wanglab/gogpt-training-data huggingface dataset:
Protein: Odorant receptor 2a (O46077)
Organism: Drosophila melanogaster (Fruit fly)
Function: Odorant receptor which mediates acceptance or avoidance behavior, depending on its substrates. The odorant receptor repertoire encodes a large collection of odor stimuli that vary widely in identity, intensity, and duration. May form a complex with Orco to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MEKQEDFKLNTHSAVYYHWRVWELTGLMRPPGVSSLLYVVYSITVNLVVTVLFPLSLLARLLFTTNMAGLCENLTITITDIVANLKFANVYMVRKQLHEIRSLLRLMDARARLVGDPEEISALRKEVNIAQGTFRTFASIFVFGTTLSCVRVVVRPDRELLYPAWFGVDWMHSTRNYVLINIYQLFGLIVQAIQNCASDSYPPAFLCLLTGHMRALELRVRRIGCRTEKSNKGQTYEAWREEVYQELIECIRDLARVHRLREIIQRVLSVPCMAQFVCSAAVQCTVAMHFLYVADDHDHTAMIISIVFFSAVTLEVFVICYFGDRMRTQSEALCDAFYDCNWIEQLPKFKRELLFTLARTQRPSLIYAGNYIALSLETFEQVMRFTYSVFTLLLRAK
Protein: Aminopeptidase NAALADL1 (EC 3.4.11.-) (100 kDa ileum brush border membrane protein) (I100) (Ileal dipeptidylpeptidase) (N-acetylated-alpha-linked acidic dipeptidase-like protein) (NAALADase L) (O54697)
Organism: Rattus norvegicus (Rat)
Function: Aminopeptidase with broad substrate specificity. Has lower activity with substrates that have Asp or Glu in the P2' position, or Pro in the P3' position. Lacks activity with substrates that have both Pro in the P3' position and Asp or Glu in the P2' position. Lacks carboxypeptidase activity. Lacks dipeptidyl-peptidase IV type activity.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:9388249}; Single-pass type II membrane protein {ECO:0000305|PubMed:9388249}. Note=Ileal brush border membrane. {ECO:0000269|PubMed:9388249}.
Interaction partners:
Sequence:
MHWAKILGVGIGAAALLGLGIILGHFAIPKATEPLASSVSDSQDLDLAILDSVMGQLDASRIRENLRELSKEPHVATSARDEALVQLLLGRWKDSASGLDTAKTYEYTVLLSFPSTEQPNSVEVVGPNGTVFHSFQPFEKNLTGEQAEPNVLQPYAAYAPPGTPKGPLVYANRGSEDDFKKLEAEGINLKGTIALTRYGSVGRGAKAINAARHGVVGVLVYTDPGDINDGKSLPNETFPNSWGLPPSGVERGSYYEYFGDPLTPYLPAHPVSFRLDPHNISGFPPIPTQPIGFEDAKNLLCNLNGTSAPDSWQGALGCEYKLGPGFEPNGNFPAGSEVKVSVYNRLELRNSSNVLGIIQGAVEPDRYVIYGNHRDSWVHGAVDPSSGTAVLLEISRVLGTLLKKGTWRPRRSIIFASWGAEEFGLIGSTEFTEEFLSKLQERTVTYINVDISVFSNATLRAQGTPPVQSVIFSATKEISAPGSSGLSIYDNWIRYTNRSSPVYGLVPSMGTLGAGSDYASFIHFLGITSMDLAYTYDRSKTSARIYPTYHTAFDTFDYVEKFLDPGFSSHQAVARTAGSVLLRLSDSLFLPLNVSDYSETLQSFLQAAQENLGALLESHNISLGPLVTAVEKFKAAAAALNQHILTLQKSSPDPLQVRMVNDQLMLLERAFLNPRAFPEERYYSHVLWAPNTASVATFPGLANAYARAQEINSGAEAWAEVERQLSIAVMALEGAAATLQPVTDL
Protein: 2-oxoacid:ferredoxin oxidoreductase 2, subunit alpha (OFOR2) (EC 1.2.7.11) (Q96XT2)
Organism: Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7) (Sulfolobus tokodaii)
Function: Catalyzes the coenzyme A-dependent oxidative decarboxylation of different 2-oxoacids such as 2-oxoglutarate, pyruvate and 2-oxobutyrate to form their CoA derivatives.
Interaction partners:
- 2-oxoacid:ferredoxin oxidoreductase 2, subunit beta
- 2-oxoacid:ferredoxin oxidoreductase 1, subunit beta
- 2-oxoacid oxidoreductase
- 2-oxoacid oxidoreductase
- ADP-forming acetyl-CoA synthetase
- Succinyl-CoA synthetase beta subunit
- Succinate--CoA ligase subunit alpha
- Succinate-semialdehyde dehydrogenase
- Pyruvate kinase
- isocitrate dehydrogenase
Sequence:
MTRIVWMIGGAQGLGVDTSANIFGNAVAKAGYYLFGNREYYSNIKGRHSYFEVVISEKPIRSLSSYVNILASFDAETVFQHFTETKEYLIYNVEYENTTVDLVKSMEPEMAEQVKEALSKERLGFTIKDVLEYLKRRGVKVIGFNYTELIKKIADTFKVPMSVVERAKNMIAVGASYGLLGLKFDYLKDAISSTFKNELFIKFNTMAAELGYNSVPNVYKLQEYKIEKQRIQVDGNTISAMGKLAGGLRFQSYYPITPASDESVYIEANQNLDMIVEGNELRKGGVVVVQAEDELAAINMAVGAALTGVRSATATSGPGFSLMSEGISWAGMNEVPVVITYYMRGAPATGLPTRSGQADLKFALNVGHGEFPRIVIASGDHVEIFWDAIWALNLAEKYQTPVIHIIEKTLANAYSVFEEELITNRPYVIERGKIVKPTSDYFNRFEVTEDGISPRVFLGQASIFYTGDEHNEEGHITENSINRMKMYEKRNKKLETADKEIPEEQRVNIVGDADIVLLTWGSPKGAILDAMEELSKDGIKTMMVQVKMFNPYPKNLMKKILSGKSKIIAVENNYNAQGAEVLAEKTGIFATNYILKWTGRPITREEVIEGIKKILERDEKRVVLYGGA
Protein: D-3-phosphoglycerate dehydrogenase 3, chloroplastic (EC 1.1.1.95) (Q9LT69)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the plastidial phosphorylated pathway of serine biosynthesis (PPSB).
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:24058165, ECO:0000269|PubMed:24368794}.
Interaction partners:
- Phosphoserine aminotransferase 1, chloroplastic
- Phosphoserine aminotransferase 2, chloroplastic
- D-glycerate 3-kinase, chloroplastic
- Serine--glyoxylate aminotransferase
- Phosphoserine phosphatase, chloroplastic
- 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase 2
- Phosphoglycerate mutase-like protein 4
- 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase 1
- 2,3-bisphosphoglycerate-independent phosphoglycerate mutase 1
- Probable 2,3-bisphosphoglycerate-independent phosphoglycerate mutase 2
Sequence:
MATSLNLSSIFSSSSRLVTTPSSVFPIRQRRRIILVTSSSSGGGGKPTILVTEKLGQAGIDLLKKYANVDCSYDLSLEELCTKISLCDALIVRSGTKVGRDVFESSRGRLKVVGRAGVGIDNVDLAAATEYGCLVVNAPTANTVAAAEHGIALLTAMARNIAQADASIKAGKWTRNKYVGVSLVGKTLAVLGFGKVGSEVARRARGLGMHVITHDPYAPADRARAIGVELVSFEVAISTADFISLHLPLTAATSKMMNDVTFAMMKKGVRIVNVARGGVIDEEALLRALDSGIVAQAALDVFTVEPPVKDNKLVLHESVTATPHLGASTMEAQEGVSIEVAEAVIGALRGELAATAVNAPMVPLEVLRELKPYVVLAEKLGRLAVQLVTGGSGVNAVKVTYASSRAPDDLDTRLLRAMVIKGIIEPISSVFINLVNSDYIAKQRGVKISEERMVLDGSPENPIEYITVRIANVESRFASALSESGEIKVEGRVKQGVPSLTKVGLFGVDVSLEGSVILCRQVDQPGMIGKVASILGDENVNVSFMSVGRIAPGKQAVMAIGVDEQPSKETLKKIGDIPAIEEFVFLKL
Protein: Protein E7 (Q8B5B5)
Organism: Human papillomavirus type 92
Subcellular location: Host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04004}. Host nucleus {ECO:0000256|HAMAP-Rule:MF_04004}. Note=Predominantly found in the host nucleus. {ECO:0000256|HAMAP-Rule:MF_04004}.
Interaction partners:
Sequence:
MIGKQATIPDIVLDLQDLVQPIDLHCDEDLSENQEEEPAPQRIDYKIVSSCGGCGIKLRIFASCTQFGIRTLQDLLLEEIALLCPDCKNGR
Protein: Protein canopy homolog 4 (Q8N129)
Organism: Homo sapiens (Human)
Function: Plays a role in the regulation of the cell surface expression of TLR4.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Lymphocyte antigen 96
- Toll-like receptor 4
Sequence:
MGPVRLGILLFLFLAVHEAWAGMLKEEDDDTERLPSKCEVCKLLSTELQAELSRTGRSREVLELGQVLDTGKRKRHVPYSVSETRLEEALENLCERILDYSVHAERKGSLRYAKGQSQTMATLKGLVQKGVKVDLGIPLELWDEPSVEVTYLKKQCETMLEEFEDIVGDWYFHHQEQPLQNFLCEGHVLPAAETACLQETWTGKEITDGEEKTEGEEEQEEEEEEEEEEGGDKMTKTGSHPKLDREDL
Protein: Uncharacterized protein (Q580H3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- T. brucei spp.-specific protein
- Uncharacterized protein
- Uncharacterized protein
Sequence:
MAMQLFTFGHPCEHQLRRQCIGGKSCPLCGYPNEWCCSYIKGKINFKRDKPCEGSRCRWNYQHPPQSLFDAVTQVLNESRPIALKIDEGDDKEILALSIDNHHIVDTVQCALQMLRNPPSTYSARVGQLLAYAALRARDTKVFMQLLKTMKKPVDGYILGAYDYLMRGTIPAPLNSSSNTVGGNANNNSVNSGNNNSAGSNQGRAAAKKAGTGSNGNNSSNNNNNDKKEDIADELKSDMVDLMNAALSSGGQLVDREDQHTLQAVFIQSLRSYPKSNKKRQEMLESAVAMFGSKPGPRSTTAAVTAVEQTPPNNISGNSNSPPTTAAVVTNATNNNNNNNNNSAASRAGSVAAATGGAVPGARTVARVVEAAQDENVSVPQRSGSFSNTNNSSGNSGNASYVNVCSAGAGATTAAAVVAAAVAAAGAPSRRPQGTTGSTTPVTPVSTRSKEPCVPTTTIAPTTTVQPTRQQQQQQQQQRPPPPIVGISQLVQQPRQPAACRYEPIRTDLPLPNITLFGGLFGLTTQSAAWAPLGAATSRKTSPPSLPGVVVGSGAATPGLAADMDEKAFRFLSPTTSGVNFFGGIDSLPPEHQLLKGICDD
Protein: Calcium-transporting ATPase (EC 7.2.2.10) (Q86C61)
Organism: Trypanosoma brucei
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361146}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361146}.
Interaction partners:
Sequence:
MHPLESPQEHKTQVSPENNGNETKSVLQKLFTCNEDPKPLYEELGGVEGIAERLGTSITDGIDSFSVENRRAVYGRNELPEEAPLTFWKILKAAWSDRMIILLTLAACVSLILGLTVPEPGHEKVDYKTGWIEGTAILMAVIAVTSASSIQDYRKELKFRALVEENSAQPISVIRDGHKVTVDVTEIVVGDLVSLSPGLVIPVDGLYVRGLSVVVDESSVTGENDLKKKGAEHPILLSGTVVSTAEDAYILACAVGESSFGGKLLMESRLDGEPRATPLQERLDELAAFIGRVAIISAVLLFIVLCIIEIERIATNKQQFYPKKFLNFLLLCVTIVVVAVPEGLPLAVTIALAYSQNQMQKDNNQVRRLCACETMGNATQICSDKTGTLTQNRMTVVQGYIGMRRFRVSNPGDPSSTVNLEGVSSDAQSLLMLGLALNSSSEKELLPGNVGAESDLLSRWTWRTDKGNKTDQAILDFVDRVLISVPGSCNDKELPHQKLRMTNRSRGFAIFPFTSERKFMTAVVAGADGVVMQYVKGGSDRVLGMCNRYLSSEGREEPLTEEVTEMITEQIRSIAGDANRTIGVAYGRIGTDGAVPEEEPEGPFVWLALLGIQDPLRPEVVDAVRMCQRAGVTVRMCTGDNLDTAVAISRQCGIYNRLRGDLALTGKDFRNLVYDTYGDEANMEKFWPVLDRMMVMGRSQPLDKQLLVLMLMLRGEVVAVTGDGTNDAPALRLANVGFVMRSGTDIAVKSGDIVLLDDNFRSVQRAVVWGRTVNDNIRKFLQLQLTVNVVSFLVTVVGTLVREGKSSPLTTVQLLWVNLLMDTLAALALATEQPTEDCLNRGPSSPRAPLVSRRMWFTIFSVATVQLTAFFSVLTFGGKYFGEDENGKHLHRTFLFNVFVFGTIFHMLNCRKLYRELNVFEGMGRSVFFIVVVGSCIAFQVLAICTFNDFMGVRPLSIKQWGVSIGIAAISLVVGILSRVVSIREPVFALIPDSRNVDGSASRLIKDVSVAAEQRQRETDGTSDASSLLAGRLRAQSRWRRLQAEHVKKPRVVNAFRRAWTDRDMKRGSTRQLYDTLRMV
Protein: Transcription factor E4F1 (EC 2.3.2.27) (E4F transcription factor 1) (Putative E3 ubiquitin-protein ligase E4F1) (RING-type E3 ubiquitin transferase E4F1) (Transcription factor E4F) (Transcription factor phi AP3) (p120E4F) (Q8CCE9)
Organism: Mus musculus (Mouse)
Function: May function as a transcriptional repressor. May also function as a ubiquitin ligase mediating ubiquitination of chromatin-associated TP53. Functions in cell survival and proliferation through control of the cell cycle. Functions in the p53 and pRB tumor suppressor pathways and regulates the cyclin CCNA2 transcription.
Subcellular location: Nucleus, nucleoplasm {ECO:0000269|PubMed:15226446, ECO:0000269|PubMed:8262041}. Cytoplasm {ECO:0000250}. Note=A small fraction is detected in the cytoplasm (By similarity). Excluded from the nucleolus where it is targeted upon CDKN2A overexpression. Localizes to the mitotic spindle during embryogenesis. {ECO:0000250}.
Interaction partners:
- Cellular tumor antigen p53
- Ankyrin repeat and SAM domain-containing protein 3
- Ras association domain-containing protein 1
Sequence:
MEGAMAVRVTAAHTAEARAEAGREAGEGGVAAAAALSSGGFLGLPAPFSEEDEDDVHRCGRCQVEFTALEDFVQHKIQKTCHRAPQEALPTTPAATALLDQEVVPTAAEGGPDEPITVAHIVVEATSLAEDISHAPDLVGSGHIKEVIVAAEAEPGDVEMAEAPGSPNHQELGLLGEGEQAHVKLLVNKEGRYVCMLCHKTFKTGSILKAHMVTHSSRKDHECKLCGASFRTKGSLIRHHRRHTDERPYKCAKCGKSFRESGALTRHLKSLTPCTEKIRFSISKDTAVGKEEVPAGSSASTVGTVTSSVAGDPMETSPVIHLVTDAKGTVIHEVHVQMQELPLGMKALTPESPDSEELPCSSENSRENLLHQAMQNSGIVLERVAGEESALEPAPPSGSSPQCLGDGSPELPLLKVEQIETQVASEAATVPRTHPCPQCSETFPTAATLEAHKRGHIAPRPFTCTQCGKAFPKAYLLKKHQEVHVHERRFRCGDCGKLYKTIAHVRGHRRVHSDERPFPCPQCGKRYKTKNAQQVHFRTHLEEKPHVCQFCSRGFREKGSLVRHVRHHTGEKPFKCYKCGRGFAEHGTLNRHLRTKGGCLLEVEELLVSEESPSAAATVLAEDPHTVLVEFSSVVADTQEYIIEATADDTETSEATEIIEGTQTEVDSHIMKVVQQIVHQAGAGHQIIVQNVTMDQETALGSEATAADTITIATPESLTEQVAMTLASAISEGTVLTARAGPNSTEQATVTMVSSEDIEILEHGGELVIASPEGQLEVQTVIV
Protein: Redox-sensitive transcriptional activator SoxR (P0ACS2)
Organism: Escherichia coli (strain K12)
Function: Activates the transcription of the soxS gene which itself controls the superoxide response regulon. SoxR contains a 2Fe-2S iron-sulfur cluster that may act as a redox sensor system that recognizes superoxide. The variable redox state of the Fe-S cluster is employed in vivo to modulate the transcriptional activity of SoxR in response to specific types of oxidative stress. Upon reduction of 2Fe-2S cluster, SoxR reversibly loses its transcriptional activity, but retains its DNA binding affinity.
Interaction partners:
- Regulatory protein SoxS
- HTH-type transcriptional regulator AcrR
- Multiple antibiotic resistance protein MarR
- DNA-binding transcriptional dual regulator OxyR
- Superoxide dismutase
- Multiple antibiotic resistance protein MarA
- Catalase-peroxidase
- Anaerobic nitric oxide reductase transcription regulator NorR
- HTH-type transcriptional regulator IscR
- HTH-type transcriptional repressor NsrR
Sequence:
MEKKLPRIKALLTPGEVAKRSGVAVSALHFYESKGLITSIRNSGNQRRYKRDVLRYVAIIKIAQRIGIPLATIGEAFGVLPEGHTLSAKEWKQLSSQWREELDRRIHTLVALRDELDGCIGCGCLSRSDCPLRNPGDRLGEEGTGARLLEDEQN
Protein: Sulfotransferase 2B1 (EC 2.8.2.2) (Alcohol sulfotransferase) (Hydroxysteroid sulfotransferase 2) (Sulfotransferase family cytosolic 2B member 1) (ST2B1) (O35400)
Organism: Mus musculus (Mouse)
Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation. Preferentially sulfonates cholesterol. Catalyzes sulfation of the 3beta-hydroxyl groups of steroids, such as, pregnenolone and dehydroepiandrosterone (DHEA). Cholesterol sulfation is approximately 10-fold higher than for pregnenolone and 20-fold higher than for DHEA. Plays a role in epidermal cholesterol metabolism and in the regulation of epidermal proliferation and differentiation (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:O00204}. Microsome {ECO:0000250|UniProtKB:O00204}. Nucleus {ECO:0000250|UniProtKB:O00204}.
Interaction partners:
- Cytochrome P450 7B1
- Steroid 17-alpha-hydroxylase/17,20 lyase
- Cytochrome P450 7A1
- Cholesterol side-chain cleavage enzyme, mitochondrial
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1
- Cytochrome P450 2E1
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 3
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 6
- Steroid 21-hydroxylase
Sequence:
MDGPQPRALWSSSEKNVSEMSWNFGGEYFRYKGIPFPVGMYSPESLSLAENTSNVRDDDIFIVTYPKSGTNWMIEIVCLILKDGDPSWIRSEPIWQRAPWCETIISAFNVLDRPSPRIMSSHLPIELFTKAFFSSKAKVIYVGRNPRDVVVSLYYYSKIAGQLKDPGTPDQFLQNFLKGEVQFGSWFDHIKGWIRMQNQENFLFITYEELQQDLRGSVQRICEFLGRPLGEEALSSVVAHSAFAAMKANTMSNYSLLPASLLDHRQGEFLRKGISGDWKNHFTVAQSEAFDSVYREQMHGVQRFPWDTSEEDSSPDGQPDPEPSPSPASDDPNPGSSQ
Protein: Non-selective voltage-gated ion channel VDAC2 (VDAC-2) (mVDAC2) (Outer mitochondrial membrane protein porin 2) (Voltage-dependent anion-selective channel protein 6) (VDAC-6) (mVDAC6) (Q60930)
Organism: Mus musculus (Mouse)
Function: Forms a channel through the mitochondrial outer membrane that allows diffusion of small hydrophilic molecules (By similarity). The channel adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV (By similarity). The open state has a weak anion selectivity whereas the closed state is cation-selective (By similarity). Binds various lipids, including the sphingolipid ceramide, the phospholipid phosphatidylcholine, and the sterol cholesterol (By similarity). Binding of ceramide promotes the Binding of ceramide promotes the mitochondrial outer membrane permeabilization (MOMP) apoptotic pathway (By similarity).
Subcellular location: Mitochondrion outer membrane {ECO:0000305|PubMed:22561200}. Membrane {ECO:0000250|UniProtKB:P45880}. Note=May localize to non-mitochondrial membranes. {ECO:0000250|UniProtKB:P45880}.
Interaction partners:
- Cytochrome c, somatic
- Cytochrome c, testis-specific
- Non-selective voltage-gated ion channel VDAC1
- Non-selective voltage-gated ion channel VDAC3
- ADP/ATP translocase 2
- Steroidogenic acute regulatory protein, mitochondrial
- Peptidyl-prolyl cis-trans isomerase F, mitochondrial
- ADP/ATP translocase 1
- Hexokinase-1
- Translocator protein
Sequence:
MAECCVPVCPRPMCIPPPYADLGKAARDIFNKGFGFGLVKLDVKTKSCSGVEFSTSGSSNTDTGKVSGTLETKYKWCEYGLTFTEKWNTDNTLGTEIAIEDQICQGLKLTFDTTFSPNTGKKSGKIKSAYKRECINLGCDVDFDFAGPAIHGSAVFGYEGWLAGYQMTFDSAKSKLTRSNFAVGYRTGDFQLHTNVNNGTEFGGSIYQKVCEDFDTSVNLAWTSGTNCTRFGIAAKYQLDPTASISAKVNNSSLIGVGYTQTLRPGVKLTLSALVDGKSFNAGGHKLGLALELEA
Protein: Zinc finger protein 397 (Zinc finger and SCAN domain-containing protein 15) (Zinc finger protein 47) (Q8NF99)
Organism: Homo sapiens (Human)
Function: Isoform 3 acts as a DNA-dependent transcriptional repressor.
Subcellular location: [Isoform 1]: Nucleus.; SUBCELLULAR LOCATION: [Isoform 3]: Nucleus. Cytoplasm.
Interaction partners:
- Zinc finger protein 446
- Zinc finger and SCAN domain-containing protein 30
- Zinc finger protein with KRAB and SCAN domains 4
- Zinc finger protein with KRAB and SCAN domains 3
- SCAN domain-containing protein 1
- Zinc finger protein 213
- Zinc finger protein 24
- Zinc finger and SCAN domain-containing protein 32
- Zinc finger protein 197
- Zinc finger protein 394
Sequence:
MAVESGVISTLIPQDPPEQELILVKVEDNFSWDEKFKQNGSTQSCQELFRQQFRKFCYQETPGPREALSRLQELCYQWLMPELHTKEQILELLVLEQFLSILPEELQIWVQQHNPESGEEAVTLLEDLEREFDDPGQQVPASPQGPAVPWKDLTCLRASQESTDIHLQPLKTQLKSWKPCLSPKSDCENSETATKEGISEEKSQGLPQEPSFRGISEHESNLVWKQGSATGEKLRSPSQGGSFSQVIFTNKSLGKRDLYDEAERCLILTTDSIMCQKVPPEERPYRCDVCGHSFKQHSSLTQHQRIHTGEKPYKCNQCGKAFSLRSYLIIHQRIHSGEKAYECSECGKAFNQSSALIRHRKIHTGEKACKCNECGKAFSQSSYLIIHQRIHTGEKPYECNECGKTFSQSSKLIRHQRIHTGERPYECNECGKAFRQSSELITHQRIHSGEKPYECSECGKAFSLSSNLIRHQRIHSGEEPYQCNECGKTFKRSSALVQHQRIHSGDEAYICNECGKAFRHRSVLMRHQRVHTIK
Protein: Ral guanine nucleotide dissociation stimulator-like, isoform E (M9PCE9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Ras-related protein Ral-a
- Ras-like protein 1
- Ras-related protein Rap1
- RNA-binding protein Unr
- small monomeric GTPase
- Canoe, isoform E
Sequence:
MNFTSRANCKCPHSQKHQQKPALIKSHTCAYQLQDLTGYNRALMPPLDNTDFSNAWRQVNNNTTSQSCAYHQQRQQQQQQQDAKDSKRHYHHHTCPRQRKKSMTPVEPTHLCQKHQEAKQRRSRSASAKPRRNSSYHSYDDLDVSSAVLNAERKVVASLKYLCACTGATLRNLSKKTKDLHAKNYTYTKPTWRLWGEEHEKNAIFTVYLKKVRYHRPTPTASNDSDDEISHLEWETVRVRFVKAATLARLVEALATDDGELESTFINVFLSTYRTFSTPKQVLSLLTQRYDALHEKHLEELEQAQQNGQVMDPAYDPHASIHEQHKKTLVSALHVWLDGFPEDWHEDNLQQILAFATKRLKRSDLHIKVLNRLERLIKQSLYGNGGGSGGSENNGHSWLSAARSQQMQQFMIPTHYGSSYDLTDQFNGMYLSPMGHGPIYRGPTHFLQAFRFPHVPVRHFAEQLTRMDTELFKRLIPHQCLGHTWARRDSGGSETVVATINQFNAVLFRVVSSILIDRLKPQERALNISRWIDIAQELRMLKNFSSLKAIISALNSNSIYRLSKIWEVLPKERMEVFTELANICSEDNNAWTLREVLKREGTAKNPDPGSDHSDRHLQKLILNLGTQTSHGTIPYLGTFLTDLTMIHTANPDYLTENKLINFDKKRKEFEVLAQIKLLQGAANTYNLQADALFDHWFNSMPVFDEREAFELSCRLEPPPPAPRKSVVSTNTSLTNTTASSTASIMGHRKTDSIHSNSSSGAGSQFYCELNSSTSSRHNSLDRDVHHQHASLMSASSSVSNLSLDSSNSGGRQSGKLTHSQSMGNGLKSHGNGTTNGGSPHINAQLVQPSSGTPHSAPDFYIIRVTYETDNIELDGIVLYKSIMLGNNERTPQVIRNAMLKLGLEDDPDRFTLAQVLPDKELVMPKNANVYYAVNTNYNLNFILRPRKEEGVAGSXSTAVPLSQLWCLGYEGEE
Protein: Bromodomain PHD finger transcription factor (A2A653)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
VGPYGIRSEYCIRKIICPIGVPEAPKETPTPQRKGLRSSALRPKRPETPKQTGPVIIESWVAEEELELWEIRAFAERVEKEKAQAAEQQTKKRLEQQKPAVIAASTTSPANNTSSTVSPAQKVMVAPLSGSVTPGTKMVLATKVGSPATVTFQQNKNFHQTFATWVKQGQSNSATSTAATSATTIASTGQTFQITGSPVTMAGKVITKLPLPANSKIVAVNVPATQGGMVQVQQKVLGIIPSTTGPSQQTFTSFQPRTATVTIRPNTSASAGTTTTSQVITGPQIRPGM
Protein: Cytoplasmic dynein 2 intermediate chain 1 (Dynein 2 intermediate chain 1) (WD repeat-containing protein 60) (Q8WVS4)
Organism: Homo sapiens (Human)
Function: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 2 complex (dynein-2 complex), a motor protein complex that drives the movement of cargos along microtubules within cilia and flagella in concert with the intraflagellar transport (IFT) system. DYNC2I1 plays a major role in retrograde ciliary protein trafficking in cilia and flagella. Requires also to maintain a functional transition zone.
Subcellular location: Cell projection, cilium {ECO:0000269|PubMed:23910462}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:25205765}. Note=Located at the base of the primary cilium in serum-starved fibroblasts. {ECO:0000269|PubMed:23910462}.
Interaction partners:
- Cytoplasmic dynein 2 light intermediate chain 1
- Cytoplasmic dynein 2 intermediate chain 2
- Cytoplasmic dynein 2 heavy chain 1
- Dynein light chain 1, cytoplasmic
- Dynein light chain roadblock-type 1
- Dynein light chain Tctex-type protein 2B
- Dynein light chain Tctex-type 1
- Dynein light chain Tctex-type 3
- Dynein light chain roadblock-type 2
- Cytoplasmic dynein 1 light intermediate chain 1
Sequence:
MEPGKRRTKDDTWKADDLRKHLWAIQSGGSKEERKHREKKLRKESEMDLPEHKEPRCRDPDQDARSRDRVAEVHTAKESPRGERDRDRQRERRRDAKDREKEKLKEKHREAEKSHSRGKDREKEKDRRARKEELRQTVAHHNLLGQETRDRQLLERAERKGRSVSKVRSEEKDEDSERGDEDRERRYRERKLQYGDSKDNPLKYWLYKEEGERRHRKPREPDRDNKHREKSSTREKREKYSKEKSNSFSDKGEERHKEKRHKEGFHFDDERHQSNVDRKEKSAKDEPRKRESQNGEHRNRGASSKRDGTSSQHAENLVRNHGKDKDSRRKHGHEEGSSVWWKLDQRPGGEETVEIEKEETDLENARADAYTASCEDDFEDYEDDFEVCDGDDDESSNEPESREKLEELPLAQKKEIQEIQRAINAENERIGELSLKLFQKRGRTEFEKEPRTDTNSSPSRASVCGIFVDFASASHRQKSRTQALKQKMRSTKLLRLIDLDFSFTFSLLDLPPVNEYDMYIRNFGKKNTKQAYVQCNEDNVERDIQTEEIETREVWTQHPGESTVVSGGSEQRDTSDAVVMPKIDTPRLCSFLRAACQVMAVLLEEDRLAAEPSWNLRAQDRALYFSDSSSQLNTSLPFLQNRKVSSLHTSRVQRQMVVSVHDLPEKSFVPLLDSKYVLCVWDIWQPSGPQKVLICESQVTCCCLSPLKAFLLFAGTAHGSVVVWDLREDSRLHYSVTLSDGFWTFRTATFSTDGILTSVNHRSPLQAVEPISTSVHKKQSFVLSPFSTQEEMSGLSFHIASLDESGVLNVWVVVELPKADIAGSISDLGLMPGGRVKLVHSALIQLGDSLSHKGNEFWGTTQTLNVKFLPSDPNHFIIGTDMGLISHGTRQDLRVAPKLFKPQQHGIRPVKVNVIDFSPFGEPIFLAGCSDGSIRLHQLSSAFPLLQWDSSTDSHAVTGLQWSPTRPAVFLVQDDTSNIYIWDLLQSDLGPVAKQQVSPNRLVAMAAVGEPEKAGGSFLALVLARASGSIDIQHLKRRWAAPEVDECNRLRLLLQEALWPEGKLHK
Protein: Cd209f protein (Q0P6C8)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
PRVRNRPHRGCCRGPWGYINPRAEGRWRGGSQEKQRMAGEPEFHQSKNHEEEVTSGEQGFAEHDPEGLICSSKSLQGHLTQVPWLLLLLISLGLFLLMLATLVQVSRIRAYSQGQTQDQQGSSSLDKVAVPREQTHSGLEQIQQIQQQLTQFNASLAGLCRPCPWDWELFQGSCYLFSRTLGSWETSASSCEDLGAHLVIVNSVSEQRFMKYWNVRKNQRSWIGLSDHIHDVPGSGWTAAPSSSAFGKRGNLTMTEMRTAWSCSWMIGMIISALNRTFGSVSSPLLPALITEDLCSPSHTGNLGALCSHSSCLIHPSAPVLRPLRS
Protein: Type 2 topoisomerase subunit A (EC 5.6.2.2) (DNA gyrase subunit A) (O67108)
Organism: Aquifex aeolicus (strain VF5)
Function: A type II topoisomerase. Despite its similarity to DNA gyrase, this enzyme is not able to supercoil DNA, and instead acts like topoisomerase IV. Relaxes both positively and negatively supercoiled DNA in an ATP-dependent fashion, decatenates interlocked circles. This the first bacteria shown to not contain DNA gyrase, although it has 2 copies of a reverse gyrase that introduces positive supercoils. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P0AES4}.
Interaction partners:
- Type 2 topoisomerase subunit B
- Bifunctional protein FolD
- Bifunctional chorismate mutase/prephenate dehydratase
- Small ribosomal subunit protein bS1
- DNA 3'-5' helicase
- Replicative DNA helicase
- Chromosomal replication initiator protein DnaA
- Beta sliding clamp
- DNA mismatch repair protein MutL
Sequence:
MENRENLVEIPIEEEVKQAYIDYAMSVIVGRAIPDVRDGLKPVQRRILYSMYEMGLLPDKPFKKSARIVGETLGKYHPHGDQAVYEALVRMAQDFTMRYPLIIGQGNFGSIDGDPAAQMRYTEAKLSPLAVEMLTDIDKDTVDFQPNFDDTLMEPEVLPSKFPNLLCNGTSGIAVGLATSIPPHNLTEVGNALVKLAQNPQISVDEIMEILKGPDFPTGGVIENFAQVKEIYKTGRGIIKVKGKAHVEKVQGGRERIVITEIPYQVNKAELIKKIADNVRNGKIKEISDIRDETDKEGIRIVVELKRDAKGEEVLKKLYKYTPLEKGFPVNLVVLIDKEPKLVDIKTLLREFIKHRLEVILRRSKYFLKKVQDRLHIVEGLLKAINFIDDIIERIRRSKDASEARNYLMEEFGLSEKQAQAVLDLRLQRLTSLEREKLLEEEKELREKIEYYKKLVASEGERIKVFIEETEELVKKYGDKRRTFIGGVKEVKEGSITVAVLQDGSIIPVEELPLEKAPVVNILRVPFTEGLFLVSNRGRVYWIAGSQALQGSKVSLKSREEKIVGAFIREKFGNRLLLATKKGYVKKIPLAEFEYKAQGMPIIKLTEGDEVVSIASSVDETHILLFTKKGRVARFSVREVPPSTPGARGVQGIKLEKNDETSGLRIWNGEPYLLVITAKGRVKKISHEEIPKTNRGVKGTEVSGTKDTLVDLIPIKEEVELLITTKNGKAFYDKINQKDIPLSTKKSIPRTRWKLEDDEIIKVVIKKSE
Protein: Monothiol glutaredoxin-S13 (AtGrxS13) (Protein ROXY 18) (Q84TF4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May only reduce GSH-thiol disulfides, but not protein disulfides.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Transcription factor TGA2
- Mediator of RNA polymerase II transcription subunit 18
- Monothiol glutaredoxin-S17
- Glutaredoxin-C13
- Glutaredoxin-C2
- Glutaredoxin-C14
- Glutaredoxin-C1
- Transcription factor TGA5
- Mediator of RNA polymerase II transcription subunit 8
Sequence:
MQKAIRPYESPWTKTVPGNSIFLLKNEDKPSSSSSSLSWLTSGSPKPTSISNKRSSNLVVMENAVVVFARRGCCLGHVAKRLLLTHGVNPVVVEIGEEDNNNYDNIVSDKEKLPMMYIGGKLFGGLENLMAAHINGDLVPTLRQAGALWL
Protein: CB1 cannabinoid receptor-interacting protein 1 (CRIP-1) (Q5M7A7)
Organism: Rattus norvegicus (Rat)
Function: Suppresses cannabinoid receptor CNR1-mediated tonic inhibition of voltage-gated calcium channels.
Interaction partners:
- Cannabinoid receptor 1
Sequence:
MGDLPGIVRLSIALRIQPNDGPVFFKVDGQRFGQNRTIKLLTGSSYKVEVKIKPTTLQVENISIGGVLVPLELKCKEPDGERVVYTGIYDTEGVAPTKSGERQPIQITMPFTDIGTFETVWQVKFYNYHKRDHCQWGSPFSVIEYECKPNETRSLMWVNKESFL