAGSAAGLKLYLNETFSELRLDSVAQWMEHFETWPSHLPIVAHAERQSVAAVLMVAQLTRRSVHICHVARKEEILLIKTAKAQGLPVTCEVAPHHLFLNREDLERLGPGKGEVRPELGSREDMEALWENMAVIDCFASDHAPHTLEEKCGPKPPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPLQEDTYVEVDLEHEWTVPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYIDGQVLVPPGYGQDVRKWPQGAVPQPPPPTPTTTEITTTPERPRRVIPGLPDGRFHLPPRIHRASDPGLPAEEPKEKPPRKVAESELIGTPDGPCYPVPPVPRQASPQNLGSSGLLHPQMSPLLHSLVGQHILSVKQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATSSVQKGESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGDLKHGRTVHSLACLLTQYRVSLRYVAPPSLRMPSSVWDFVASRGTKQEEFESIEEALPDTDVLYMTRIQKERFGSSQEYEACFGQFILTPHIMTRAKKKMVVMHPMPRVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLGRF
Protein: CCN family member 2 (Cellular communication network factor 2) (Connective tissue growth factor) (Q98TQ8)
Organism: Gallus gallus (Chicken)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
Sequence:
MSPASLAVALLLALLGPEVRGQECSGQCQCGSGPGPSCPAGVSLVLDGCGCCRVCAKQLGELCTERDPCDHHKGLFCDFGSPANRRIGVCTARDGAPCVFSGMVYRSGESFQSSCKYQCTCLDGAVGCVPLCSMDVRLPSPDCPYPRRVKLPGKCCEEWVCDEAKEQTAVGPALAAYRLEDTYGPDPTMMRANCLVQTTEWSACSKTCGMGISTRVTNDNAFCRLEKQSRLCMVRPCEADLEENIKKGKKCIRTPKISKPIKFELSGCTSVKTYRAKFCGVCTDGRCCTPHRTATLPVEFKCPDGEIMKRKMMFIKTCACHYNCPGDNDIFESLYYRKMYGDMA
Protein: 1-acyl-sn-glycerol-3-phosphate acyltransferase 2 (EC 2.3.1.51) (Lysophosphatidyl acyltransferase 2) (Q8LG50)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating acyl moiety at the 2 position. Has preference for C-18-CoA substrates compared to C-16-CoA substrates. Required for female but not male gametophyte development.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15772283}; Multi-pass membrane protein {ECO:0000269|PubMed:15772283}.
Interaction partners:
- 1-acyl-sn-glycerol-3-phosphate acyltransferase LPAT1, chloroplastic
- Lysophospholipid acyltransferase 2
- Lysophospholipid acyltransferase 1
- Glycerol-3-phosphate acyltransferase 9
- Probable 1-acyl-sn-glycerol-3-phosphate acyltransferase 5
- Triacylglycerol lipase SDP1L
- Triacylglycerol lipase SDP1
- Phosphatidate phosphatase PAH2
- Phosphatidate phosphatase PAH1
- Glycerol-3-phosphate acyltransferase, chloroplastic
Sequence:
MVIAAAVIVPLGLLFFISGLAVNLFQAVCYVLIRPLSKNTYRKINRVVAETLWLELVWIVDWWAGVKIQVFADNETFNRMGKEHALVVCNHRSDIDWLVGWILAQRSGCLGSALAVMKKSSKFLPVIGWSMWFSEYLFLERNWAKDESTLKSGLQRLSDFPRPFWLALFVEGTRFTEAKLKAAQEYAASSELPIPRNVLIPRTKGFVSAVSNMRSFVPAIYDMTVTIPKTSPPPTMLRLFKGQPSVVHVHIKCHSMKDLPESDDAIAQWCRDQFVAKDALLDKHIAADTFPGQQEQNIGRPIKSLAVVLSWACVLTLGAIKFLHWAQLFSSWKGITISALGLGIITLCMQILIRSSQSERSTPAKVVPAKPKDNHHPESSSQTETEKEK
Protein: V-type proton ATPase 16 kDa proteolipid subunit c (V-ATPase 16 kDa proteolipid subunit c) (Vacuolar proton pump 16 kDa proteolipid subunit c) (P27449)
Organism: Homo sapiens (Human)
Function: Proton-conducting pore forming subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity).
Subcellular location: Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250|UniProtKB:P63081}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:P63081}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- V-type proton ATPase subunit E 1
- V-type proton ATPase subunit S1
- V-type proton ATPase 116 kDa subunit a 4
- V-type proton ATPase 116 kDa subunit a 1
- V-type proton ATPase subunit F
- V-type proton ATPase subunit B, brain isoform
- V-type proton ATPase subunit H
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit d 2
- V-type proton ATPase subunit C 1
Sequence:
MSESKSGPEYASFFAVMGASAAMVFSALGAAYGTAKSGTGIAAMSVMRPEQIMKSIIPVVMAGIIAIYGLVVAVLIANSLNDDISLYKSFLQLGAGLSVGLSGLAAGFAIGIVGDAGVRGTAQQPRLFVGMILILIFAEVLGLYGLIVALILSTK
Protein: Beta-glucosidase B (EC 3.2.1.21) (Beta-D-glucoside glucohydrolase B) (Cellobiase B) (Gentiobiase B) (Q5BFG8)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose.
Interaction partners:
- Probable glucan endo-1,3-beta-glucosidase eglC
- Glycosyl hydrolases family 32 superfamily
- Probable beta-glucosidase N
- Probable beta-glucosidase F
- 1,4-beta-D-glucan cellobiohydrolase C
- Probable beta-glucosidase D
- Probable beta-glucosidase E
- Probable beta-glucosidase A
- Probable beta-glucosidase L
- Probable beta-glucosidase M
Sequence:
MSFQKVDPAQIESVLSKLTLEEKISLLAGKNFWETQDYPEKGVPPVKTSDGPNGARGATFKGGVTAACFPASSLLAATWDLDAAKHIGEALADETRSKGARVLLAPTVCIHRHPLGGRNFESFSEDPFLAGKLAAQYIKGLQGNGVAATIKHYAANEQETCRFTVNEHITERALREIYLKPFEIAIKESNPLAVMTAYNIVNGTHADSNNFLLRDVLRGEWGWKGLVMSDWGGTNSTADALNAGLDLEMPGPTRWRKVDEVLAVVKSGAVLEETIDERARNVLELLAKLNCFENPTIPEEKAINRPEHQKLIRSVGSQGLVLLKNEGDVLPLRKEILTNKKVALLGFAREALIHGGGSASVNAHYRVTPEEGLRAALGDTVEFEYAKGAHTFRQLPLMSDNVVNLEGQPGWTLDFFADEEPNGEPGSSISSEQPSYIPLFVKESWGSVRASAHFTPTQSGKHYFGMSGLGRSKLLIDGEVIYEQKLNCPDSMGFLLGGVEEPEIQYSFEAGKTYAVEVVSVKPTSKGGLALLDGFIGFRLGFMTEEEHNRDLLSEAVDVAKRSDIAIVFTGHTPDWETEGQDQISFHLPSNGSQDRLVAAVGAANPNTVVVNCTGVAVAMPWLDKVKAVVQAWFPGQEAGNAIADVLTGAVNPSGRLPVSFPRAIEDAPAHGNFPGDYTDGKDNRRHLEVTYKEGVFVGYRHYDLSEANRAKVLFPFGYGLSYTTFTHANHKASATSRNTVEVAVDVTNVGTCAGADVVQVYAGAKLAVPENPVKELVGFAKVHLKPGETKTANITFEVRQLTHFTERSGKWELESGDYEISIGQSVRDITGKVEIGLEAQNYKP
Protein: Serine/threonine-protein phosphatase PP2A 65 kDa regulatory subunit (PR65) (Protein phosphatase PP2A regulatory subunit A) (P36179)
Organism: Drosophila melanogaster (Fruit fly)
Function: The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit.
Subcellular location: Nucleus {ECO:0000269|PubMed:39032490}.
Interaction partners:
- Protein phosphatase PP2A 55 kDa regulatory subunit
- Serine/threonine-protein phosphatase PP2A
- Serine/threonine protein phosphatase 2A regulatory subunit
- Well-rounded, isoform B
- Connector of kinase to AP-1, isoform E
- Cerebral cavernous malformation 3
- AT25231p
- MOB kinase activator-like 4
- Uncharacterized protein, isoform B
- CTTNBP2 N-terminal-like protein
Sequence:
MAASDKSVDDSLYPIAVLIDELKNEDVQLRLNSIKKLSTIALALGEERTRSELIPFLTETIYDEDEVLLALADQLGNFTSLVGGPEFAMYLIPPLESLATVEETVVRDKAVESLRTVAAEHSAQDLEIHVVPTLQRLVSGDWFTSRTSACGLFSVCYPRVTQPVKAELRANFRKLCQDETPMVRRAAANKLGEFAKVVETEYLKSDLIPNFVQLAQDDQDSVRLLAVEACVSIAQLLPQDDVEHLVLPTLRQCASDSSWRVRYMVAEKFVDLQKAVGPEITRVDLVPAFQYLLKDAEAEVRAAVATKVKDFCANLDKVNQVQIILSSILPYVRDLVSDPNPHVKSALASVIMGLSPMLGAYQTVEQLLPLFLIQLKDECPEVRLNIISNLDCVNDVIGIQQLSQSLLPAIVELAEDSKWRVRLAIIEYMPALAGQLGQEFFDQKLRGLCMGWLNDHVYAIREAATLNMKKLVEQFGAPWAEQAIIPMILVMSRNKNYLHRMTCLFCLNVLAEVCGTDITTKLLLPTVLLLAADPVANVRFNVAKTLQKISPFLEASVIDAQVKPTLDKLNTDTDVDVKHFAAQAIAGIAAA
Protein: Exportin-2 (Exp2) (Cellular apoptosis susceptibility protein) (Chromosome segregation 1-like protein) (Importin-alpha re-exporter) (P55060)
Organism: Homo sapiens (Human)
Function: Export receptor for importin-alpha. Mediates importin-alpha re-export from the nucleus to the cytoplasm after import substrates (cargos) have been released into the nucleoplasm. In the nucleus binds cooperatively to importin-alpha and to the GTPase Ran in its active GTP-bound form. Docking of this trimeric complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of the importin-alpha from the export receptor. CSE1L/XPO2 then return to the nuclear compartment and mediate another round of transport. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9323134}. Nucleus {ECO:0000269|PubMed:9323134}. Note=Shuttles between the nucleus and the cytoplasm. {ECO:0000269|PubMed:9323134}.
Interaction partners:
- Importin subunit alpha-5
- Importin subunit alpha-3
- Importin subunit alpha-4
- Exportin-1
- Importin subunit alpha-1
- GTP-binding nuclear protein Ran
- Exportin-4
- Exportin-T
- Ran GTPase-activating protein 1
- Nuclear pore complex protein Nup50
Sequence:
MELSDANLQTLTEYLKKTLDPDPAIRRPAEKFLESVEGNQNYPLLLLTLLEKSQDNVIKVCASVTFKNYIKRNWRIVEDEPNKICEADRVAIKANIVHLMLSSPEQIQKQLSDAISIIGREDFPQKWPDLLTEMVNRFQSGDFHVINGVLRTAHSLFKRYRHEFKSNELWTEIKLVLDAFALPLTNLFKATIELCSTHANDASALRILFSSLILISKLFYSLNFQDLPEFFEDNMETWMNNFHTLLTLDNKLLQTDDEEEAGLLELLKSQICDNAALYAQKYDEEFQRYLPRFVTAIWNLLVTTGQEVKYDLLVSNAIQFLASVCERPHYKNLFEDQNTLTSICEKVIVPNMEFRAADEEAFEDNSEEYIRRDLEGSDIDTRRRAACDLVRGLCKFFEGPVTGIFSGYVNSMLQEYAKNPSVNWKHKDAAIYLVTSLASKAQTQKHGITQANELVNLTEFFVNHILPDLKSANVNEFPVLKADGIKYIMIFRNQVPKEHLLVSIPLLINHLQAESIVVHTYAAHALERLFTMRGPNNATLFTAAEIAPFVEILLTNLFKALTLPGSSENEYIMKAIMRSFSLLQEAIIPYIPTLITQLTQKLLAVSKNPSKPHFNHYMFEAICLSIRITCKANPAAVVNFEEALFLVFTEILQNDVQEFIPYVFQVMSLLLETHKNDIPSSYMALFPHLLQPVLWERTGNIPALVRLLQAFLERGSNTIASAAADKIPGLLGVFQKLIASKANDHQGFYLLNSIIEHMPPESVDQYRKQIFILLFQRLQNSKTTKFIKSFLVFINLYCIKYGALALQEIFDGIQPKMFGMVLEKIIIPEIQKVSGNVEKKICAVGITKLLTECPPMMDTEYTKLWTPLLQSLIGLFELPEDDTIPDEEHFIDIEDTPGYQTAFSQLAFAGKKEHDPVGQMVNNPKIHLAQSLHKLSTACPGRVPSMVSTSLNAEALQYLQGYLQAASVTLL
Protein: Suppressor of disruption of TFIIS (P53078)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Could be an enzyme that inactivates 6-azauracil by modifying it.
Interaction partners:
- Uridine nucleosidase
- Purine nucleoside phosphorylase
- IMP-specific 5'-nucleotidase 1
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1
- NAD-capped RNA hydrolase NPY1
- Nicotinamide mononucleotide adenylyltransferase
- Nicotinate-nucleotide pyrophosphorylase [carboxylating]
- Nicotinate phosphoribosyltransferase
- S-methyl-5'-thioadenosine phosphorylase
Sequence:
MTVEYTASDLATYQNEVNEQIAKNKAHLESLTHPGSKVTFPIDQDISATPQNPNLKVFFFDIDNCLYKSSTRIHDLMQQSILRFFQTHLKLSPEDAHVLNNSYYKEYGLAIRGLVMFHKVNALEYNRLVDDSLPLQDILKPDIPLRNMLLRLRQSGKIDKLWLFTNAYKNHAIRCLRLLGIADLFDGLTYCDYSRTDTLVCKPHVKAFEKAMKESGLARYENAYFIDDSGKNIETGIKLGMKTCIHLVENEVNEILGQTPEGAIVISDILELPHVVSDLF
Protein: Antitoxin VapB35 (P9WF17)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Antitoxin component of a type II toxin-antitoxin (TA) system. Upon expression in M.smegmatis neutralizes the effect of cognate toxin VapC35.
Interaction partners:
- Ribonuclease VapC35
- Transcriptional repressor Mce3R
Sequence:
MNEVSIRTLNQETSKVLARVKRGEEINLTERGKVIARIIPASAGPLDSLISTGSVQPARVHGPAPRPTIPMRGGLDSGTLLERMRAEERY
Protein: S-adenosylmethionine decarboxylase proenzyme 1 (AdoMetDC1) (EC 4.1.1.50) [Cleaved into: S-adenosylmethionine decarboxylase 1 alpha chain; S-adenosylmethionine decarboxylase 1 beta chain] (Q96286)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Essential for biosynthesis of the polyamines spermidine and spermine. Essential for polyamine homeostasis, and normal plant embryogenesis, growth and development.
Interaction partners:
- Spermidine synthase 1
- Spermine synthase
- Spermidine synthase 2
- S-adenosylmethionine synthase 2
- S-adenosylmethionine synthase 4
- S-adenosylmethionine synthase 1
- S-adenosylmethionine synthase 3
- Thermospermine synthase ACAULIS5
- Arginine decarboxylase 1, chloroplastic
- Arginine decarboxylase 2
Sequence:
MALSAIGFEGYEKRLEVTFFEPSIFQDSKGLGLRALTKSQLDEILTPAACTIVSSLSNDQLDSYVLSESSFFVYPYKVIIKTCGTTKLLLSIPPLLKLAGELSLSVKSVKYTRGSFLCPGGQPFPHRSFSEEVSVLDGHFTQLGLNSVAYLMGNDDETKKWHVYAASAQDSSNCNNNVYTLEMCMTGLDREKAAVFYKDEADKTGSMTDNSGIRKILPKSEICDFEFEPCGYSMNSIEGDAISTIHVTPEDGFSYASFEAVGYDFNTLDLSQLVTRVLSCFEPKQFSVAVHSSVGANSYKPEITVDLEDYGCRERTFESLGEESGTVMYQTFEKLGKYCGSPRSTLKCEWSSNNSCSSEDEKDEGI
Protein: SNF2 domain-containing protein CLASSY 4 (EC 3.6.4.-) (Protein CHROMATIN REMODELING 40) (AtCHR40) (Q9LK10)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable chromatin remodeling factor.
Subcellular location: Nucleus {ECO:0000250, ECO:0000255|PROSITE-ProRule:PRU00768}.
Interaction partners:
- DNA-directed RNA polymerase IV subunit 1
- Protein SAWADEE HOMEODOMAIN HOMOLOG 1
- DNA-directed RNA polymerase V subunit 1
- Cation/H
- DEAD-box ATP-dependent RNA helicase 26
- DEAD-box ATP-dependent RNA helicase 34
- DExH-box ATP-dependent RNA helicase DExH18, mitochondrial
- Chromatin structure-remodeling complex protein SYD
- Probable pre-mRNA-splicing factor ATP-dependent RNA helicase DEAH3
- DExH-box ATP-dependent RNA helicase DExH1
Sequence:
MDMTSCVARRTRSRTESYLNSILNKSKGISGEEEDQSLGCVNSRTEKRRVNMRDACSPSPRKKKRRRRKDDDDDVVFVRTEYPEGKRDDENVGSTSGNLQSKSFDFGDRVCDFDADDRNLGCEEKASNFNPIDDDDDVVFVGTVQRENDHVEDDDNVGSASVISPRVCDFDEDDAKVSGKENPLSPDDDDDVVFLGTIAGENQHVEDVNAGSEVCDILLDDANLRGEEKTYVSDEVVSLSSSSDDEEDPLEELGTDSREEVSGEDRDSGESDMDEDANDSDSSDYVGESSDSSDVESSDSDFVCSEDEEGGTRDDATCEKNPSEKVYHHKKSRTFRRKHNFDVINLLAKSMLESKDVFKEDIFSWDKIAEVDSREDPVVRESSSEKVNEHGKPRERRSFHRVREKNHLNGESFYGGEKLCDGEETINYSTEDSPPLNLRFGCEEPVLIEKTEEEKELDSLWEDMNVALTLEGMHSSTPDKNGDMLCSKGTHDFVLDDEIGLKCVHCAYVAVEIKDISPAMDKYRPSVNDNKKCSDRKGDPLPNRLEFDASDPSSFVAPLDNIEGTVWQYVPGIKDTLYPHQQEGFEFIWKNLAGTTKINELNSVGVKGSGGCIISHKAGTGKTRLTVVFLQSYLKRFPNSHPMVIAPATLMRTWEDEVRKWNVNIPFYNMNSLQLSGYEDAEAVSRLEGNRHHNSIRMVKLVSWWKQKSILGISYPLYEKLAANKNTEGMQVFRRMLVELPGLLVLDEGHTPRNQSSLIWKVLTEVRTEKRIFLSGTLFQNNFKELSNVLCLARPADKDTISSRIHELSKCSQEGEHGRVNEENRIVDLKAMIAHFVHVHEGTILQESLPGLRDCVVVLNPPFQQKKILDRIDTSQNTFEFEHKLSAVSVHPSLYLCCNPTKKEDLVIGPATLGTLKRLRLKYEEGVKTKFLIDFIRISGTVKEKVLVYSQYIDTLKLIMEQLIAECDWTEGEQILLMHGKVEQRDRQHMIDNFNKPDSGSKVLLASTKACSEGISLVGASRVVILDVVWNPSVESQAISRAFRIGQKRAVFIYHLMVKDTSEWNKYCKQSEKHRISELVFSSTNEKDKPINNEVVSKDRILDEMVRHEKLKHIFEKILYHPKKSDMNTSFF