wanglab/gogpt-training-data huggingface dataset:
Protein: Ribosomal protein S6 kinase (EC 2.7.11.1) (E9PJN1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGDEDDDESCAVELRITEANLTGHEEKVSVENFELLKVLGTGAYGKVFLVRKAGGHDAGKLYAMKVLRKAALVQRAKTQEHTRTERSVLELVRQAPFLVTLHYAFQTDAKLHLILDYVSGGEMFTHLYQRQYFKEAEVRVYGGEIVLALEHLHKLGIIYRDLKLENVLLDSEGHIVLTDFGLSKEFLTEEKERTFSFCGTIEYMAPEIIRSKTGHGKAVDWWSLGILLFELLTGASPFTLEGERNTQAEVSRRILKCSPPFPPRIGPVAQDLLQRLLCKDPKKRLGAGPQGAQEVRNHPFFQGLDWVALAARKIPAPFRPQIRSELDVGNFAEEFTRLEPVYSPPGSPPPGDPRIFQGYSFVAPSILFDHNNAVMTDGLEAPGAGDRPGRAAVARSAMMQYELDLREPALGQGSFSVCRRCRQRQSGQEFAVKILSRRLEANTQREVAALRLCQSHPNVVNLHEVHHDQLHTYLVLELLRGGELLEHIRKKRHFSESEASQILRSLVSAVSFMHEEAGVVHRDLKPENILYADDTPGAPVKIIDFGFARLRPQSPGVPMQTPCFTLQYAAPELLAQQGYDESCDLWSLGVILYMMLSGQVPFQGASGQGGQSQAAEIMCKIREGRFSLDGEAWQGVSEEAKELVRGLLTVDPAKRLKLEGLRGSSWLQDGSARSSPPLRTPDVLESSGPAVRSGLNATFMAFNRGKREGFFLKSVENAPLAKRRKQKLRSATASRRGSPAPANPGRAPVASKGAPRRANGPLPPS
Protein: Propionyl-CoA carboxylase beta chain, mitochondrial (PCCase subunit beta) (EC 6.4.1.3) (Propanoyl-CoA:carbon dioxide ligase subunit beta) (P05166)
Organism: Homo sapiens (Human)
Function: This is one of the 2 subunits of the biotin-dependent propionyl-CoA carboxylase (PCC), a mitochondrial enzyme involved in the catabolism of odd chain fatty acids, branched-chain amino acids isoleucine, threonine, methionine, and valine and other metabolites. Propionyl-CoA carboxylase catalyzes the carboxylation of propionyl-CoA/propanoyl-CoA to D-methylmalonyl-CoA/(S)-methylmalonyl-CoA. Within the holoenzyme, the alpha subunit catalyzes the ATP-dependent carboxylation of the biotin carried by the biotin carboxyl carrier (BCC) domain, while the beta subunit then transfers the carboxyl group from carboxylated biotin to propionyl-CoA (By similarity). Propionyl-CoA carboxylase also significantly acts on butyryl-CoA/butanoyl-CoA, which is converted to ethylmalonyl-CoA/(2S)-ethylmalonyl-CoA at a much lower rate. Other alternative minor substrates include (2E)-butenoyl-CoA/crotonoyl-CoA (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000305|PubMed:16023992}.
Interaction partners:
- Propionyl-CoA carboxylase alpha chain, mitochondrial
- Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial
- Pyruvate carboxylase, mitochondrial
- Methylmalonyl-CoA epimerase, mitochondrial
- Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
- Methylmalonate-semialdehyde/malonate-semialdehyde dehydrogenase [acylating], mitochondrial
- Trifunctional enzyme subunit beta, mitochondrial
- 3-ketoacyl-CoA thiolase, mitochondrial
- Short-chain specific acyl-CoA dehydrogenase, mitochondrial
- 3-ketoacyl-CoA thiolase, peroxisomal
Sequence:
MAAALRVAAVGARLSVLASGLRAAVRSLCSQATSVNERIENKRRTALLGGGQRRIDAQHKRGKLTARERISLLLDPGSFVESDMFVEHRCADFGMAADKNKFPGDSVVTGRGRINGRLVYVFSQDFTVFGGSLSGAHAQKICKIMDQAITVGAPVIGLNDSGGARIQEGVESLAGYADIFLRNVTASGVIPQISLIMGPCAGGAVYSPALTDFTFMVKDTSYLFITGPDVVKSVTNEDVTQEELGGAKTHTTMSGVAHRAFENDVDALCNLRDFFNYLPLSSQDPAPVRECHDPSDRLVPELDTIVPLESTKAYNMVDIIHSVVDEREFFEIMPNYAKNIIVGFARMNGRTVGIVGNQPKVASGCLDINSSVKGARFVRFCDAFNIPLITFVDVPGFLPGTAQEYGGIIRHGAKLLYAFAEATVPKVTVITRKAYGGAYDVMSSKHLCGDTNYAWPTAEIAVMGAKGAVEIIFKGHENVEAAQAEYIEKFANPFPAAVRGFVDDIIQPSSTRARICCDLDVLASKKVQRPWRKHANIPL
Protein: Microspherule protein 1 (G3V9E0)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- KAT8 regulatory NSL complex subunit 3
- KAT8 regulatory NSL complex subunit 2
- PHD finger protein 20
- KAT8 regulatory NSL complex subunit 1
- WD repeat-containing protein 5
- UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
- Host cell factor 1
- INO80 complex subunit C
- Nuclear factor-related to kappa B-binding protein.
- Histone acetyltransferase KAT8
Sequence:
MDKDSQGLLDSSLMASGTASRSEDEESLAGQKRASSQALGTIPKRRSSSRFIKRKKFDDELVESSLAKSSTRVKGAGSVESGRCSGSEPSSSEKKKVSKAPSTPVPPSPAPTPGLTKRVKKSKQPLQVTKDLGRWKPADDLLLINAVLQTNDLTSVHLGVKFSCRFTLREVQERWYALLYDPVISKLACQAMRQLHPEAIAAIQSKALFSKAEEQLLSKVGSTSQPTLETFQDLLHRHPDAFYLARTAKALQAHWQLMKQYYLLEDQTVQPLPKGDQVLNFSDAEDLIDDSKLKDMRDEVLEHELTVADRRQKREIRQLEQELHKWQVLVDSITGMSSPDFDNQTLAVLRGRMVRYLMRSREITLGRATKDNQIDVDLSLEGPAWKISRKQGVIKLKNNGDFFIANEGRRPIYIDGRPVLCGSKWRLSNNSVVEIASLRFVFLINQDLIALIRAEAAKITPQ
Protein: Leishmanolysin (EC 3.4.24.36) (Q4QHG9)
Organism: Leishmania major
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MSVDSSSTHRRRCVAARLVRLAAAGAAVTVAVGTAAAWAHAGALQHRCVHDAMQARVRQSVADHHKAPGAVSAVGLPYVTLDAAHTAAAADPRPGSARSVVRDVNWGALRIAVSTEDLTDPAYHCARVGQHVKDHAGAIVTCTAEDILTNEKRDILVKHLIPQAVQLHTERLKVQQVQGKWKVTDMVGEICGDFKVPQAHITEGFSNTDFVMYVASVPSEEGVLAWATTCQTFSDGHPAVGVINIPAANIASRYDQLVTRVVTHEMAHALGFSGPFFEDARIVASVPNVRGKNFDVPVINSSTAVAKAREQYGCDTLEYLEMEDQGSAGSAGSHIKMRNAQDELMAAASGAGYYTALTMAILQDLGFYQADFSKAEVMPWGQNAGCAFLTNKCMEQNITQWPAMFCNESEDAIRCPTSRLSLGACGVTRHPGLPPYWQYFTDPSLAGVSAFMDYCPVVVPYSDISCTQRASEAHASLLPFNVFSDAARCIDGAFRPKATNGIVKSYAGLCANVQCDTATRTYSVQVHGSNDYTNCTPGLRVELSTVSNAFEGGGYITCPPYVEVCQGNVQAAKDGGNTAAGRRGPRAAATALLVAALLAVAL
Protein: Calcium-transporting ATPase 4, endoplasmic reticulum-type (EC 7.2.2.10) (Q9XES1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to an endomembrane compartment.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Vacuolar cation/proton exchanger 3
- Purple acid phosphatase 18
- V-type proton ATPase subunit c''2
- Putative clathrin assembly protein At2g25430
Sequence:
MGKGGEDCGNKQTNSSELVKSDTFPAWGKDVSECEEKFGVSREKGLSTDEVLKRHQIYGLNELEKPEGTSIFKLILEQFNDTLVRILLAAAVISFVLAFFDGDEGGEMGITAFVEPLVIFLILIVNAIVGIWQETNAEKALEALKEIQSQQATVMRDGTKVSSLPAKELVPGDIVELRVGDKVPADMRVVALISSTLRVEQGSLTGESEAVSKTTKHVDENADIQGKKCMVFAGTTVVNGNCICLVTDTGMNTEIGRVHSQIQEAAQHEEDTPLKKKLNEFGEVLTMIIGLICALVWLINVKYFLSWEYVDGWPRNFKFSFEKCTYYFEIAVALAVAAIPEGLPAVITTCLALGTRKMAQKNALVRKLPSVETLGCTTVICSDKTGTLTTNQMAVSKLVAMGSRIGTLRSFNVEGTSFDPRDGKIEDWPTGRMDANLQMIAKIAAICNDANVEKSDQQFVSRGMPTEAALKVLVEKMGFPEGLNEASSDGNVLRCCRLWSELEQRIATLEFDRDRKSMGVMVDSSSGKKLLLVKGAVENVLERSTHIQLLDGSTRELDQYSRDLILQSLHDMSLSALRCLGFAYSDVPSDFATYDGSEDHPAHQQLLNPSNYSSIESNLVFVGFVGLRDPPRKEVRQAIADCRTAGIRVMVITGDNKSTAEAICREIGVFEADEDISSRSLTGKEFMDVKDQKNHLRQTGGLLFSRAEPKHKQEIVRLLKEDGEVVAMTGDGVNDAPALKLADIGVAMGISGTEVAKEASDLVLADDNFSTIVAAVGEGRSIYNNMKAFIRYMISSNIGEVASIFLTAALGIPEGMIPVQLLWVNLVTDGPPATALGFNPPDKDIMKKPPRRSDDSLITAWILFRYMVIGLYVGVATVGVFIIWYTHNSFMGIDLSQDGHSLVSYSQLAHWGQCSSWEGFKVSPFTAGSQTFSFDSNPCDYFQQGKIKASTLSLSVLVAIEMFNSLNALSEDGSLVTMPPWVNPWLLLAMAVSFGLHFVILYVPFLAQVFGIVPLSLNEWLLVLAVSLPVILIDEVLKFVGRCTSGYRYSPRTPSAKQKEE
Protein: Fasciclin-like arabinogalactan protein 8 (AtAGP8) (O22126)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be a cell surface adhesion protein.
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor.
Interaction partners:
- Glycerophosphodiester phosphodiesterase GDPDL4
- Fasciclin-like arabinogalactan protein 16
- Fasciclin-like arabinogalactan protein 15
- Arabinogalactan protein 12
- Classical arabinogalactan protein 9
- Classical arabinogalactan protein 26
- Fasciclin-like arabinogalactan protein 18
- Arabinogalactan protein 14
- Non-classical arabinogalactan protein 30
- Fasciclin-like arabinogalactan protein 21
Sequence:
MAASQTFSLLAFTFSLLAFASTVSSHNITQILADSPDYSSFNSYLSQTKLADEINSRTTITVLVLNNGAMSALAGKHPLSVIKSALSLLVLLDYYDPQKLHKISKGTTLSTTLYQTTGNAPGNLGFVNITDLKGGKVGFGSAASGSKLDSSYTKSVKQIPYNISILEIDAPIIAPGVLTAPAPSASLSNITGLLEKAGCKTFANLLVSSGVLKTYESAVEKGLTVFAPSDEAFKAEGVPDLTKLTQAEVVSLLEYHALAEYKPKGSLKTNKNNISTLATNGAGKFDLTTSTSGDEVILHTGVAPSRLADTVLDATPVVIFTVDNVLLPAELFGKSKSPSPAPAPEPVTAPTPSPADAPSPTAASPPAPPTDESPESAPSDSPTGSANSKSANAAVGVSTPSLFTALVTIAAIAVSVSLCS
Protein: Uncharacterized protein P19A11.02c (Q9HDV8)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Single-pass type I membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Spore wall structural constituent isp3
Sequence:
MQFSVLCKFLLLVTAVMAQTEYTPGFTTDVATTVTPTPLPSANVTTTSFSSASTETSTHSVTSTNITSIVPPPSTSHNSTTTTVPPTTSMNTTTTVPPTTSLNTTTTTAPPTTHVNSTTTVVPPTTHVNTTTVVPPTTHVNTTTVVPPTTHANTTSFVPTTTESSIHPITTGFYNTTFTTGYFNTSVTSVAVHNSTTVFPTSVPIVNTTSFNVTTIPSSAVHYASPSGLLALVVMLISAFAFLA
Protein: Homeodomain-interacting protein kinase 4 (EC 2.7.11.1) (Q3V016)
Organism: Mus musculus (Mouse)
Function: Protein kinase that phosphorylates murine TP53 at Ser-9, and thus induces TP53 repression of BIRC5 promoter. May act as a corepressor of transcription factors (Potential).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18022393}.
Interaction partners:
- Cellular tumor antigen p53
- Ras association domain-containing protein 5
Sequence:
MATIQSETDCYDIIEVLGKGTFGEVAKGWRRSTGEMVAIKILKNDAYRSRIIKNELKLLRCVRGLDPDEAHVIRFLEFFHDALKFYLVFELLEQNLFEFQKENNFAPLPARHIRTVTLQVLRALARLKELAIIHADLKPENIMLVDQTRCPFRVKVIDFGSASIFSEVRYVKEPYIQSRFYRAPEILLGLPFCEKVDVWSLGCVMAELHLGWPLYPGNNEYDQVRYICETQGLPKPHLLHAARKAHHFFKRNPHPDATNPWQLKSSADYLAETKVRPLERRKYMLKSLDQIETVNGGGAVSRLSFPDREALAEHADLKSMVELIKRMLTWESHERISPSAALRHPFVSMQQLRSAHEATRYYQLSLRGCRLSLQVDGKPPPPVIASAEDGPPYYRLAEEEETAGLGGVTGSGSFFREDKAPGMQRAIDQLDDLSLQEARRGLWSDTRADMVSDMLVPLKVASTSHRVPDSGPEPILAFYGSRLTGRHKARKAPAGSKSDSNFSNLIRLSQASPEDAGPCRGSGWEEGEGRTTSTEPSVIPQREGDGPGIKDRPMDAERPGPELFDPSSCPGEWLSEPEWTLEGIRGSRAQGLPAHHPHPHGPPRTTSFLQHVGGHH
Protein: Cholesterol 22-hydroxylase CYP90B27 (EC 1.14.14.-) (Cytochrome P450 CYP90B27) (PpCYP90B27) (A0A5A4DV62)
Organism: Paris polyphylla (Daiswa polyphylla)
Function: Involved in the biosynthesis of steroidal saponins and alkaloids natural products from cholesterol such as spirostane-type saponins and polyphyllins, compounds with pharmacological activity. Catalyzes the C-22 hydroxylation of cholesterol to form 22R-hydroxycholesterol.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MALELILVLSSLIVILIIFFSFKSNGKSENKLAKLPPGQMGWPFIGQTIPFMQPHSSASLGLFMDQNIAKYGRIFRTNLLAKPTIVSADPDFNRYILQNEGRLFENSCPTSIKEIMGPWSMLALAGDIHREMRSIAVNFMSNVKLRTYFLPDIEQQAIKVLASWENTPEAFSAQEQGKKFAFNLMVKHLMSMDPGMPETEKLRTEYHAFMKGMASIPLNLPGTAYRKALQSRSIILKIMGQKLDERIRQVRDGCEGLEQDDLLASVSKHPHLTKEQILDLILSMLFAGHETSSAAIALAIYFLDSCPKAAQQLREEHVEIARQKAERGETGLNWDDYKQMEFTHCVINETLRLGNIVKFLHRKTLKDVQFKGYDIPCGWEVVTIISAAHLDPSVYDEPQRYNPWRWQNISATASKNNSIMSFSGGPRLCPGAELAKLEMAVFLHHLVRKFHWELAEHDYPVSFPFLGFPKGLPIKVRPLEKSEA
Protein: Small ribosomal subunit protein mS26 (28S ribosomal protein S26, mitochondrial) (Q2ACD8)
Organism: Gallus gallus (Chicken)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}. Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MAPGGCLLLALLLLAGTAQGQHWSHGWYPGGKRDLSAPQAIPAWSPWLVPSRGRKSRYDPPAKSKASRLKVPPPVDPAELYVVTERYRQHRLVLSALRSIFRSEVVQRKREAQRDAEDSAALSEEHRLLMAWNDAENARQRARREERIR
Protein: Ubiquitin carboxyl-terminal hydrolase 21 (EC 3.4.19.12) (Deubiquitinating enzyme 21) (AtUBP21) (Ubiquitin thioesterase 21) (Ubiquitin-specific-processing protease 21) (Q9FIQ1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins (By similarity).
Interaction partners:
- Rho GTPase-activating protein
- SMAD/FHA domain-containing protein
- Holliday junction resolvase
- Ubiquitin-conjugating enzyme E2 20
- Ubiquitin-conjugating enzyme E2 19
- ATPase family AAA domain-containing protein FIGL1
- Proteasome subunit alpha type-3
- At1g65985
Sequence:
MAEFSDPPPSNLSSSHKLTKPNQTLDESSPTAPIRDLVTNSLSLSSPIRQIQALSPAKPDGSSSSPPDKTLNFNPEENRDVNPDESSSSPSDKTLIAPPAQISPVSNNNHLRITNTSDSYLYRPPRRYIEYESDDDELNKMEPTKPLQLSWWYPRIEPTGVGAGLYNSGNTCFIASVLQCFTHTVPLIDSLRSFMYGNPCNCGNEKFCVMQALRDHIELALRSSGYGINIDRFRDNLTYFSSDFMINHQEDAHEFLQSFLDKLERCCLDPKNQLGSVSSQDLNIVDNVFGGGLMSTLCCCNCNSVSNTFEPSLGWSLEIEDVNTLWKALESFTCVEKLEDQLTCDNCKEKVTKEKQLRFDKLPPVATFHLKRFTNDGVTMEKIFDHIEFPLELDLSPFMSSNHDPEVSTRYHLYAFVEHIGIRATFGHYSSYVRSAPETWHNFDDSKVTRISEERVLSRPAYILFYAREGTPWFSSTFEQLKTVFEATPLHFSPVSVLDNSYESVDNSSKACNDSVGVSIPDVKWPDSCCQEPKEEVFHSAESSNNEDSSAMIDALGSPQSEKPFAETSQQTEPESCPTENKAYIDKSEKPFAETSQPKEPKPFADRASIDAPLLKVQNQDISPKRKAGERATLGGPKLKYQKPNSHQKRQGTFQIQRAHLQTKKQEESRKTKRPLFRSNVAASAPDPKYKNHALSYLNRAQTPRARKLANALSDSPTKKKKSSNMRRSIKL
Protein: Glutamate receptor (G1TPJ8)
Organism: Oryctolagus cuniculus (Rabbit)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Postsynaptic cell membrane {ECO:0000256|RuleBase:RU367118}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU367118}.
Interaction partners:
- Glutamate receptor
- Glutamate receptor
- Glutamate ionotropic receptor NMDA type subunit 2A
- Peripheral plasma membrane protein CASK
- Glutamate ionotropic receptor NMDA type subunit 2C
- Glutamate receptor
- Metabotropic glutamate receptor 1
Sequence:
MKDETRSQELHSGLPHGCQGPRLCGSSSAAFPDTLTGSWVGNGAAGTRTGAHMRRWCHRQQLSLLGLDSLTPGPTDIAGEGGERALRGTPLSELGAEGPLAAARRASARGRGLTSGPSRQEKGSTFLQLGSSTEQQLQVIFEVLEEYDWTSFVAVTTRAPGHRAFLSYIEVLTDGSLVGWEHRGALTLDPGAGEAVLGAQLRSVSAQIRLLFCAREEAEPVFRAAEEAGLTGPGYVWFMVGPQLAGGGGSGAPGEPPLLPGGVPLPAGLFAVRSAGWRDDLARRVAAGVAVVARGAQALLRDYGFLPELGHDCRAQNRTHRGESLHRYFMNITWDNRDYSFNEDGFLVNPSLVVISLTRDRTWEVVGSWEQQTLRLKYPLWSRYGRFLQPVDDTQHLTVATLEERPFVIVEPADPTSGTCIRDSVPCRSQLNRTHSPPPDAPRPEKRCCKGFCIDILKRLAHTIGFSYDLYLVTNGKHGKKIDGVWNGMIGEVFYQRADMAIGSLTINEERSEIVDFSVPFVETGISVMVARSNGTVSPSAFLEPYSPAVWVMMFVMCLTVVAVTVFIFEYLSPVGYNRSLATGKRPGGSTFTIGKSIWLLWALVFNNSVPVENPRGTTSKIMVLVWAFFAVIFLASYTANLAAFMIQEEYVDTVSGLSDRKFQRPQEQYPPLKFGTVPNGSTEKNIRSNYPDMHSYMVRYNQPRVEEALTQLKAGKLDAFIYDAAVLNYMARKDEGCKLVTIGSGKVFATTGYGIALHKGSRWKRPIDLALLQFLGDDEIEMLERLWLSGICHNDKIEVMSSKLDIDNMAGVFYMLLVAMGLSLLVFAWEHLVYWRLRHCLGPTHRMDFLLAFSRGMYSCCSAEAAPPPAKXXXXXXXXXXXXXXXX
Protein: Intron-binding protein aquarius (Q9U1Q7)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|PIRNR:PIRNR038901}.
Interaction partners:
- Pre-mRNA-processing factor 19
- Pre-mRNA-splicing factor SYF1
- TPR_REGION domain-containing protein
- Tr-type G domain-containing protein
- Cell division cycle 5-like protein
- Protein isy-1
- Pre-mRNA-splicing factor 8 homolog
- Peptidyl-prolyl cis-trans isomerase E
- Pre-mRNA-splicing factor RBM22
- Protein BUD31 homolog
Sequence:
MVTKRHQEAVVTRGAIENDTISAVAAKFWAPFTAETHENFDAKLIDTIYDNEMLKTSFNSRKIMMLEFSQYLEAYLWPNYVPEKASKAWNMSIVVMINEKFRERNLDSWNCFTKKSEHFPHFFKSILQLSLQEEGLASSEHCALLTFLVNAFGSVETPIVHKETRKLVSIEIWAGLLDSQREDLFKKQKKLKKIWENVRQKMTAAAADNNEFERTYLWNLIEKFKRVLNSLEPNEAQESEEGEVRDPIDSIKYCERFIELLIDLESILQTRRFFNSVLHSSHILTHCLLSSLISTDAGSLFFQLVQLLKFYARFEIDDLSGRQLTHKEVSEQHYQSVTRLQKAAFRLFNETMKEFYVLNVSGVDTRRALQKQFGDMNHAEVYRFAEYLHLVPAFGEDPNHQTSLLHLYPHQHLVETITLHCERRPNQLTQLNEKPLFPTEKVIWDENIIPYENYTGDGVLALDKLNLQFLTLHDYLLRNFNLFQLESTYEIRQDLEDVLFRMKPFQHESRNETVFSGWARMALQIDHFQISEVAKPLVGEKSPAVVRGVVTVNIGRRQDIRQEWENLRKHDVCFLVACRSRKSASGLKFDVRRPFSEQIEVLSVRGCDVEGMLDQDGHLLEEFTAWEKKAKIPGDLRKFRLLLDPNQYRIDMEQGTKDDIYDTFNLIVRRDSKTNNFKAVLQTIRDLLNTECVVPDWLTDVILGYGEPDSAHYSKLSSAVPELDFNDTFLSFAHVKESFPGYKIELADGFDEKEAVPPFKLEFKELERRQDVEIKPGELRTILVTPLTRKKVTPYSYDPRKNQVKFTPSQVEAIKSGMQPGLTMVVGPPGTGKTDVAVQIISNIYHNWPNQRTLIVTHSNQALNQLFEKIIALDVDERHLLRMGHGEEALETEKDFSRYGRVNYVLKERLQLLNCVEKLAKALKIVGDVAYTCENAGYFFRFSVCRVWEEFLAKVTSKGCNKLAEGIISEIFPFTGFFKDIPDLFSGNNSADLKVAHSCWRHIEQIFEKLDEFRAFELLRNGRDRTEYLLVKEAKIIAMTCTHAALRRNELVKLGFRYDNIVMEEAAQILEVETFIPLLLQNPQDGHNRLKRWIMIGDHHQLPPVVQNQAFQKYSNMEQSLFARLVRLSVPNVQLDRQGRARAQIAELYQWRYNGLGNLPHVDGLPQFQNANAGFAFPFQFIDIPDFNGHGETQPSPHFYQNLGEAEYACALYTYMRILGYPAEKISILTTYNGQAQLIRDVFQRRCDTNPLIGMPAKVSTVDKYQGQQNDFIILSLVKTRNIGHIRDVRRLVVALSRARLGLYVLGRSKVFMDCLELTPAMRIFAKYPRKLVILPFEAHPTIRKWNERSKDGEPMEIQDTLHMTHFVHEFYMSNLPAMRDAYEQAMNEYMESQRLLNPPIDETQMDVETEHEKKHREAMERKKKQEMDDKKEADIHFEDMDHEMQEPAATAAPAPGAPAVEEPPPK
Protein: Single-stranded DNA-binding protein WHY1, chloroplastic (Protein PLASTID TRANSCRIPTIONALLY ACTIVE 1) (Protein WHIRLY 1) (AtWHY1) (Q9M9S3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Single-stranded DNA-binding protein that functions in both chloroplasts and nucleus. In chloroplasts, maintains plastid genome stability by preventing break-induced and short homology-dependent illegitimate recombinations. In nucleus, modulates telomere length homeostasis by inhibiting the action of the telomerase at the extreme termini of chromosomes. Is recruited to a distal element upstream of the kinesin KP1 to mediate the transcriptional repression of KP1. Is required for full salicylic acid-dependent plant disease resistance responses. Can bind double-stranded DNA in vivo.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:15967440}. Nucleus {ECO:0000269|PubMed:14960277, ECO:0000269|PubMed:15967440}. Note=Can localize to both chloroplast and nucleus (PubMed:15967440).
Interaction partners:
- Protein PLASTID TRANSCRIPTIONALLY ACTIVE 12, chloroplastic
- Plastid transcriptionally active 18
- Chloroplastic group IIA intron splicing facilitator CRS1, chloroplastic
- MAR-binding filament-like protein 1
- Plastid transcriptionally active 3
- Fructokinase-like 2, chloroplastic
- Pentatricopeptide repeat-containing protein At1g74850, chloroplastic
- CBL-interacting serine/threonine-protein kinase 14
Sequence:
MSQLLSTPLMAVNSNPRFLSSSSVLVTGGFAVKRHGFALKPTTKTVKLFSVKSRQTDYFEKQRFGDSSSSPSPAEGLPARFYVGHSIYKGKAALTVDPRAPEFVALDSGAFKLSKDGFLLLQFAPSAGVRQYDWSKKQVFSLSVTEIGTLVSLGPRESCEFFHDPFKGKSDEGKVRKVLKVEPLPDGSGHFFNLSVQNKLVNVDESIYIPITRAEFAVLISAFNFVLPYLIGWHAFANSIKPEETSRVNNASPNYGGDYEWNR
Protein: TGFB-induced factor homeobox 1 (A0A8I6GEN1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00108}.
Interaction partners:
Sequence:
MKTLGVVAAASGSDSEDEDSMDSPLDLSSSAASGKRRRRGNLPKESVQILRDWLYEHRYNAYPSEQEKALLSQQTHLSTLQVCNWFINARRRLLPDMLRKDGKDPNQFTISRRGAKISEASSIEAAMGIKNFMPTLEESPFHSCVVGPNPTLGRPVSPKPPSPGPILARPSVICHTTVTALKDGPFSLCQAVSVGHSTDVQQVAPSNFTDASLRYPEDTCKSGPSPNPQSGLFNTPPPTPPDLNQDFSGFQLLVDVALKQAAEMELQAKLTA
Protein: Stress-response A/B barrel domain-containing protein DABB1 (Dimeric A/B barrel domain-containing protein 1) (AtDabb1) (Q9SYD8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in defense against fungal pathogens. Possesses antifungal activity against diverse pathogenic fungi.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:18674644}.
Interaction partners:
- Aminomethyltransferase, mitochondrial
- Putative transferase At1g60990, chloroplastic
- FAD-dependent oxidoreductase domain-containing protein 1
- Monodehydroascorbate reductase 2
- Monodehydroascorbate reductase, chloroplastic/mitochondrial
- Monodehydroascorbate reductase 1, peroxisomal
- Monodehydroascorbate reductase 3
- Monodehydroascorbate reductase 4, peroxisomal
Sequence:
MSSIVEHVVLFKLNDDDVDSGKINSMVNGINELVNLDQVLHLYCGSIHRLITTTASDFTHVLHSRYRSKEDLNAYAIHPDHVRVVKESESIREDIMAVDWIAEQAPEALAPPLGSIGKITLLKLKENVMEEAKLEIMEVMKEKFEGIDQITVGENFSPGRSKDFSIGSISYFRDLGEIEAVDDQMKLQNDKIRDYVDDTIVVEFNVPSSS
Protein: Testis-expressed protein 35 (Testis-specific conserved protein of 24 kDa) (Q14BK3)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000269|PubMed:17077512}.
Interaction partners:
- Sperm-associated microtubule inner protein 10
- Spermatogenesis-associated protein 45
Sequence:
MSAKNAELKKTNLKKNYKAVCMEPKLTQIYDFKGFKQEGLLIRKGMTRELKNELREVREQLTEKMEEIKQIKDIMDKDFDKLYEFVEIMKEMQQDMDEKMDVLINNQKNNKLPFQNQAKEQQKFWQLGKMDKSSQAMITEEPDGVPLACDKNVVPPKPTRNPLESLHPCQSCCEKCLLCALKTNRNQGRPSHHAWVPFSPLSSGAAF
Protein: Apolipoprotein C-II (Apo-CII) (ApoC-II) (Apolipoprotein C2) [Cleaved into: Proapolipoprotein C-II (ProapoC-II)] (P02655)
Organism: Homo sapiens (Human)
Function: Component of chylomicrons, very low-density lipoproteins (VLDL), low-density lipoproteins (LDL), and high-density lipoproteins (HDL) in plasma. Plays an important role in lipoprotein metabolism as an activator of lipoprotein lipase. Both proapolipoprotein C-II and apolipoprotein C-II can activate lipoprotein lipase. In normolipidemic individuals, it is mainly distributed in the HDL, whereas in hypertriglyceridemic individuals, predominantly found in the VLDL and LDL.
Subcellular location: Secreted {ECO:0000269|PubMed:3525527}.
Interaction partners:
- Apolipoprotein C-III
- Apolipoprotein E
- Apolipoprotein C-I
- Lipoprotein lipase
- Apolipoprotein A-I
- Apolipoprotein A-II
- Apolipoprotein A-V
- Apolipoprotein B-100
- Apolipoprotein A-IV
- Apolipoprotein C-IV
Sequence:
MGTRLLPALFLVLLVLGFEVQGTQQPQQDEMPSPTFLTQVKESLSSYWESAKTAAQNLYEKTYLPAVDEKLRDLYSKSTAAMSTYTGIFTDQVLSVLKGEE
Protein: Membrane frizzled-related protein (Membrane-type frizzled-related protein) (Q9BY79)
Organism: Homo sapiens (Human)
Function: May play a role in eye development.
Subcellular location: Apical cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Complement C1q tumor necrosis factor-related protein 5
- Visual system homeobox 2
- Serine protease 56
- Protein RD3
- Transmembrane protein 98
Sequence:
MKDFSDVILCMEATESSKTEFCNPAFEPESGPPCPPPVFPEDASYSVPAPWHGRRPRGLRPDCRFSWLCVLLLSSLLLLLLGLLVAIILAQLQAAPPSGASHSPLPAGGLTTTTTTPTITTSQAAGTPKGQQESGVSPSPQSTCGGLLSGPRGFFSSPNYPDPYPPNTHCVWHIQVATDHAIQLKIEALSIESVASCLFDRLELSPEPEGPLLRVCGRVPPPTLNTNASHLLVVFVSDSSVEGFGFHAWYQAMAPGRGSCAHDEFRCDQLICLLPDSVCDGFANCADGSDETNCSAKFSGCGGNLTGLQGTFSTPSYLQQYPHQLLCTWHISVPAGHSIELQFHNFSLEAQDECKFDYVEVYETSSSGAFSLLGRFCGAEPPPHLVSSHHELAVLFRTDHGISSGGFSATYLAFNATENPCGPSELSCQAGGCKGVQWMCDMWRDCTDGSDDNCSGPLFPPPELACEPVQVEMCLGLSYNTTAFPNIWVGMITQEEVVEVLSGYKSLTSLPCYQHFRRLLCGLLVPRCTPLGSVLPPCRSVCQEAEHQCQSGLALLGTPWPFNCNRLPEAADLEACAQP
Protein: ATP synthase subunit O, mitochondrial (Oligomycin sensitivity conferral protein) (OSCP) (Q24439)
Organism: Drosophila melanogaster (Fruit fly)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements.
Subcellular location: Mitochondrion. Mitochondrion inner membrane.
Interaction partners:
- ATP synthase subunit beta, mitochondrial
- ATP synthase-coupling factor 6, mitochondrial
- Protein stunted
- ATP synthase F
- ATP synthase subunit g
- ATP synthase subunit d, mitochondrial
- Putative ATP synthase subunit f
- ATP synthase subunit alpha, mitochondrial
- ATP synthase F
- ATP synthase subunit gamma, mitochondrial
Sequence:
MASINKLALLSRTLSSAAAQATVKPPVQVFGLEGRYATALYSAASKLSQLDQVEKDLTALQATIRSDKKLREYVTSPIINKKVMATALKEASEKLRFAPATVNLLGLLADNGRLKKLDTVINAYKTIMAAHRGEVVCEVVTAKPLDASQSKQLEGALKSFLKGNESLKITSRVDPSIIGGLIVSIGDKYVDMSIATKVKLYTDVIQTAA
Protein: (Z)-2-((N-methylformamido)methylene)-5-hydroxybutyrolactone dehydrogenase (MFMB dehydrogenase) (EC 1.2.1.-) (Q6F9F7)
Organism: Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Function: Involved in the degradation of the pyridine ring of trigonelline (TG; N-methylnicotinate) into succinate and methylamine as carbon and nitrogen sources, respectively. Catalyzes the NAD(+)-dependent oxidation of (Z)-2-((N-methylformamido)methylene)-5-hydroxybutyrolactone (MFMB) to yield (E)-2-((N-methylformamido)methylene)succinate (MFMS).
Interaction partners:
- Flavin-dependent trigonelline monooxygenase, oxygenase component
- Peptide synthetase
- Flavin-dependent trigonelline monooxygenase, reductase component
- (E)-2-((N-methylformamido)methylene)succinate hydrolase (MFMS hydrolase)
Sequence:
MQQFQLYINGKFEDGAAQFDSINPATGEIWAKMPEARTDQVNRAVDAAEQAFYDSSWSGLTASQRGKLLYKLADLVEKSAPRLAALETTDTGKIIRETSSQIAYVAEYYRYYAGLADKIEGSFIPVDKPDMQAWLVREPVGVVAAIVPWNSQLFLSAVKVGPALAAGCTVVLKASEEAPAPLLEFAKLIDEAGFPAGVVNVITGFGPECGAVLSAHPKVAHIAFTGGPETAKHIVRNSAENLAKVSLELGGKSPFIVFADTDINSALNAQIAAIFAATGQSCVAGSRLLIEESIKDEFLQRLAERVQSIKMGLPDDMQTEYGPLCTLKQREKIQQVVQRSVEQGAKLITGGQVCDGAGYYYPPTILDCSGVSDAQSIHTELFGPVLSVDTFSTEAEAIQKANSTPYGLASGVFTSNLTRAHRMTRAIRSGIVWLNTYRVVSPLAPFGGYGLSGHGREGGLSAALEYTTTKTVWLRMSDQPIDDPFVMR