wanglab/gogpt-training-data huggingface dataset:
Protein: Proline dehydrogenase 1, mitochondrial (EC 1.5.5.2) (Proline oxidase) (Protein sluggish-A) (Q04499)
Organism: Drosophila melanogaster (Fruit fly)
Function: Converts proline to delta-1-pyrroline-5-carboxylate. Involved in the conversion of proline to glutamate, which functions as transmitter at neuromuscular junctions. Glutamate deficiency could possibly account for reduced motor activity.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:8096642}.
Interaction partners:
- GH20963p
- Multifunctional fusion protein
- Pyrroline-5-carboxylate reductase
- Pyrroline-5-carboxylate reductase
- Cytosol aminopeptidase
- Cytosol aminopeptidase
- Cytosol aminopeptidase
- Cytosol aminopeptidase
- Cytosol aminopeptidase
- Cytosol aminopeptidase
Sequence:
MALLRSLSAQRTAISLVYGRNSSKSSNSVAVAACRSFHQRGSGSTSIAGEGAASESTRGVNGARFLHSGDRPLQASTLVQPEVVSSETVKRSMKQESSQEKNPSPAGSPQRDPLDVSFNDPIAAFKSKTTGELIRAYLVYMICSSEKLVEHNMTLMKLARNLLGQKLFVLLMKSSFYGHFVAGENRHTIVPALERLRSFGVKPILDYSVEEDITQEEAEKREVESSVSSAGDKKEEGSMPQYHVDKSFADRRYKVSSARTYFYLNEATCERNMEIFIKCLEAVSDDDRKAPRAVATGATFGTGITAIKLTALGRPQLLLQLSEVIMRTRKYMEDMVGGQGNVLTHHKTIKDLEKYYATLGDNKDVKEFLNNVTSDKEGILHLFPWSGIVDEDSQLSDTFRVPDPQTGQMRRLISQIPPKEEEMFRNMIRRLNTIVKAAADLDVRIMVDAEQTYFQPAISRITLEMMRKYNKDKAIVFNTYQCYLRETFREVNTDLEQAKRQNFYFGAKLVRGAYMDQERDRAKSLGYPDPVNPTFEATTDMYHRTLSECLRRIKLMKDCDDDARKIGIMVASHNEDTVRFAIQQMKEIGISPEDKVICFGQLLGMCDYITFPLGQAGYSAYKYIPYGPVEEVLPYLSRRAQENKGVLKKIKKEKRLLLSEIRRRLMRGQLFYKPKGNYVPI
Protein: Transcription factor E2-alpha (Transcription factor 3) (Q70IK3)
Organism: Gallus gallus (Chicken)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MNQQQQRMAAVGTDKELSDLLDFSMMFPLPVANGKNRPTTLASTQFGGSGLDERPGSGSWGTGDQNSSTFDQGRQSYGEGPHYGEHRDLPSHNSLSSSPFLGPGLVGKSGERASYSTFGRDAGMPGLSQTGFLPSEMGIASPSTLSPTGVKGGSQYFSYPNNPRRRGAESSIADGQPKKVRKVPPGLPSSVYPSNSGDDYSRDPAGYTPSKPPSTVYPGAFYMADGLHNSPDLWSSPGAMSQSSYGAMLGSSSSPLPQSASFNSLHQHERMNYQLHSGELNGGLPSVSGFSSASTPYGVSSHTPPISGTDTMMGNRGTTAGSSGDALGKALASIYSPDHSSNNFSSNPSTPVGSPQGLAGTSQWSRAGGQGALSPSYEGSLHTLQNKMEDRLDEAIHVLRNHAVGQTAAMPSNHGDMHGLLGSAPAHSAAVGSLGQAFPASVMSLGGRHPSLVGGGHPEDGLSSTPSMLHNHVTLPSQPSSLPDLNRQQDTYSGLSGGLGRSSVSSGTNEIKREEKEDEENTSVADNSEEEKKELKPSRNRTSQDEDEEDDLLPPEQKAERERERRVANNARERLRVRDINEAFKELGRMCQLHLNSEKPQTKLLILHQAVSVILNLEQQVRERNLNPKAACLKRREEEKVSGVVGDPQMTLSASHPGLGDGHNPVGHM
Protein: Protein TMED8 (Q6PL24)
Organism: Homo sapiens (Human)
Interaction partners:
- Delta-1-pyrroline-5-carboxylate synthase
Sequence:
MSDLQAAEGPGSWSPTARPGSAGGVGDCQGVEGSQAAASENEDLENKDTSLLASATDPEPCSSPHRPQMVSPVSKDATEDLRKATGPLEAQALVKQDLLPADQAQVLNEMAKYQVPQRSGDIVMIQSEHTGAIDVLSADLESADLLGDHRKVSPPLMAPPCIWTFAKVKEFKSKLGKEKNSRLVVKRGEVVTIRVPTHPEGKRVCWEFATDDYDIGFGVYFDWTPVTSTDITVQVSDSSDDEDEEEEEEEEIEEPVPAGDVERGSRSSLRGRYGEVMPVYRRDSHRDVQAGSHDYPGEGIYLLKFDNSYSLLRNKTLYFHIYYTS
Protein: Ceramide kinase (hCERK) (EC 2.7.1.138) (Acylsphingosine kinase) (Lipid kinase 4) (LK4) (Q8TCT0)
Organism: Homo sapiens (Human)
Function: Catalyzes specifically the phosphorylation of ceramide to form ceramide 1-phosphate. Acts efficiently on natural and analog ceramides (C6, C8, C16 ceramides, and C8-dihydroceramide), to a lesser extent on C2-ceramide and C6-dihydroceramide, but not on other lipids, such as various sphingosines. Shows a greater preference for D-erythro isomer of ceramides. Binds phosphoinositides.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19168031}. Cell membrane {ECO:0000269|PubMed:16269826, ECO:0000269|PubMed:19168031}; Peripheral membrane protein {ECO:0000269|PubMed:19168031}.
Interaction partners:
- Acid ceramidase
- Ceramide glucosyltransferase
- Neutral ceramidase
- Alkaline ceramidase 2
- Alkaline ceramidase 1
- Ceramide synthase 6
- Sphingomyelin phosphodiesterase
- Ceramide synthase 2
- Phosphatidylcholine:ceramide cholinephosphotransferase 1
- Ceramide synthase 4
Sequence:
MGATGAAEPLQSVLWVKQQRCAVSLEPARALLRWWRSPGPGAGAPGADACSVPVSEIIAVEETDVHGKHQGSGKWQKMEKPYAFTVHCVKRARRHRWKWAQVTFWCPEEQLCHLWLQTLREMLEKLTSRPKHLLVFINPFGGKGQGKRIYERKVAPLFTLASITTDIIVTEHANQAKETLYEINIDKYDGIVCVGGDGMFSEVLHGLIGRTQRSAGVDQNHPRAVLVPSSLRIGIIPAGSTDCVCYSTVGTSDAETSALHIVVGDSLAMDVSSVHHNSTLLRYSVSLLGYGFYGDIIKDSEKKRWLGLARYDFSGLKTFLSHHCYEGTVSFLPAQHTVGSPRDRKPCRAGCFVCRQSKQQLEEEQKKALYGLEAAEDVEEWQVVCGKFLAINATNMSCACRRSPRGLSPAAHLGDGSSDLILIRKCSRFNFLRFLIRHTNQQDQFDFTFVEVYRVKKFQFTSKHMEDEDSDLKEGGKKRFGHICSSHPSCCCTVSNSSWNCDGEVLHSPAIEVRVHCQLVRLFARGIEENPKPDSHS
Protein: MYB binding protein 1a (I3L1L3)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
XGVGRETARPCYSLALAQLLQSFEDLPLCSILQQIQEKYDLHQVKKAMLRPALFANLFGVLALFQSGRLVKDQEALMKSVKLLQALAQYQNHLQEQPRKALVDILSEVSKATLQEILPEVLKADLNIILSSPEQLELFLLAQQKVPSKLKKLVGSVNLFSDENVPRLVNVLKMAASSVKKDRKLPAIALDLLRLALKEDKFPRFWKEVVEQGLLKMQFWPASYLCFRLLGAALPLLTKEQLHLVMQGDVIRHYGEHVCTAKLPKQFKFAPEMDDYVGTFLEGCQDDPERQLAVLVAFSSVTNQGLPVTPTFWRVVRFLSPPALQGYVAWLRAMFLQPDLDSLVDFSTNNQKKAQDSSLHMPERAVFRLRKWIIFRLVSIVDSLHLEMEEALTEQVARFCLFHSFFVTKKPTSQIPETKHPFSFPLENQAREAVSSAFFSLLQTLSTQFKQAPGQTQGGQPWTYHLVQFADLLLNHSHNVTTVTPFTAQQRQAWDRMLQTLKELEAHSAEARAAAFQHLLLLVGIHLLKSPAESCDLLGDIQTCIRKSLGEKPRRSRTKTIDPQEPPWVEVLVEILLALLAQPSHLMRQVARSVFGHICSHLTPRALQLILDVLNPETSEDENDRVVVTDDSDERRLKGAEDKSEEGEDNRSSESEEESEGEESEEEERDGDVDQGFREQLMTVLQAGKALGGEDSENEEELGDEAMMALDQSLASLFAEQKLRIQARRDEKNKLQKEKALRRDFQIRVLDLVEVLVTKQPENALVLELLEPLLSIIRRSLRSSSSKQEQDLLHKTARIFTHHLCRARRYCHDLGERAGALHAQVERLVQQAGRQPDSPTALYHFNASLYLLRVLKGNTAEGCVHETQEKQKAGTDPSHMPTGPQAASCLDLNLVTRVYSTALSSFLTKRNSPLTVPMFLSLFSRHPVLCQSLLPILVQHITGPVRPRHQACLLLQKTLSMREVRSCFEDPEWKQLMGQVLAKVTENLRVLGEAQTKAQHQQALSSLELLNVLFRTCKHEKLTLDLTVLLGVLQGQQQSLQQGAHSTGSSRLHDLYWQAMKTLGVQRPKLEKKDAKEIPSATQSPISKKRKKKGFLPETKKRKKRKSEDGTPAEDGTPAATGGSQPPSMGRKKRNRTKAKVPAQANGTPTTKSPAPGAPTRSPSTPAKSPKLQKKNQKPSQVNGAPGSPTEPAGQKQHQKALPKKGVLGKSPLSALARKKARLSLVIRSPSLLQSGAKKKAQTLRFTISSSKK
Protein: Porin B (Glucose porin) (Outer membrane protein D1) (Q51485)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Substrate-selective channel for a variety of different sugars. Could potentially facilitate the diffusion of diverse compounds, dependent on the presence of a hydroxyl group, but is presumably restricted to carbohydrates. Involved in the transport of glucose, mannitol, fructose and glycerol (sugars able to support the growth of P.aeruginosa). Facilitates glucose diffusion across the outer membrane.
Subcellular location: Cell outer membrane; Multi-pass membrane protein.
Interaction partners:
- Probable ATP-binding component of ABC transporter
- Porin P
- Porin D
- Outer membrane porin F
- Porin O
- Probable permease of ABC sugar transporter
- Anaerobically-induced outer membrane porin OprE
- Probable permease of ABC sugar transporter
- Copper transport outer membrane porin OprC
- Probable sugar-binding periplasmic protein
Sequence:
MYKNKKTRPAARTVGCLFALGALGLGSAAHAAEAFSPNSKWMLGDWGGKRTELLEKGYDFKLEYVGEAAANLDGGYDDDKTGRYTDQFALGVHMDLEKILGWKATEFQFTVTERNGKNLSNDRIGDPRAGHISSVQEVWGRGQTWRLTQLWLKQQYFDGALDVKFGRFGEGEDFNSFPCDFQNLAFCGSQVGNWAGSIWYNWPVSQWALRVKYNFAPDWYVQVGAYEQNPSNLETGNGFKMSGSGTKGALLPVELIWQPKVGAEQLPGEYRLGYYYSTAKADDVYDDVDGQPQGLTGNDFKSRGSKHGWWVVAQQQVTSHNGDASRGLSLFANLTVHDKATNVVDNYQQLGVVYKGPFDARPKDDIGLGIARIHVNDDVKKRQRLVNQVNGIDDYDNPLYQPLQDTEYNAELYYGVHVTDWLTVRPNLQYIKQPGGVDEVDNALVAGIKIQTVF
Protein: F-box/WD-40 repeat-containing protein At5g21040 (Q94AD8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- RING-box protein 1b
- RING-box protein 1a
- Protein AUXIN SIGNALING F-BOX 2
- Protein TRANSPORT INHIBITOR RESPONSE 1
- F12K8.23 protein
- F-box protein AUF2
- Receptor-like protein 48
- Integral membrane HRF1 family protein
- F-box protein At5g52880
- F-box/LRR-repeat protein At1g67190
Sequence:
MEFECQERLEAANDQRSESGLLNTDLRIGNDGSVEIPNVKLCCQKKKGTLVPSGSKQLLSDKDLSTTIIDLPQALISEILNCLDPKELGLVSCVSTYLHRLASEHHAWKEFYRERWGLPVVFGAASSGLSDERSWKDLFVEREFRSRTFLGRYSIDTLYGHTEAVRTVFLLASAKLVFTSGYDSIVRMWDMEEGLSIAASKPLGCTIRALAADTKLLVAGGTDGFIHCWKSLDGLRNLFDLTGFQKEKTEFRLWGHEGPITSLALDMTSIFSGSWDMSVRIWDRSSMKCVKTLRHSDWVWGLAPHETTLASTSGSDVYIWDVSSETPLAIIPDAHEGTTYSLARSHTGDFLFTGGEDGGIKMFEIRRYGSETSVVLISQWMPHTSPVYSLSFEFPWLVSASGDGKLALIDVRKLLKTNRCAYSKRISSSTVEPPQRMLHGFGSNLFSVDVGYDRIVCGGEEGTVRIWNFTQALEIERRTRALKGMRHENRMRRRRMQMEMNAKNGRPDQCSIAAHKNPINGERNRAWHSKRRASGKAKA
Protein: Protein BNI1 (Pointed projection formation protein 3) (Sensitive to high expression protein 5) (Synthetic lethal 39) (P41832)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for the assembly of F-actin structures, such as actin cables and stress fibers. Nucleates actin filaments. Binds to the barbed end of the actin filament and acts as leaky capper, slowing both polymerization and depolymerization. Protects the growing actin fiber from tight capping proteins and so increases the time of elongation and the total amount of F-actin. May organize microtubules by mediating spindle positioning and movement in the budding process. Potential target of the RHO family members.
Subcellular location: Cell membrane. Cell projection, ruffle membrane. Cytoplasm, cytoskeleton.
Interaction partners:
- Bud site selection protein 6
- Cell division control protein 42
- Protein SPA2
- Actin
- Profilin
- Protein PEA2
- GTP-binding protein RHO1
- GTPase-activating protein GYP3
- GTPase-activating protein MSB4
- BNI1-related protein 1
Sequence:
MLKNSGSKHSNSKESHSNSSSGIFQNLKRLANSNATNSNTGSPTYASQQQHSPVGNEVSTSPASSSSFRKLNAPSRSTSTEARPLNKKSTLNTQNLSQYMNGKLSGDVPVSSQHARSHSMQSKYSYSKRNSSQASNKLTRQHTGQSHSASSLLSQGSLTNLSKFTTPDGKIYLEMPSDPYEVEVLFEDIMYKRNIFQSLSEDKQEALMGYSIEKKWLIVKQDLQNELKKMRANTTSSSTASRTSMASDHHPILTANSSLSSPKSVLMTSASSPTSTVYSNSLNHSTTLSSVGTSTSKGKKLVSGSLKKQPSLNNIYRGGAENNTSASTLPGDRTNRPPIHYVQRILADKLTSDEMKDLWVTLRTEQLDWVDAFIDHQGHIAMANVLMNSIYKTAPRENLTKELLEKENSFFKCFRVLSMLSQGLYEFSTHRLMTDTVAEGLFSTKLATRKMATEIFVCMLEKKNKSRFEAVLTSLDKKFRIGQNLHMIQNFKKMPQYFSHLTLESHLKIIQAWLFAVEQTLDGRGKMGSLVGASDEFKNGGGENAILEYCQWTMVFINHLCSCSDNINQRMLLRTKLENCGILRIMNKIKLLDYDKVIDQIELYDNNKLDDFNVKLEANNKAFNVDLHDPLSLLKNLWDICKGTENEKLLVSLVQHLFLSSSKLIEENQNSSKLTKQLKLMDSLVTNVSVASTSDEETNMNMAIQRLYDAMQTDEVARRAILESRALTKKLEEIQAERDSLSEKLSKAEHGLVGQLEDELHERDRILAKNQRVMQQLEAELEELKKKHLLEKHQQEVELRKMLTILNSRPEESFNKNEGTRGMNSSLNSSEKANIQKVLQDGLSRAKKDYKDDSKKFGMTLQPNKRLKMLRMQMENIENEARQLEMTNFAEFEKDRLEPPIHIKKPKVKKMKNKDRKPLVKPQEADVNKLNDLRRALAEIQMESNDISKFNVEERVNELFNEKKSLALKRLKELETKYKGFGIDFNVDEIMDSPKKNTGDVETEEDANYASLDPKTYQKKLDEINRITDQLLDIQTQTEHEIQVEEDGESDLSSSSSDDESEEIYQDASPTQELRSEHSELSSGSGPGSFLDALSQKYGTGQNVTASAAFGENNNGSGIGPLHSKVEKTFMNRLRKSTVSSAPYLEELTQKVNKVEPYEQNEDEGLDKKSLPENSTASAASAFDKAEKDMRQHVENGKQGRVVNHEEDKTADFSAVSKLNNTDGAEDLSTQSSVLSSQPPPPPPPPPPVPAKLFGESLEKEKKSEDDTVKQETTGDSPAPPPPPPPPPPPPMALFGKPKGETPPPPPLPSVLSSSTDGVIPPAPPMMPASQIKSAVTSPLLPQSPSLFEKYPRPHKKLKQLHWEKLDCTDNSIWGTGKAEKFADDLYEKGVLADLEKAFAAREIKSLASKRKEDLQKITFLSRDISQQFGINLHMYSSLSVADLVKKILNCDRDFLQTPSVVEFLSKSEIIEVSVNLARNYAPYSTDWEGVRNLEDAKPPEKDPNDLQRADQIYLQLMVNLESYWGSRMRALTVVTSYEREYNELLAKLRKVDKAVSALQESDNLRNVFNVILAVGNFMNDTSKQAQGFKLSTLQRLTFIKDTTNSMTFLNYVEKIVRLNYPSFNDFLSELEPVLDVVKVSIEQLVNDCKDFSQSIVNVERSVEIGNLSDSSKFHPLDKVLIKTLPVLPEARKKGDLLEDEVKLTIMEFESLMHTYGEDSGDKFAKISFFKKFADFINEYKKAQAQNLAAEEEERLYIKHKKIVEEQQKRAQEKEKQKENSNSPSSEGNEEDEAEDRRAVMDKLLEQLKNAGPAKSDPSSARKRALVRKKYLSEKDNAPQLLNDLDTEEGSILYSPEAMDPTADTVIHAESPTPLATRGVMNTSEDLPSPSKTSALEDQEEISDRARMLLKELRGSDTPVKQNSILDEHLEKLRARKERSIGEASTGNRLSFK
Protein: Glutamate synthase [NADPH] large chain (EC 1.4.1.13) (Glutamate synthase subunit alpha) (GLTS alpha chain) (NADPH-GOGAT) (P09831)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the conversion of L-glutamine and 2-oxoglutarate into two molecules of L-glutamate.
Interaction partners:
- NAD-dependent dihydropyrimidine dehydrogenase subunit PreT
- Putative oxidoreductase UacF
- Putative oxidoreductase AegA
- Glutamate synthase small chain
- NADP-specific glutamate dehydrogenase
- Glutamine synthetase
- Putative oxidoreductase YgfK
- 2,4-dienoyl-CoA reductase [
- Carbamoyl phosphate synthase large chain
- Glutamate decarboxylase beta
Sequence:
MLYDKSLERDNCGFGLIAHIEGEPSHKVVRTAIHALARMQHRGAILADGKTGDGCGLLLQKPDRFFRIVAQERGWRLAKNYAVGMLFLNKDPELAAAARRIVEEELQRETLSIVGWRDVPTNEGVLGEIALSSLPRIEQIFVNAPAGWRPRDMERRLFIARRRIEKRLEADKDFYVCSLSNLVNIYKGLCMPTDLPRFYLDLADLRLESAICLFHQRFSTNTVPRWPLAQPFRYLAHNGEINTITGNRQWARARTYKFQTPLIPDLHDAAPFVNETGSDSSSMDNMLELLLAGGMDIIRAMRLLVPPAWQNNPDMDPELRAFFDFNSMHMEPWDGPAGIVMSDGRFAACNLDRNGLRPARYVITKDKLITCASEVGIWDYQPDEVVEKGRVGPGELMVIDTRSGRILHSAETDDDLKSRHPYKEWMEKNVRRLVPFEDLPDEEVGSRELDDDTLASYQKQFNYSAEELDSVIRVLGENGQEAVGSMGDDTPFAVLSSQPRIIYDYFRQQFAQVTNPPIDPLREAHVMSLATSIGREMNVFCEAEGQAHRLSFKSPILLYSDFKQLTTMKEEHYRADTLDITFDVTKTTLEATVKELCDKAEKMVRSGTVLLVLSDRNIAKDRLPVPAPMAVGAIQTRLVDQSLRCDANIIVETASARDPHHFAVLLGFGATAIYPYLAYETLGRLVDTHAIAKDYRTVMLNYRNGINKGLYKIMSKMGISTIASYRCSKLFEAVGLHDDVVGLCFQGAVSRIGGASFEDFQQDLLNLSKRAWLARKPISQGGLLKYVHGGEYHAYNPDVVRTLQQAVQSGEYSDYQEYAKLVNERPATTLRDLLAITPGENAVNIADVEPASELFKRFDTAAMSIGALSPEAHEALAEAMNSIGGNSNSGEGGEDPARYGTNKVSRIKQVASGRFGVTPAYLVNADVIQIKVAQGAKPGEGGQLPGDKVTPYIAKLRYSVPGVTLISPPPHHDIYSIEDLAQLIFDLKQVNPKAMISVKLVSEPGVGTIATGVAKAYADLITIAGYDGGTGASPLSSVKYAGCPWELGLVETQQALVANGLRHKIRLQVDGGLKTGVDIIKAAILGAESFGFGTGPMVALGCKYLRICHLNNCATGVATQDDKLRKNHYHGLPFKVTNYFEFIARETRELMAQLGVTRLVDLIGRTDLLKELDGFTAKQQKLALSKLLETAEPHPGKALYCTENNPPFDNGLLNAQLLQQAKPFVDERQSKTFWFDIRNTDRSVGASLSGYIAQTHGDQGLAADPIKAYFNGTAGQSFGVWNAGGVELYLTGDANDYVGKGMAGGLIAIRPPVGSAFRSHEASIIGNTCLYGATGGRLYAAGRAGERFGVRNSGAITVVEGIGDNGCEYMTGGIVCILGKTGVNFGAGMTGGFAYVLDESGDFRKRVNPELVEVLSVDALAIHEEHLRGLITEHVQHTGSQRGEEILANWSTFATKFALVKPKSSDVKALLGHRSRSAAELRVQAQ
Protein: Transmembrane protein 158 (40 kDa BINP-binding protein) (p40BBP) (Ras-induced senescence protein 1) (Q6F5E0)
Organism: Mus musculus (Mouse)
Function: Receptor for brain injury-derived neurotrophic peptide (BINP), a synthetic 13-mer peptide.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MLPLLAALLAAACQLPPAHGGATDAPGLAGTPPNASANASFTNEHSTPRLLASAASAPPERSGPEEAPAAPCNISVQRQMLSSLLVRWGRPRGLQCDLLLFSTNAHGRAFFAAAFHRVGPPLLIEHLGLAAGGAQQDLRLCVGCGWVRGRLRAPAGAPTALPAYPAAEPGPLWLQGEPRHFCCLDFSLEELQGEPGWRLNRKPIESTLVACFMTLVIVVWSVAALIWPVPIIAGFLPNGMEQRRTTAGAPAAAPAAVPAGTTAAAAAAAAAAAAAAAAVTSGVAPK
Protein: Mitochondrial import inner membrane translocase subunit Tim10 B (Fracture callus protein 1) (FxC1) (Mitochondrial import inner membrane translocase subunit Tim9 B) (TIMM10B) (Tim10b) (Q9Y5J6)
Organism: Homo sapiens (Human)
Function: Component of the TIM22 complex, a complex that mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. The TIM22 complex forms a twin-pore translocase that uses the membrane potential as the external driving force. In the TIM22 complex, it may act as a docking point for the soluble 70 kDa complex that guides the target proteins in transit through the aqueous mitochondrial intermembrane space.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:11489896, ECO:0000269|PubMed:14726512}; Peripheral membrane protein {ECO:0000269|PubMed:11489896, ECO:0000269|PubMed:14726512}.
Interaction partners:
- Mitochondrial import inner membrane translocase subunit Tim29
- Mitochondrial import inner membrane translocase subunit Tim10
- Acylglycerol kinase, mitochondrial
- Mitochondrial import inner membrane translocase subunit Tim9
- Mitochondrial import inner membrane translocase subunit Tim22
- Mitochondrial import inner membrane translocase subunit Tim8 A
- Mitochondrial import inner membrane translocase subunit Tim8 B
- Mitochondrial import inner membrane translocase subunit Tim13
- Mitochondrial intermembrane space import and assembly protein 40
- Mitochondrial import inner membrane translocase subunit Tim17-A
Sequence:
MERQQQQQQQLRNLRDFLLVYNRMTELCFQRCVPSLHHRALDAEEEACLHSCAGKLIHSNHRLMAAYVQLMPALVQRRIADYEAASAVPGVAAEQPGVSPSGS
Protein: RNA binding protein (O88720)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MWGDSRSANRTGPFRGSQEEGFAPGWNRDYPPPPLKSHARERHSGNFPGRDSLPFDFQGHSGPPFANVEEHSFSYGGRDGPHGDYQGGEGPGHDFRGGDFSSSDFQSRDSAQLDFRNRDIHSGDFRDREGPPMDYRGGDGTHMDYRGRETPHMNYRDRDSHTVDFRSRDVPPTDFRGRGTYDLDFRGREGSHSDFRGRDLSDLDFRSRDQSRSDFRNRDVSDLDFRDKDGTQVDSRGRGSATTDLDFRNRDTPHSDFRGRHRTRTYQDFRGREVGPCMEFKDREMPPMDPKVLDYIQPSPQEREHSGMNMNKREESIHDHAMERPAFGVQKGEFEHSETREGETQSGTFEHESQSDFQNSQSPVQEQDKPKLSGGEQQSSDAGLFKEEGDLDFLGQQDTDYRSIEYCDVDHRLPGNQIFGYGQSKSFSQGKMSRDAQQDLQDQDYRTGPSEEKPNRLIRLSGVPENATKEEILNAFRTSDGIPVKDLQLKEYNTGYDYGYVCVEFSLLEDAIGCMEANQGTLMIHDKEVTLEYVPSPDFWYCKRCKASTGGHQSSCSFCKGPKEEVKQELVSYPQPQKTSIPVPSEKQPNQPRPADKEHELRKRDEGQESRLGHQKRDTDRYFPHSRREGLTFRRDREKEPWSGDSRQDGESKTIMLKRIYRSTPPEVIVEVLEPCVHLTTANVRIIKNRTGPMGHTYGFIDLDSHAEALRVVKILQNLDPPFSIDGKMVAVNLATGKRRNDSGDHSDHMHYYQGKKYFRDRRGGNRNSDWSSDTNRQGQQSSSDCYIYDSTTGYYYDPLAGTYYDPNTQQEVYVPQDPESPDEEEIKEKKSTSQGKSNSKKETSKRDGKEKKDRGMTKFQESTSEGKPPLEDVFKKPLPPTVKKEESPPPPKVVNPLIGLLGEYGGDSDYEEEEEEEQAPPVQPQPQPREEMTKKENEDDKLTDWNKLACLLCRRQFPNKEVLTKHQQLSDLHKQNLEIHRKIKQSEQELAYLERREREGRFKEKGNDRREKLQSFDSPERKRIKYSRETDSDRNPVDKEDTDTSSKGGCAQQATGWRKGAGLGYSHPGLGSSEEIEGRMRGPGGGPPGRTSKRQSNETYRDAVRRVMFARYKELD
Protein: HTH-type transcriptional regulator TnrA (Transcriptional nitrogen regulatory protein A) (TnrA) (Q45666)
Organism: Bacillus subtilis (strain 168)
Function: Transcription regulator that actives the transcription of genes required for nitrogen assimilation such as nrgAB (ammonium transport), nasABCDEF (nitrate/nitrite assimilation), ureABC (urea degradation) and gabP (GABA transport), during nitrogen limitation. Also represses glnRA and gltAB in the absence of ammonium. On the contrary of the MerR members, which require longer DNA sites for high-affinity binding, TnrA requires a DNA sequence of 17 nucleotides as minimal binding site.
Subcellular location: Cell membrane. Note=Under poor nitrogen source such as nitrate, TnrA is associated with the cell membrane via the ammonium uptake proteins AmtB and its cognate regulator GlnK (PubMed:21435182). Without usable nitrogen source, TnrA is released from the membrane to the cytoplasm where it is degraded by proteolysis (PubMed:21435182). The presence of 4 mM ATP leads to concomitant solubilization of GlnK and TnrA (PubMed:17001076). GlnK and Amtb are required for the membrane association of TnrA (PubMed:17001076). {ECO:0000269|PubMed:17001076, ECO:0000269|PubMed:21435182}.
Interaction partners:
- Glutamine synthetase
- Ammonium transporter
- Global transcriptional regulator CodY
- Sensor histidine kinase GlnK
- Catabolite control protein A
- Transcriptional dual regulator GltC
- Stress response protein YkoL
- Uncharacterized protein YkzB
- Purine catabolism regulatory protein
- L-asparaginase 2
Sequence:
MTTEDHSYKDKKVISIGIVSELTGLSVRQIRYYEERKLIYPQRSSRGTRKYSFADVERLMDIANKREDGVQTAEILKDMRKKEQMLKNDPQVRKKMLEGQLNAHFRYKNR
Protein: Candida glabrata strain CBS138 chromosome M complete sequence (Q6FJ68)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- glucan 1,3-beta-glucosidase
- 1,3-beta-glucan synthase
- 1,3-beta-glucan synthase
- glucan 1,3-beta-glucosidase
- 1,3-beta-glucan synthase
- glucan 1,3-beta-glucosidase
Sequence:
MLHLFVVIFLALGVLGYDNSGLTTDELQSLQKRFQDYYNDGEVQVKGITIGGWLVTEPYITPSLYETAFTHVNKTLNGTNSTTFQNSTFGNYSIVDEYTLCKELGYQNALTLLKDHYETFITEDDFAQIKENGFNLVRLPIGYWAWKKNSNDTSRYNYVGNISYDDPYVSEGLQLQYLLKAIDWASKYELNVWIDLHGAPGSQNGFDNSGQRILYDDLGWLHADKTKPLTLAIWKDMFEKFVRTNNYNGYNTSSVVGLEIMNEPLGPKIGMRNIAQSYYEAFDMFKTAEAENNNPQNDNLTFVIHDAFQSIGYWNLHLNPDYRNVSNQYYNLTNVTYNSQSVLVDHHHYEVFTDFQLKNNQYNRIMDIINYGDSISKELDFHPAVVGEWSGAITDCARWVNGIGIGARYDGSYYKTTAFQSDSPPNGTCISQNDISTWSESYKTRVRQFIEAQLATYSAKTTGWIFWNWKTENAAEWDYLKLKENNLFPQPFDNFTYFNKDGQINSSFSTSLSIEAFGSPTSSRVSSTKHKNFAISTKMRTSITGSSNNNTWMYFLSAALGMLAVCCVM
Protein: GATA-factor (C8VHD4)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Uncharacterized protein
- Uncharacterized protein
- Developmental and secondary metabolism regulator veA
- Velvet complex subunit B
- Protein-methionine methyltransferase laeA
Sequence:
MANRDINDFGGFDDRQLPAIRSPDYIESNEESHIAHMATYTSSVPVGDYAYTMHNSMLAYDTANEGNSVSVSLGSESAFAYDVSTYPSSTTALNYDLNQFASLHSHAPGSDNASTYSSAQRHYWTQPHTSGGMVSSTQTLLSHPAQPSRAAEPSAAQKIPPGQLQDINPFPQASVSATSHRPIQPKSLAGKGARSEASRSSTPYPNVYSRSGYDMMGILAEVVSRDNPRIDLGPVDLSCAFVLCDLTMEDSPIVYVSHAFERLTGYNEKEIVGRNCRFLQSPDAKVEKGEPRKFVDSHTVSRLRSAVDRRSEIQVSIINYRKGGQPFLNLVTMIPVRWNAKDYYVGFQVDLVERPEAVTRRNSDGTYMIDYHRSQLPAYVVPAADMYRDGHVPTAMLSPRQVSVILNDFVKGQSSVAVNLFHHMLVENTDDLIFVLSFEGEFLYLSPSCQTVLEYKPNDLCGKTLSAICHPSDIGPVTRDMRTCTTGDPISILYRIRRKESGYTWFENHGGWHITQRGRQFMVLVGRLIPMYSPIQLANVESGGLAENDIWAKLSLSGIILFMSSKSRAVLGQPSDDLIGKRLQDFLVTDNFHSEPAVQQALETSRHNQQATFTHRIRHRKGHIISAQITLYPGDIVYGASKPAFLIAHLRFPRELQLQASTTEDQSNSQSQSQTSSDTGPGDYKTPQNQQQTAESHQKPHPNFPQPPTSSATLAVPSSASPNSAEPPTELGMHLFEELNPTRGSNWHFELRELEKQNRHLTDEAQRLLARRRKRKRKQSAAAMEKSCAMCGTRTTPEWRRGPSGNRDLCNSCGLRWAKQVRSAAAVHSQAKSGGEG
Protein: RNA polymerase II subunit A C-terminal domain phosphatase (EC 3.1.3.16) (TFIIF-associating CTD phosphatase) (Q9Y5B0)
Organism: Homo sapiens (Human)
Function: Processively dephosphorylates 'Ser-2' and 'Ser-5' of the heptad repeats YSPTSPS in the C-terminal domain of the largest RNA polymerase II subunit. This promotes the activity of RNA polymerase II. Plays a role in the exit from mitosis by dephosphorylating crucial mitotic substrates (USP44, CDC20 and WEE1) that are required for M-phase-promoting factor (MPF)/CDK1 inactivation.
Subcellular location: Nucleus {ECO:0000269|PubMed:22692537}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:22692537}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:22692537}. Midbody {ECO:0000269|PubMed:22692537}. Note=Found at centrosomes in prometaphase, at spindle and spindle poles in metaphase and at spindle midzone and midbody in anaphase and telophase-G1 respectively.
Interaction partners:
- General transcription factor IIF subunit 1
- DNA-directed RNA polymerase II subunit RPB1
- General transcription factor IIF subunit 2
- DNA-directed RNA polymerase II subunit RPB7
- DNA-directed RNA polymerase II subunit RPB3
- Transcription initiation factor IIB
- DNA-directed RNA polymerase II subunit RPB2
- DNA-directed RNA polymerase II subunit RPB4
- Transcription elongation factor A protein 1
- Cyclin-dependent kinase 9
Sequence:
MEVPAAGRVPAEGAPTAAVAEVRCPGPAPLRLLEWRVAAGAAVRIGSVLAVFEAAASAQSSGASQSRVASGGCVRPARPERRLRSERAGVVRELCAQPGQVVAPGAVLVRLEGCSHPVVMKGLCAECGQDLTQLQSKNGKQQVPLSTATVSMVHSVPELMVSSEQAEQLGREDQQRLHRNRKLVLMVDLDQTLIHTTEQHCQQMSNKGIFHFQLGRGEPMLHTRLRPHCKDFLEKIAKLYELHVFTFGSRLYAHTIAGFLDPEKKLFSHRILSRDECIDPFSKTGNLRNLFPCGDSMVCIIDDREDVWKFAPNLITVKKYVYFQGTGDMNAPPGSRESQTRKKVNHSRGTEVSEPSPPVRDPEGVTQAPGVEPSNGLEKPARELNGSEAATPRDSPRPGKPDERDIWPPAQAPTSSQELAGAPEPQGSCAQGGRVAPGQRPAQGATGTDLDFDLSSDSESSSESEGTKSSSSASDGESEGKRGRQKPKAAPEGAGALAQGSSLEPGRPAAPSLPGEAEPGAHAPDKEPELGGQEEGERDGLCGLGNGCADRKEAETESQNSELSGVTAGESLDQSMEEEEEEDTDEDDHLIYLEEILVRVHTDYYAKYDRYLNKEIEEAPDIRKIVPELKSKVLADVAIIFSGLHPTNFPIEKTREHYHATALGAKILTRLVLSPDAPDRATHLIAARAGTEKVLQAQECGHLHVVNPDWLWSCLERWDKVEEQLFPLRDDHTKAQRENSPAAFPDREGVPPTALFHPMPVLPKAQPGPEVRIYDSNTGKLIRTGARGPPAPSSSLPIRQEPSSFRAVPPPQPQMFGEELPDAQDGEQPGPSRRKRQPSMSETMPLYTLCKEDLESMDKEVDDILGEGSDDSDSEKRRPEEQEEEPQPRKPGTRRERTLGAPASSERSAAGGRGPRGHKRKLNEEDAASESSRESSNEDEGSSSEADEMAKALEAELNDLM