wanglab/gogpt-training-data huggingface dataset:
Protein: Radish, isoform L (X2JF15)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTMTAICFVCNLPIMSHQVGLVWQGGNGWDDLVREQLEESTIRQRLGGRRDSAAQITTPPSTSPPPGLQRRRRSSLAQLTDILREWSGGTKQQQQHHSQQQQQQLQQASRSKAQLNRRETLADLARSLPWRTSTTTDASTGAGGSGGGGCTTYMAPRKRRESSADSGIRSMRSRRDSNTAEFVRHWNRRESGAVEEQPSVSVPVVVECSKSASRRGSGESYLSSSRRDSNVAGRVTTPPPPGKYQMTKKRDSLAAPEFPNFRQEQRPSTSSAGSCSDHSMPLISTHSSTHHLAHQQVDSACQALPPPTIITSSVTPPATSPTAPKGRRDSQTQCGRVNRRDSKAGVSPERAPRLQRLQRQATAFDEGCLPGGSRRGSQPALSPDPPDDCERRTSRRDSLSPDSASRGGRRDSRTHLSPDRSHERDGSPRRHTLRRQSSSAARSPRSPDSNSCCSSRDPSPCSRPQTQTTVEQNQRPAIRRQSTTEEILIARGFRRQSTTEEMIRCRNFRRQSSQSDDVCRYRGRRDSSAQIIDGTIGTMTVETTSTFFDSSTQTEPSPLYDNNHYHEECLRCNSCGLNLTGPNQKRARRFKNQILCDLHFADVALMECSDFMQQLRSFKPQSLGCAVARRKSSTTLIFPLPPQACSDEFCEEYPHNLMPTPGYWIECSRQKITMPTPHTIWDESDSEHEDIRAGSASDAYLERECSDLYEDDEDSEATPSPRKKTTIEEQWDQQGAFELISVEQETYEKYFYGTEHWNYFTSDEDLGPVILSIKQETLNGRDQFRILVRAGSYTVHGLIPASCVFADRYNREEVVRSLGKEVNLNPPLTLGQLPDTPEELLKLDQVFIKSELKVGVIFVKEDQYTEEQILDNNENSPLFDEFLTLLGDRVRLRGFDKYKGGLDTVHDLTGLFSVYTNWRNIEIMFHVSTLLPYEKHDPQKLQRKRHIGNDIVCVVFLEADNTRFSPACIKSHFLHTFILVRVSARIKHKPTRYEVSVVTRDEVGAYKPYLWEQSVFEKGPMFREWLLTKIVNGERASYSAPKFARMQERTRSQMLEDLVMNLSNHAETGQIPKPYRRGSWRPIGHMRPSSPLLDSVRDQFEDYDQLAKDFTRVFLNEEPSCLTNAHLFDVVFLVGQSKQKARFIGVRAILGVRSRVFQEMLYGIQTGFGSPQIPVAEIFARPAPSLVSPQNQKPKSNNYLTVPDSDSIRPKSVPSSPMVKRAFSRLGTITAGWGRSIRNKNTNQLNPDDKKKWISSTDCSNRDSKDKDKDKPGNNQLAVPRLSVCADAQKVDRAKLAQTEFNIIEFDPDTFRVLLDYLHTGTCPLTCVSIPGLLCAAEHYDLPELLQACFHHCKQFLRIEVVCPMLISLENYYWRYTSASELVNMILSFVESKAHSLFKCPEFLHLSESMVQMIMCRELQTPEIRKFEAMLAWAQHKVGKLKNHPNKDTQFEFECIMERLTRDLNLCRISPSELLTVVLPSKSMKNERIMETLMVQVNLGTYRMPELDAYRQQLRQQESAEATVQVHRAHQNHHNPPPIDARAYAMASLAAALEMQNSSNPLQSNAARDAADEEVELYASFDNAPSTSRVAAQMQAAKEARRKRWAADGASGSSGDGGCASGSSGSGRRY
Protein: Cryptochrome-1 (A4QN37)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Period circadian protein homolog 2
- Aryl hydrocarbon receptor nuclear translocator-like 1a
- Period circadian clock 1a.
- Circadian locomoter output cycles protein kaput
- Period homolog 1b
- Period circadian clock 3.
- Aryl hydrocarbon receptor nuclear translocator-like 1b.
- Circadian locomoter output cycles protein kaput
- Aryl hydrocarbon receptor nuclear translocator-like 2
- Protein timeless homolog
Sequence:
MVVNTVHWFRKGLRLHDNPSLRDSILGAHSVRCVYILDPWFAGSSNVGISRWRFLLQCLEDLDASLRKLNSRLFVIRGQPTDVFPRLFKEWNINRLSYEYDSEPFGKERDAAIKKLANEAGVEVIVRISHTLYDLDKIIELNGGQSPLTYKRFQTLISRMEAVETPAETITAEVMGPCTTPLSDDHDEKFGVPSLEELGFDTEGLSSAVWPGGETEALTRLERHLERKAWVANFERPRMNANSLLASPTGLSPYLRFGCLSCRLFYFKLTDLYRKVKKNSSPPLSLYGQLLWREFFYTAATNNPRFDKMEGNPICVQIPWDKNPEALAKWAEGRTGFPWIDAIMTQLRQEGWIHHLARHAVACFLTRGDLWISWEEGMKVFEELLLDADWSVNAGSWMWLSCSSFFQQFFHCYCPVSFGRRTDPNGDYIRRYLPVLRGFPAKYIYDPWNAPESVQKAAKCIIGVHYPMPMVHHAEASRLNIERMKQIYQQLSCYRGLGLLAMVPSNPNGNGENSTSLMGFKTGDMTKEVTTPSGYQMPPTSQGEWHGRTMVYSQGDQQTSSIMTSQGFGNNGSTMCYRQDAQQITGRGLHSSIIQTSGKRHSEESGPTTVSKVQRQCSS
Protein: Histone H3 (P61833)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Subcellular location: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
Interaction partners:
- Histone H4
- Histone acetyltransferase GCN5
- Histone H2B.2
- Histone H2A.2
- Histone H2B.1
- Histone-lysine N-methyltransferase, H3 lysine-79 specific
- Histone-lysine N-methyltransferase, H3 lysine-4 specific
- Histone H2A.1
- Histone-lysine N-methyltransferase, H3 lysine-36 specific
- FACT complex subunit SPT16
Sequence:
MARTKQTARKSTGGKAPRKQLASKAARKSAPSTGGVKKPHRYKPGTVALREIRRFQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAIGALQESVEAYLVSLFEDTNLAAIHAKRVTIQKKDIKLARRLRGERS
Protein: Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-3 (P63216)
Organism: Mus musculus (Mouse)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit beta-5
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit beta-4
- Pituitary adenylate cyclase-activating polypeptide type I receptor
- 5-hydroxytryptamine receptor 7
- Ras-specific guanine nucleotide-releasing factor 1
Sequence:
MKGETPVNSTMSIGQARKMVEQLKIEASLCRIKVSKAAADLMTYCDAHACEDPLITPVPTSENPFREKKFFCALL
Protein: Cyclic phosphodiesterase (CPDase) (EC 3.1.4.37) (O04147)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Hydrolyzes ADP-ribose 1'',2''-cyclic phosphate (Appr>1) that is produced during tRNA splicing into ADP-ribose 1''-phosphate (Appr-1''p). Acts also on nucleoside 2',3'-cyclic phosphates.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9148938}.
Interaction partners:
- 2'-phosphotransferase
- 2'-phosphotransferase
- tRNA ligase 1
- Polynucleotide 3'-phosphatase ZDP
- At5g40190
- Inosine-5'-monophosphate dehydrogenase 1
- tRNA-splicing endonuclease subunit Sen2-2
- DNA ligase 6
- Plastid division protein CDP1, chloroplastic
Sequence:
MEEVKKDVYSVWALPDEESEPRFKKLMEALRSEFTGPRFVPHVTVAVSAYLTADEAKKMFESACDGLKAYTATVDRVSTGTFFFQCVFLLLQTTPEVMEAGEHCKNHFNCSTTTPYMPHLSLLYAELTEEEKKNAQEKAYTLDSSLDGLSFRLNRLALCKTDTEDKTLETWETVAVCNLNP
Protein: Voltage-dependent L-type calcium channel subunit beta-1 (CAB1) (Calcium channel voltage-dependent subunit beta 1) (P54283)
Organism: Rattus norvegicus (Rat)
Function: Regulatory subunit of L-type calcium channels. Regulates the activity of L-type calcium channels that contain CACNA1A as pore-forming subunit (By similarity). Regulates the activity of L-type calcium channels that contain CACNA1C as pore-forming subunit and increases the presence of the channel complex at the cell membrane (Probable). Required for functional expression L-type calcium channels that contain CACNA1D as pore-forming subunit. Regulates the activity of L-type calcium channels that contain CACNA1B as pore-forming subunit (By similarity).
Subcellular location: Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P19517}; Peripheral membrane protein {ECO:0000250|UniProtKB:P19517}; Cytoplasmic side {ECO:0000250|UniProtKB:P19517}. Cell membrane {ECO:0000250|UniProtKB:Q02641}; Peripheral membrane protein {ECO:0000250|UniProtKB:P19517}.
Interaction partners:
- Voltage-dependent calcium channel subunit alpha-2/delta-1
- Voltage-dependent L-type calcium channel subunit alpha-1S
- Voltage-dependent L-type calcium channel subunit alpha-1C
- Voltage-dependent calcium channel gamma-1 subunit
- Voltage-dependent R-type calcium channel subunit alpha-1E
- Voltage-dependent P/Q-type calcium channel subunit alpha-1A
- Voltage-dependent L-type calcium channel subunit alpha-1D
- Voltage-dependent L-type calcium channel subunit beta-2
- Voltage-dependent L-type calcium channel subunit beta-3
- Voltage-dependent calcium channel subunit alpha-2/delta-2
Sequence:
MVQKSGMSRGPYPPSQEIPMEVFDPSPQGKYSKRKGRFKRSDGSTSSDTTSNSFVRQGSAESYTSRPSDSDVSLEEDREALRKEAERQALAQLEKAKTKPVAFAVRTNVGYNPSPGDEVPVQGVAITFEPKDFLHIKEKYNNDWWIGRLVKEGCEVGFIPSPVKLDSLRLLQEQTLRQNRLSSSKSGDNSSSSLGDVVTGTRRPTPPASAKQKQKSTEHVPPYDVVPSMRPIILVGPSLKGYEVTDMMQKALFDFLKHRFDGRISITRVTADISLAKRSVLNNPSKHIIIERSNTRSSLAEVQSEIERIFELARTLQLVALDADTINHPAQLSKTSLAPIIVYIKITSPKVLQRLIKSRGKSQSKHLNVQIAASEKLAQCPPEMFDIILDENQLEDACEHLAEYLEAYWKATHPPSRTPPNPLLNRTMATAALAVSPAPVSNLQGPYLVSGDQPLDRATGEHASVHEYPGELGQPPGLYPSNHPPGRAGTLWALSRQDTFDADTPGSRNSVYTEPGDSCVDMETDPSEGPGPGDPAGGGTPPARQGSWEEEEDYEEEMTDNRNRGRNKARYCAEGGGPVLGRNKNELEGWGQGVYIR
Protein: Vacuolar membrane protease (EC 3.4.-.-) (FXNA-related family protease 1) (O94479)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: May be involved in vacuolar sorting and osmoregulation.
Subcellular location: Membrane {ECO:0000269|PubMed:10759889}. Vacuole membrane {ECO:0000250|UniProtKB:P38244}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MTNSRRHIFERICAKAFQSSLTCSIFGFTVLLILYLLDWKRIAQVPGPNLLKDLEFQRAWNDLEYISSLPHPYNSKQNEHVRSYILKSMRELEATNQSYITVIDDTLTNITFESTDNDTLTYFEGDNILVKFEGKSKDLFPILLSAHFDSVSTGYGATDDGMGVATVMAIARYYAKNQPNRDLIININNAEEDYLFGAKAFASHKLSKNVTAFVNLEGAGSGGKAMLFRSSNGHVSSAYFKGNHYPLASILGNDFFKRGVIRSQTDYIVYEKMHNHTAGLDIAFYENRDIYHTRKDDINHLMPSSLRHMMYTASNAVKNLLNDSKSDLTKFRKPMFFLAFGKYWQLNLPIYQVLNIIFAVICPIVLLLTLIRFPSLYEQLKKPRYTVCFVVSCIFVSIFDTLTVLLLTWINPYVINSHTGLILALFYLTNLIALAFSFRAAATHSKLSSEDLSSIEIVFIWYAQILWYLVFIVSVILSIYFQLGSTYWVTLSYLCTFTCCIMTIIRINYFVDNVVTTQTTHEEDALIGSSINTSSHQHYGSTLNSTPHRRNSIALSNRAHVKLIDNIWTVIYFIFNVPFPVFLCYDILVETILPAGSQTLTDSVFSSKLYKLVIFVVFLSLVNSGPFIFRALSKKSLAVLTMLWITLFVQALSVNPFTESAPLKLSFVQMYDMDRMNNTVYVKNISPFTQDVLSLNPHFLFSNGSCNTSLCYYESTDPDFGGLKTPMSIHIEREKHQLDISINSGSKWCYVDFNTSVFFEAINGNSISGMYSSVRMGQRSFYAPYTLNLTITEVVKAEVTCLYDDIHEGIIPAYNTFVEHLPSWVAGVKASTGLLKVKSSIVI
Protein: Solute carrier family 2, facilitated glucose transporter member 2 (Glucose transporter type 2, liver) (GLUT-2) (P14246)
Organism: Mus musculus (Mouse)
Function: Facilitative hexose transporter that mediates the transport of glucose, fructose and galactose. Likely mediates the bidirectional transfer of glucose across the plasma membrane of hepatocytes and is responsible for uptake of glucose by the beta cells; may comprise part of the glucose-sensing mechanism of the beta cell. May also participate with the Na(+)/glucose cotransporter in the transcellular transport of glucose in the small intestine and kidney. Also able to mediate the transport of dehydroascorbate.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P11168}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cellular tumor antigen p53
- Hexokinase-4
- Solute carrier family 2, facilitated glucose transporter member 1
- Sodium/glucose cotransporter 1
- Insulin-2
- Insulin-1
- Glucose-6-phosphatase catalytic subunit 1
- Pro-glucagon
- Homeobox protein Nkx-6.1
- Neurogenic differentiation factor 1
Sequence:
MSEDKITGTLAFTVFTAVLSSFQFGYDIGVINAPQEVIISHYRHVLGVPLDDRKAAINYDVNGTDTPLTVTPAYTTPAPWDEEETEGSAHIVTMLWSLSVSSFAVGGMVASFFGGWLGDKLGRIKAMLAANSLSLTGALLMGCSKFGPAHALIIAGRSVSGLYCGLISGLVPMYIGEIAPTTLRGALGTLHQLALVTGILISQIAGLSFILGNQDHWHILLGLSAVPALLQCLLLLFCPESPRYLYIKLEEEVRAKKSLKRLRGTEDVTKDINEMKKEKEEASTEQKVSVIQLFTDANYRQPILVALMLHMAQQFSGINGIFYYSTSIFQTAGISQPVYATIGVGAINMIFTAVSVLLVEKAGRRTLFLTGMIGMFFCTIFMSVGLVLLDKFAWMSYVSMTAIFLFVSFFEIGPGPIPWFMVAEFFSQGPRPTALALAAFSNWVCNFVIALCFQYIADFLGPYVFFLFAGVVLVFTLFTFFKVPETKGKSFEEIAAEFRKKSGSAPPRKAAVQMEFLASSESV
Protein: NAD-dependent protein deacetylase SIR2rp1 (EC 2.3.1.286) (Regulatory protein SIR2 homolog 1) (SIR2-related protein 1) (Q57V41)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Function: NAD-dependent protein deacetylase, which is involved in repression of RNA polymerase I-mediated expression immediately adjacent to telomeres. It is however not involved in antigenic variation and subtelomeric variant surface glycoprotein (VSG) gene silencing. Plays a role in DNA damage response. Also has ADP-ribosylation activity in vitro.
Subcellular location: Nucleus. Chromosome, telomere. Note=Co-localizes with telomeres and minichromosomes.
Interaction partners:
- NAD-dependent protein deacylase SIR2rp3
- NAD+ synthase, putative
- Cytidyltransferase-like domain-containing protein
- ATP-NAD kinase-like protein
- Inosine-adenosine-guanosine-nucleoside hydrolase
- Nucleoside hydrolase, putative
- Histone H4
- Histone H4
- Histone H3 variant
- Histone H3, putative
Sequence:
MTEPKLATTHVVGEPTFEGLARFIERNNITKIFVMVGAGISVAAGIPDFRSPHTGLYAKLSRYNLNSPEDAFSLPLLRQQPSVFYNILMDMDLWPGKYCPTTVHHFISLLAKKGMLLCCCTQNIDGLERACGIPESLLVEAHGSFSSASCVDCHAKYDINMARAETRAGKVPHCNQCGGIVKPDVVFFGENLPEAFFNVAGLIEETELLLILGTSLQVHPFADLALMVPSDVPRVLFNLERVGGRMFRFPTDRTPNFRASSYRLSTGNGNGSKISSGDSSNSSSVDGYDQFTLAENDETGVLRDIFFPGDCQVSVRSFAQALGFGEQLDASVREGREIFERTRRREKVVEG
Protein: Uncharacterized protein YOR062C (P36025)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Uncharacterized globin-like protein YNL234W
Sequence:
MTSLDDSVLTKKNIALLDNATNYIRPAIDYFHFKFNYDSLDVSTTWRLLLKMRKHKLLRLPSCSSENEFDYSIYMARLYHCIWRRWSIKHFNLDEYKIDPLSINWNKEIDVTVLYGPDLVGIHEREQPTPTDFPMGNIKEQGKQLLDVRKEGSASSLLKKGSVFYSKGKWLSQRSISFDDTVRRRDIDKRGRFRESCVLINDVEQFQNYSIVWDESRHRYRRQALPDTYDYEHLYPNGDETPRNTPHDNIIIHQNLHSITEGSYIYIK
Protein: Filamin A (A0A8I5ZV49)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MSSSHSRSGQSAAGASPAGGIDTRDAEMPATEKDLAEDAPWKKIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHNQRPTFRQMQLENVSVALEFLDRESIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMPMWDEEEDEEAKKQTPKQRLLGWIQNKLPQLPITNFSRDWQSGRALGALVDSCAPGLCPDWDSWDASKPVNNAREAMQQADDWLGIPQVITPEEIVDPNVDEHSVMTYLSQFPKAKLKPGAPLRPKLNPKKARAYGPGIEPTGNMVKKRAEFTVETRSAGQGEVLVYVEDPAGHQEEAKVTANNDKNRTFSVWYVPEVTGTHKVTVLFAGQHIAKSPFEVYVDKSQGDASKVTAQGPGLEPSGNIANKTTYFEIFTAGAGIGEVEVVIQDPTGQKGTVEPQLEARGDSTYRCSYQPTMEGVHTVHVTFAGVPIPRSPYTVTVGQACNPTACRAVGRGLQPKGVRVKETADFKVYTKGAGSGELKVTVKGPKGEERVKQKDLGDGVYGFEYYPTIPGTYTVTITWGGQNIGRSPFEVKVGTECGNQKVRAWGPGLEGGIVGKSADFVVEAIGDDVGTLGFSVEGPSQAKIECDDKGDGSCDVRYWPQEAGEYAVHVLCNSEDIRLSPFMADIREAPQDFHPDRVKARGPGLEKTGVAINKPAEFTVDAKHAGKAPLRVQVQDNEGHSVETTVKDNGNGTYSCSYVPRKPVKHTAMVSWGGVSIPNSPFRVNVGAGSHPNKVKVYGPGVAKTGLKAHEPTYFTVDCTEAGQGDVSIGIKCAPGVVGPTEADIDFDIIRNDNDTFTVKYTPCGAGSYTIMVLFADQATPTSPIRVKVEPSHDASKVKAEGPGLNRTGVELGKPTHFTVNAKTAGKGKLDVQFSGLAKGDAVRDVDIIDHHDNTYTVKYTPVQQGPVGVSVTYGGDHIPKSPFSVGVSPSLDLSKIKVSGLVDKVDVGKDQEFTVKSKGAGGQGKVASKIVSPSGAAVPCKVEPGLGADNSVVRFVPREEGPYEVEVTYDGVPVPGSPFPVEAVAPTKPSKVKAFGPGLQGGNAGSPARFTIDTKGAGTGGLGLTVEGPCEAQLECLDNGDGTCSVSYVPTEPGDYNINILFADTHIPGSPFKAHVVPCFDASKVKCSGPGLERATAGEVGQFQVDCSSAGSAELTIEICSEAGLPAEVYIQDHGDGTHTITYIPLCPGAYTVTIKYGGQPVPNFPSKLQVEPAVDTSGVQCYGPGIEGQGVFREATTEFSVDARALTQTGGPHVKARVANPSGNLTDTYVQDCGDGTYKVEYTPYEEGVHSVDVTYDGSPVPSSPFQVPVTEGCDPSRVRVHGPGIQSGTTNKPNKFTVETRGAGTGGLGLAVEGPSEAKMSCMDNKDGSCSVEYIPYEAGTYSLNVTYGGHQVPGSPFKVPVHDVTDASKVKCSGPGLSPGMVRANLPQSFQVDTSKAGVAPLQVKVQGPKGLVEPVDVVDNADGTQTVNYVPSREGSYSISVLYGEEEVPRSPFKVKVLPTHDASKVKASGPGLNTTGVPASLPVEFTIDAKDAGEGLLAVQITDPEGKPKKTHIQDNHDGTYTVAYVPDVTGRYTILIKYGGDEIPFSPYRVRAVPTGDASKCTVTVSIGGHGLGAGIGPTIQIGEETVITVDTKAAGKGKVTCTVCTPDGSEVDVDVVENEDGTFDIFYTAPQPGKYVICVRFGGEHVPNSPFQVTALAGDQPTVQTPLRPQQLPSQYTYPQGSQQTWIPERPMVGVNGLDVTSLRPFDLVIPFTIKKGEITGEVRMPSGKVAQPSITDNKDGTVTVRYSPSEAGLHEMDIRYDNMHIPGSPLQFYVDYVNCGHITAYGPGLTHGVVNKPATFTVNTKDAGEGGLSLAIEGPSKAEISCTDNQDGTCSVSYLPVLPGDYSILVKYNDQHIPGSPFTARVTGDDSMRMSHLKVGSAADIPINISETDLSLLTATVVPPSGREEPCLLKRLRNGHVGISFVPKETGEHLVHVKKNGQHVASSPIPVVISQSEIGDASRVRVSGQGLHEGHTFEPAEFIIDTRDAGYGGLSLSIEGPSKVDINTEDLEDGTCRVTYCPTEPGNYIINIKFADQHVPGSPFSVKVTGEGRVKESITRRRRAPSVANVGSHCDLSLKIPEISIQDMTAQVTSPSGKTHEAEIVEGENHTYCIRFVPAEMGMHTVSVKYKGQHVPGSPFQFTVGPLGEGGAHKVRAGGPGLERAEAGVPAEFGIWTREAGAGGLAIAVEGPSKAEISFEDRKDGSCGVAYVVQEPGDYEVSVKFNEEHIPDSPFVVPVASPSGDARRLTVSSLQESGLKVNQPASFAVSLNGAKGAIDAKVHSPSGALEECYVTEIDQDKYAVRFIPRENGVYLIDVKFNGTHIPGSPFKIRVGEPGHGGDPGLVSAYGAGLEGGVTGSPAEFIVNTSNAGAGALSVTIDGPSKVKMDCQECPEGYRVTYTPMAPGSYLISIKYGGPYHIGGSPFKAKVTGPRLVSNHSLHETSSVFVDSLTKVATVPQHATSGPGPADVSKVVAKGLGLSKAYVGQKSNFTVDCSKAGNNMLLVGVHGPRTPCEEILVKHMGSRLYSVSYLLKDKGEYTLVVKWGDEHIPGSPYRIMVP
Protein: Signaling pathway modulator ZraP (Zinc resistance-associated protein) (Zra periplasmic repressor partner) (Zra system accessory protein ZraP) (P0AAA9)
Organism: Escherichia coli (strain K12)
Function: Binds zinc. Could be an important component of the zinc-balancing mechanism.
Subcellular location: Periplasm {ECO:0000269|PubMed:9694902}.
Interaction partners:
- Sensor histidine kinase ZraS
- Transcriptional regulatory protein ZraR
- Zinc/cadmium/lead-transporting P-type ATPase
Sequence:
MKRNTKIALVMMALSAMAMGSTSAFAHGGHGMWQQNAAPLTSEQQTAWQKIHNDFYAQSSALQQQLVTKRYEYNALLAANPPDSSKINAVAKEMENLRQSLDELRVKRDIAMAEAGIPRGAGMGMGYGGCGGGGHMGMGHW
Protein: Solute carrier organic anion transporter family, member 6c1 (G3V7R7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MGQVQNKKPDAKKDDKHNQETEGLKKIDTYLRTIPTVTKKFKGRPQKKRSPTSAELLLDPKYSASKEGPFGLGPLVFPCLQRFNNIDCFMIFFIASVLIHGALFALADMILNLYHSLLTLSKRELYFMDFSGYIVSSLVAIFVAHFGGKGNRTKWIAAACILMAFGSILLGFPFSKYEIMKSGGQRVELCVEENKRRNIHCVTNSNPDRTKCICFFIIGQCLNGIAGMPIYILGKTFIFDHVPTRSAGFYLALGHSAHLMGYFLGIFGGMKNLSPPPKEKLSAVDSAKIHLLLQFGWWKTFLFVAAISFSVFLVLLCFPTSLPGAHKLKLAKRKEPPTFDKRLKDQKIQPRFKGFVFAIWYMLRNPLLMTQAMCKVSESFAFHTSLEFLPYHLQTQFSITPQIASMLTGLFVIPGGVIGHFLGGLIVDRLEMTNKNKLKFSLVTSVVSVALFLLIFFVECETTKFAGINEDYDGLGKLGNLTAGCNYHCACTTSLYSSVCGRDEKEYFSPCFAGCSATKVQQNEKTYYNCSCIKEGLTTSDADGHFIDATDGTCNSNCLTLPLFFAFYFSATVFSTMCSTPIILIILQSVPANFSSLGLGVTVAITKFTASVPEPALFGTASSVACKFWDINACGVREKCWIYNKTTLVYVFIGIWVSFKLFTALLNIYAIHIYDYVVKGKISDSKTTHVKASKAQKERRA
Protein: ArfGAP with dual PH domains 1 (A0A087WTN6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVLASLELLREQWIRAKYERQEFIYPEKQEPYSAGYREGFLWKRGRDNGQFLSRKFVLTEREGALKYFNRNDAKEPKAVMKIEHLNATFQPAKIGHPHGLQVTYLKDNSTRNIFIYHEDGKEIVDWFNALRAARFHYLQVAFPGAGDADLVPKLSRNYLKEGYMEKTGPKQTEGFRKRWFTMDDRRLMYFKDPLDAFARGEVFIGSKESGYTVLHGFPPSTQGHHWPHGITIVTPDRKFLFACETESDQREWVAAFQKAVDRPMLPQEYAVEAHFKHKP
Protein: Ankyrin repeat and LEM domain-containing protein 2 homolog (Q8MQX9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Involved in brain development probably by regulating asymmetric division of neuroblasts. Regulates neuroblast asymmetric cell division by controlling asymmetric protein localization of Mira, Baz, Par-6 and aPKC, and spindle alignment. Also, regulates the localization of kinase Ball during mitosis, specifically maintaining Ball in the nucleus during interphase. Required for proper ER and nuclear envelope morphology in neuroblasts.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:31735666}. Nucleus envelope {ECO:0000269|PubMed:31735666}. Cytoplasm {ECO:0000269|PubMed:31735666}. Note=In neuroblasts, recruited to the nuclear envelope at the initiation of mitosis and remains associated with it until the beginning of cytokinesis. {ECO:0000269|PubMed:31735666}.
Interaction partners:
- Nucleosomal histone kinase 1
- non-specific serine/threonine protein kinase
- Barrier-to-autointegration factor
- NAD-dependent protein deacetylase Sirt2
- Serine/threonine-protein phosphatase PP2A 65 kDa regulatory subunit
Sequence:
MSTYFGVYIPTSKAGCFEGSVSQCIGSIAAVNIKPSNPASGSASVASGSPSGSAASVQTGNADDGSAATKYEDPDYPPDSPLWLIFTEKSKALDILRHYKEARLREFPNLEQAESYVQFGFESIEALKRFCKAKPESKPIPIISGSGYKSSPTSTDNSCSSSPTGNGSGFIIPLGSNSSMSNLLLSDSPTSSPSSSSNVIANGRQQQMQQQQQQQPQQPDVSGEGPPFRAPTKQELVEFRKQIEGGHIDRVKRIIWENPRFLISSGDTPTSLKEGCRYNAMHICAQVNKARIAQLLLKTISDREFTQLYVGKKGSGKMCAALNISLLDYYLNMPDKGRGETPLHFAAKNGHVAMVEVLVSYPECKSLRNHEGKEPKEIICLRNANATHVTIKKLELLLYDPHFVPVLRSQSNTLPPKVGQPFSPKDPPNLQHKADDYEGLSVDLAISALAGPMSREKAMNFYRRWKTPPRVSNNVMSPLAGSPFSSPVKVTPSKSIFDRSAGNSSPVHSGRRVLFSPLAEATSSPKPTKNVPNGTNECEHNNNNVKPVYPLEFPATPIRKMKPDLFMAYRNNNSFDSPSLADDSQILDMSLSRSLNASLNDSFRERHIKNTDIEKGLEVVGRQLARQEQLEWREYWDFLDSFLDIGTTEGLARLEAYFLEKTEQQADKSETVWNFAHLHQYFDSMAGEQQQQLRKDKNEAAGATSPSAGVMTPYTCVEKSLQVFAKRITKTLINKIGNMVSINDTLLCELKRLKSLIVSFKDDARFISVDFSKVHSRIAHLVASYVTHSQEVSVAMRLQLLQMLRSLRQLLADERGREQHLGCVCASLLLMLEQAPTSAVHLPDTLKTEELCCAAWETEQCCACLWDANLSRKTSRRKRTKSLRAAAVVQSQGQLQDTSGSTGSSALHASLGVGSTSLGASRVVASASKDAWRRQQSDDEDYDSDEQVIFFDCTNVTLPYGSSSEDEENFRTPPQSLSPGISMDLEPRYELFIFGNEPTKRDLDVLNALSNVDIDKETLPHVYAWKTAMESYSCAEMNLFPSPRNVKVQKPEPWYSGTSSSHNSQPLLHPKRLLATPKLNAVVSGRRGSGPLTAPVTPRLARTPSAASIQVASETNGESVGTAVTPASPILSFAALTAATQSFQTPLNKVRGLFSQYRDQRSYNEGDTPLGNRN
Protein: Nucleoside diphosphate kinase (EC 2.7.4.6) (Q5AG68)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Mitochondrial 37S ribosomal protein MRP4
- Mitochondrial 37S ribosomal protein MRPS16
- Mitochondrial 37S ribosomal protein MRPS28
- Small ribosomal subunit protein uS7m
- 37S ribosomal protein MRP2
- Small ribosomal subunit protein uS9m
- Small ribosomal subunit protein mS29
- Small ribosomal subunit protein uS10m
- Small ribosomal subunit protein bS6m
- Small ribosomal subunit protein uS11m
Sequence:
MSDERTFIAIKPDGVQRGLISSILGRFEQRGFKLVGIKLVQPTESLLRTHYEDLQSKPFFPSLLSYMLSGPVLATVWEGKDVVKQGRAILGATNPLQSAPGTIRGDFAIDMGRNVCHGSDSVESANKEIDLWFKKEELVEYKPALFGWIYE
Protein: Cytochrome b5, putative (Q385A5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- NADH-cytochrome b5 reductase
- NADH-cytochrome b5 reductase
- NADH-cytochrome b5 reductase, putative
- cytochrome-b5 reductase
- NADH-cytochrome b5 reductase, putative
- cytochrome-b5 reductase
- NADPH--hemoprotein reductase
- Fatty acid desaturase, putative
Sequence:
MTTSQLPKYTWEEIRKHNHDKDCWVVLYRRVLDVTKFLNEHPGGLDTINDLGGYDITNSFESIGHSSSALALSKEFIIGELDPSSAPPPVRVRKLGDDVPLTKVKGGGGVLSVYHIVGLFLLILLLLCYIFAT
Protein: Storkhead-box protein 2 (Q499E5)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MKKTRSTTLRRAWPSSDFSDRASDRMRSRSEKDYRLHKRFPAAFAPQASRGYMTSGDVSPISMSPISQSQFIPLGEILCLAISAMNSARKPVTQEALMEHLTTCFPGVPTPSQEILRHTLNTLVRERKIYPTPDGYFIVTPQTYFITPSLIRTNSKWYHLDERVPDRSQCTSPQPGTITPSASGCVRERTLPRKHCDSCHCCREDVHSMHASTLQRKSAKDCKDPYCPPPLCQVPPTEKSKSTINFSYKTETLSKPKDGEKQSKKFGLKLFRLSFKKDKTKQLANFSAQFPPEEWPLRDEDTPTTIPREVEMEIIRRINPDLTVENVMRHTALMKKLEEEKAHRSKAGSSAHHSGRSKKSRTHRKSHGKSRSHSKTRVSKGDPSDGSHLDIPGEREYEFCDPLTRAPREGCFIIEHKGDNFIMHSNTNVIESHFPMTPEWDVSGELAKRRTEMPFPEPSRGSSHSKVHRSHSHTQDRRSRNERSNKAKERSRSMDNSKGPLGASSLGTPEDLAEGCSQDDQTPSQSYIDDSTLRPAQTIGHQRAHIPSASYKEVCIPEIVGGSKEPSSACSLLEPGKTPESMPSYGELSPCPAKTAVDDYFQCNTSSETVLTAPSPLGKNKEDHDTLTLVEGVKKLSPSERQTPHSSREPVGHKEESPKGPGGGPAASGGVAEGLANGRLVQHHSAEPSSLDKRKEIFSKDTLFKPLHSTLSVNSYHKSSLSLLKSHPKSPVDTLPGRCEKLEPSLGTSAAQAMPPSQRQQEPGGNQEASFDYYNVSDDDDSEEGANKNAEEEKNRDDVGTMQWLLEREKERDLQRKFEKNLTLLTPKETDSSSNQRATHSARLDSMDSSSITVDSGFNSPRTRESLASNTSSIVESNRRQNPALSPAHGGAGPTFNFRASTDPPTSEAEKLQKPSNCLQASVTSV
Protein: Insulin-like growth factor-binding protein 2 (IBP-2) (IGF-binding protein 2) (IGFBP-2) (P83628)
Organism: Oncorhynchus tshawytscha (Chinook salmon) (Salmo tshawytscha)
Function: Inhibits IGF-mediated growth and developmental rates (By similarity). IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
DLVFYCPKCTAERQTACPKL
Protein: Protein LHCP TRANSLOCATION DEFECT (Protein GRANA-DEFICIENT CHLOROPLAST 1) (Q8VY88)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the import of light-harvesting complex proteins (LHCP) and subsequent routing of these proteins to the chloroplast signal recognition particle (SRP) pathway.
Subcellular location: Plastid, chloroplast thylakoid membrane; Peripheral membrane protein. Plastid, chloroplast envelope. Plastid, chloroplast stroma.
Interaction partners:
- Carboxyl-terminal-processing peptidase 2, chloroplastic
- Pentatricopeptide repeat-containing protein At1g09820
- At1g28540
- Probable zinc metalloprotease EGY1, chloroplastic
- Deneddylase
- RING-type E3 ubiquitin transferase
- Protein CURVATURE THYLAKOID 1A
Sequence:
MASSSISFSCAPSLATSLFSTTSSSPRLLSSRFLGTRNLKLRIRPARLGPSNGSRTTCWFKFGKNGVDAENAGIYGSQSRDDFDRDDVEQYFNYMGMLAVEGTYSKMEALLNLNIHPVDILLMLAATEGDRPKIEELLKAGADYSVKDADGRTAIDRANSEEIRDLILGYSTQKA