wanglab/gogpt-training-data huggingface dataset:
Protein: Lon protease homolog 2, peroxisomal (EC 3.4.21.53) (Lon protease-like protein 2) (Lon protease 2) (Peroxisomal Lon protease) (Q9DBN5)
Organism: Mus musculus (Mouse)
Function: ATP-dependent serine protease that mediates the selective degradation of misfolded and unassembled polypeptides in the peroxisomal matrix. Necessary for type 2 peroxisome targeting signal (PTS2)-containing protein processing and facilitates peroxisome matrix protein import. May indirectly regulate peroxisomal fatty acid beta-oxidation through degradation of the self-processed forms of TYSND1.
Subcellular location: Peroxisome matrix {ECO:0000250|UniProtKB:Q86WA8, ECO:0000255|HAMAP-Rule:MF_03121}.
Interaction partners:
- ATP-dependent clpX-like chaperone, mitochondrial
- Peroxisomal leader peptide-processing protease
- ATP-dependent Clp protease proteolytic subunit, mitochondrial
- Mitochondrial disaggregase
- Peroxisomal targeting signal 1 receptor
- 60 kDa heat shock protein, mitochondrial
- GrpE protein homolog 2, mitochondrial
- GrpE protein homolog 1, mitochondrial
- Peroxisomal membrane protein PEX13
Sequence:
MSSVSPIQIPSRLPLLLTHESVLLPGSTMRTSVDTARNLQLVRSRLLKGTSLQSTILGVIPNTPDPASDTQDLPPLHRIGTAALAVQVVGSNWPKPHYTLLITGLCRFQIVQVLKEKPYPVAEVEQLDRLEEFPNICKSREELGELSEQFYRYAVQLVEMLDMSVPAVAKLRRLLDNLPREALPDILTSIIRTSNKEKLQILDAVSLEDRFKMTIPLLVRQIEGLKLLQKTRKPKQDDDKRVIAIRPIRRIPHIPGTLEDEEEEEDNDDIVMLEKKIRTSSMPEQAHKVCVKEIKRLKKMPQSMPEYALTRNYLELMVELPWNKSTTDRLDIRAARILLDNDHYAMEKLKRRVLEYLAVRQLKNNLKGPILCFVGPPGVGKTSVGRSVAKTLGREFHRIALGGVCDQSDIRGHRRTYVGSMPGRIINGLKTVGVNNPVFLLDEVDKLGKSLQGDPAAALLEVLDPEQNHNFTDHYLNVAFDLSQVLFIATANTTATIPPALLDRMEIIQVPGYTQEEKIEIAHRHLIPKQLEQHGLTPQQIQIPQHTTLAIITRYTREAGVRSLDRKFGAICRAVAVKVAEGQHKEAKLDRSDVADGEGCKEHVLEDAKPESISDTADLALPPEMPILIDSHALKDILGPPLYELEVSERLSQPGVAIGLAWTPLGGKIMFVEASRMDGEGQLTLTGQLGDVMKESAHLAISWLRSNAKKYHLTNAFGSFDLLDNTDIHLHFPAGAVTKDGPSAGVTIVTCLASLFSGRLVRSDVAMTGEITLRGLVLPVGGIKDKVLAAHRAGLKQIIIPQRNEKDLEEIPSNVRQDLSFVTASCLDEVLNAAFDGGFPVKTRPGLIDSKL
Protein: High mobility group nucleosome-binding domain-containing protein 5 (Nucleosome-binding protein 1) (P82970)
Organism: Homo sapiens (Human)
Function: Preferentially binds to euchromatin and modulates cellular transcription by counteracting linker histone-mediated chromatin compaction.
Subcellular location: Nucleus {ECO:0000269|PubMed:11161810}. Note=Associates with nucleosomes in euchromatin and is largely excluded from constitutive heterochromatin. {ECO:0000250}.
Interaction partners:
- Non-histone chromosomal protein HMG-14
- Non-histone chromosomal protein HMG-17
- Zinc finger protein 219
Sequence:
MPKRKAAGQGDMRQEPKRRSARLSAMLVPVTPEVKPKRTSSSRKMKTKSDMMEENIDTSAQAVAETKQEAVVEEDYNENAKNGEAKITEAPASEKEIVEVKEENIEDATEKGGEKKEAVAAEVKNEEEDQKEDEEDQNEEKGEAGKEDKDEKGEEDGKEDKNGNEKGEDAKEKEDGKKGEDGKGNGEDGKEKGEDEKEEEDRKETGDGKENEDGKEKGDKKEGKDVKVKEDEKEREDGKEDEGGNEEEAGKEKEDLKEEEEGKEEDEIKEDDGKKEEPQSIV
Protein: Potassium inwardly rectifying channel DIR (Q95UP7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003822}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003822}.
Interaction partners:
Sequence:
MYILLFRFRYRQTRFSSRRVRKRVVFKHEGCNVVQGNVAKRRRRYLQDIFTTLVDAQWRWTLLVFAASFVFSWAFFGFIWWIIAYAHNDLEYTNLKNQSPDLVANITHTVCVTQVSNMMSAFLYSVETQTTIGYGNRYVTEECPEAIFTMCIQCITGVFIQAFMVGIVFAKLSRPKKRAQTLLFSRNAVICHRDGVPCLMFRVGDMRKSHIIEAHVRAQIIRKKVTKEGEVLPFYQQELHIGADGGEDRLMFIWPTTIVHKIDRNSPLYMLSASDMLKERFEVVVMLEGVIESTGMTTQARSSYLPSEVLWGHRFVNVVSFRKETGEYEVDYTLFNNTYDVDTPLCSAKQLDELKSEYSKSAKCVNAPFADRTLSASLFQRIASAASVDHLDPASDESLDSGRLQIRSHSIPNGVLASELSR
Protein: Protein MON2 homolog (Q09853)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for traffic between late Golgi and early endosomes. Required for endocytosis and maintenance of vacuolar structure (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Late Golgi. {ECO:0000250}.
Interaction partners:
- Protein dop1
- Cell division control protein 42 homolog
- Guanine nucleotide exchange factor MSS4 homolog
- Rho guanine nucleotide exchange factor gef1
- Guanine nucleotide exchange factor subunit ric1
- Protein scd2/ral3
- Rho guanine nucleotide exchange factor scd1
- GTP-binding protein rho1
- Probable Rho-type GTPase-activating protein 4
- Serine/threonine-protein kinase shk1/pak1
Sequence:
MSLYDSLLSNLQSINVDTRKKNADLKKLADGSLKFLYTNKNLSQDSLVSKLKGNEAFYKPFLFCCAKKIERHIYISLNSIQLLAINDALSPDILESLFNSLNAVIQLGQDSQLRVLQIIPIICTHYAASMKLPILISLFRICFNLHNSKNSVVSNAAAATLRQIVILVFDYLDYDTLAHKQEADLFLDSLSLFKGLCSLLSAGKSESLNVDHISTTFGLELLESILVNHHRLFQIPEFQDSVRKDLLPIITASLASMSDFPVALRISRILNIIFQHYVTSLTLDIEVIFSFIISSLDNSEAAWKKALFLEVLRSIFSNTNLLYLMYTLFDGNEGRKPIIKKLVTSLSRIVNEKPSVIGVGSRVVLADTFEDYSSTSSGNPPSSMEKVSGSFTGTKPEQIIGICRATILKTPCIEQFDKQEPPIIPFAYLVYLAMCSLASISNGIADFVFQFYEDVGKKEFTLLIEGIKCENFDSKEDSTARPQNIIKCQYGLISENWTSFLVAYSTFVSSALAVELLKFCLNSYVNFVSVCTLFGLETPRDALLTTLSNKAVPSNLLSGNMTHSASSSISHNGRLSTSTMFSVEGLKEAATTIAAIASYDSNHDEKQKCFSLREILFLRCLSSIAKVVGEKMGKGWKILFETFDKADIILNRSPTSKHLSTSSLNRVNSSNSNFQDSKSFSTLMDYELVSYKNELSELMYVTSSYSQPAYMEFLESLLAVITSSSVHPIQTLTAPRQSFNEDLLSANTKNSVYKTSANRSISGGIRLLRKSSEVFYSFSILETVCSCNLDRFLDSKLDHSGWSLISKSLSEVFKIINVAPELRTRAANCLANILVDVASRLSNENSPDSYAFQEIFFESLGMLLPVTEVSDNTSRGVEYDISTIGLEALVSILETVGHHVLHGWQYVFEMLRFNCLNGATCFGSEKGAKIVRLAFSCLQLICTDFLASLDTSNYLDLMDTLLVFCRQLEDANVSLTAVGLFWNVSDTLKNMFSTSDFSCAYNSVEDLYAFTSMKSKEILPEVLWIMLLVHLADLCENSWASVRNGAAQILFRIFNSQCSKLGTNAWASCCQLVIMKLLHSQPIQNVSDVNNKKDEDDHEQTSCLIISGIADVFSENMSLLLNVNGILDVLEEAFQLMLRLHSDIYPKICISNFKALRELSFSISEFGKENATFTLLIKLVFINWGRFCEVSFSERRLANISQEGLTLLIESVVFLLKAYNFGIEEIKDSLLQVRKAVFYEESTSFALDVDFLSSLQLAVESLTDLLISKFKLNHLVLELWSDVLTYAFNEEKTIRASLPTLICLSKKIFENAENVVENHSLDFLNRGTMQHMFESLLVPMRLKYRCPKASRVNQSTLPIWVLASKCFVRLMINCFKDLKGSDAIEDAEKMQCLFLLTVEATNSIISPNADYEYVWSLEDVFENEDVSSLKQLHNLWKPHLQLNCLSDEVAQYYITLCKGSFYYQMRNTEDMVISRSNLDIQKEAARNFFPSTESPVSNRRQRIAVDCFSILLDDYNSSYEHVSLTIRPILQSRLCWSLKRYVADKSVSGYLPLSKSQEMDMSTVAECLNNHPSLYSNPIHYLLRKAYHTTNASPVATSLNAILGQLTLKNEVLNAI
Protein: Myomesin 2 (A0A8I6AC90)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MGLGEAALCLNIAPPLAINGGKHGALQGEISSAVLGQCLGNSSTALFVSAGFFPLECERQRAQDRLLKIISLSGISKMSLVVVPFYQKRHKHFDQSYRNIQTRYLLDRYASKKQASSQSSSQRSLTERSSSKRASSQSSAEGMTCRLCAKRMSASEEEEVENENRYRSLAASYGEAKRQRFLSELAQLEENVQLARTQARNKLDKYFLEQTVADNLALERSSFEDRLSRAPEILVRLRSHTIWERMSVRLCFTVQGFPTPVVQWYKDGSLICQAGEPGKYRIESRYGVHTLEINRADFEDTATYSAVATNPHGQVSTNAAVVVRRYRGDEEPYHSVGLPIGLPLSSVIPYTHFDVQFLEKFGVTFRREGETVTLKCTLLVTPDLKRVQPRAEWYRDDVLLKESKWTKMFFGEGQASLSFSHLNKDDEGLYTLRIVSRGGVSDHSAFMFVRDADPLVTGAPGAPMDLQCHDANRDYVIVTWKPPNTTTESPVIGYFIDKCEVGTNNWVQCNDAPVKICKYPVTGLFEGRSYVFRVRAVNNAGISRPSRISDAVAALDPVDLRRLQAIHLEGEKEIVIYQDDLEGDVQIPGPPTNVQASEVSRNYVVLSWDPPSPRGKEPLMYFIEKSAVGSGSWQRVNAQTAVRSPRYAVFDLAEGKSYVFRVLSANKHGLSDPSEITPPIQAQDMIVVPSAPGRVLASRNTKTSVVVQWDRPKHEEDLLGYYVDCCVAGTNMWEPCNHKPIGYNRFVVHGLTTGEQYIFRVKAVNAVGTSENSQESEVIKVQAALTVPSHPYGITLLNCDGHSMTLGWKVPKFSGGSAIIGYYLDKREVHHKNWHEINSSPVKERILTVEGLTEGSLYEFKIAATNLAGIGQPSDPSEHFKCEAWTAPEPGPAYDLTFCEVRDTSLVILWKAPVYSGSSPVSGYFVDFKEEDSGEWKTTSEAATPNRYLKVCDLHQGKTYVFRVRAVNASGPGKPSDTSEPVLVEARPGTKEISAGVDEEGNIYLGFDCQEMTDASQFTWCKAYEEIADEERFEVHTEGDHSKLYFKNPDKIDIGTYSVSVSDTDGVSSSFVLDEEELERLMALSNEIKNPTIPLKSELAYEIFDKGQVRFWLQAEHLSPDANFRFIINDREVSDSETHRIKCDRSTGMIEMVMDRFTIENEGTYTVQIQDGKAKNQSSLVLIGDAFRAVLEEAEFQRKEFLRKQGPHFAEYLHWDVTEECEVRLICKVANTKRETVFKWLKDDVLYETETPPPDLEKGICELLIPKLSKKDHGEYKATLKDDRGQDVSVLEVAGKVYEDMILAMSRVCGASASPLKVLCTPEGIRLQCFMKYFTEEMKVSWYHKEAKISSSEHMRIGGSEEMAWLQICEPTEKDKGKYTFEIFDGKDNHQRSLDLSGQAFDEAYAEFQQLKAAAFAEKNRGKVIGGLPDVVTIMEGKTLNLTCTVFGNPDPEVVWFKNDKDIELSEHFSVKVEQSKYVSLTIKGVTAEDSGKYSINVKNKYGGEKIDVTVSVYKHGEKIPDISAPQQAKPKLIPASTSAD
Protein: Iroquois homeobox protein Ziro1 (Iroquois-class homeodomain protein IRX-1b) (Q90YN0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108}.
Interaction partners:
Sequence:
MSFPQLGYPQFLNASQEVYGAERTGVMPSSPREGSSDNSANPATAAAAITPMLGMYANPWTVQNYSAFLPYNSAELALLSQMGSQYELKDNPGAHPPGFAVHAAPGFYPYGQYQYGDPARAKSATRETTSTLKAWLQEHKKNPYPTKGEKIMLAIITKMTLTQVSTWFANARRRLKKENKVTCCRSAEDRDGRIFDSDNEDDADKNDDEEEIDLETIDMDKAEEPRVDQNKEAANNPHAIENIETPRILSSPALKNTDSPMSSGNREQNVVKSVGEVSPGGAVCQRPGNSKPKIWSLAETATSPDNTQKLSIPSTPAGLRASPSTHPAFLSTNGIYTCQIGKLHNWASAAFLSANSLMGVRSLLSQNSNFPNHSPVTNPEKKPSSASGSPCLDSDNSSDSFSPKHNDQENVQRIESPTLASRSPFPVIHDRSHHETSQRALKTIS
Protein: 3-ketoacyl-CoA thiolase, peroxisomal (EC 2.3.1.16) (Acetyl-CoA C-myristoyltransferase) (EC 2.3.1.155) (Acetyl-CoA acyltransferase) (EC 2.3.1.9) (Beta-ketothiolase) (Peroxisomal 3-oxoacyl-CoA thiolase) (P09110)
Organism: Homo sapiens (Human)
Function: Responsible for the thiolytic cleavage of straight chain 3-keto fatty acyl-CoAs (3-oxoacyl-CoAs). Plays an important role in fatty acid peroxisomal beta-oxidation. Catalyzes the cleavage of short, medium, long, and very long straight chain 3-oxoacyl-CoAs.
Subcellular location: Peroxisome {ECO:0000269|PubMed:22057399, ECO:0000269|PubMed:25538232}. Note=Transported into peroxisomes following association with PEX7. {ECO:0000269|PubMed:22057399, ECO:0000269|PubMed:25538232}.
Interaction partners:
- Peroxisomal multifunctional enzyme type 2
- Peroxisomal bifunctional enzyme
- Peroxisomal acyl-coenzyme A oxidase 1
- Trifunctional enzyme subunit alpha, mitochondrial
- Peroxisomal targeting signal 2 receptor
- Peroxisomal acyl-coenzyme A oxidase 3
- Short-chain specific acyl-CoA dehydrogenase, mitochondrial
- Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial
- Hydroxymethylglutaryl-CoA synthase, mitochondrial
- Hydroxymethylglutaryl-CoA synthase, cytoplasmic
Sequence:
MQRLQVVLGHLRGPADSGWMPQAAPCLSGAPQASAADVVVVHGRRTAICRAGRGGFKDTTPDELLSAVMTAVLKDVNLRPEQLGDICVGNVLQPGAGAIMARIAQFLSDIPETVPLSTVNRQCSSGLQAVASIAGGIRNGSYDIGMACGVESMSLADRGNPGNITSRLMEKEKARDCLIPMGITSENVAERFGISREKQDTFALASQQKAARAQSKGCFQAEIVPVTTTVHDDKGTKRSITVTQDEGIRPSTTMEGLAKLKPAFKKDGSTTAGNSSQVSDGAAAILLARRSKAEELGLPILGVLRSYAVVGVPPDIMGIGPAYAIPVALQKAGLTVSDVDIFEINEAFASQAAYCVEKLRLPPEKVNPLGGAVALGHPLGCTGARQVITLLNELKRRGKRAYGVVSMCIGTGMGAAAVFEYPGN
Protein: Single-stranded nucleic acid binding R3H protein (Q93YN3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MAAMSDKEAMVDPFLVEALQNPRHRLTILRMELDIQKFFQSPEQQQYEFQPLPTSYLRLIAHRVAQHYGLFTTALEGGGVDGSGNRILATKTVESRYPYVCLSEIPVKQPEIHGRPEGFKIAIKPRPNRGAGGSGSGSGVEKNLLRSVEERKEEYDKARARIFNSPSSSDSEDSSTRAPPPPYPRLDSKHNTACPSRNETEVVVNYNSNPVDVERNGVIRDSGRTSRVAIIRDREKDRYDPDYDRNRYVRVAPPVQNFNPIPIPLPFHDAIFPQMPRTQASLNYGHPLNPAMTAPSYTEWPSATMTYAQTLNASDVHHFRHPNP
Protein: Methyl-CpG-binding domain-containing protein 9 (AtMBD9) (MBD09) (EC 2.3.1.48) (Histone acetyl transferase MBD9) (Methyl-CpG-binding protein MBD9) (Q9SGH2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcriptional regulator that acts as a histone acetyltransferase. Mediates the acetylation of histone H3 and H4 of target loci (e.g. FLC). Involved in an auxin-independent regulation of shoot branching and flowering time.
Subcellular location: Nucleus {ECO:0000269|PubMed:19419532}.
Interaction partners:
- Protein PHOTOPERIOD-INDEPENDENT EARLY FLOWERING 1
- Transcription initiation factor TFIID subunit 14b
- Actin-related protein 6
- SWR1-complex protein 4
- SWR1 complex subunit 2
- RuvB-like protein 1
- SWR1 complex subunit 6
- Actin-related protein 4
- Phosphotransferases/inositol or phosphatidylinositol kinase
- Phosphatidylinositol 3-and 4-kinase family protein with FAT domain-containing protein
Sequence:
MEPTDSTNEQLGDTKTAAVKEESRSFLGIDLNEIPTGATLGGGCTAGQDDDGEYEPVEVVRSIHDNPDPAPGAPAEVPEPDRDASCGACGRPESIELVVVCDACERGFHMSCVNDGVEAAPSADWMCSDCRTGGERSKLWPLGVKSKLILDMNASPPSDAEGYGAEETSDSRKHMLASSSCIGNSFDYAMMHSSFSSLGRGHASLEASGLMSRNTKMSMDALGSHNLGFGFPLNLNNSSLPMRFPSLDPSELFLQNLRHFISERHGVLEDGWRVEFRQPLNGYQLCAVYCAPNGKTFSSIQEVACYLGLAINGNYSCMDAEIRNENSLLQERLHTPKRRKTSRWPNNGFPEQKGSSVSAQLRRFPFNGQTMSPFAVKSGTHFQAGGSLSSGNNGCGCEEAKNGCPMQFEDFFVLSLGRIDIRQSYHNVNVIYPIGYKSCWHDKITGSLFTCEVSDGNSGPIFKVTRSPCSKSFIPAGSTVFSCPKIDEMVEQNSDKLSNRRDSTQERDDDASVEILLSEHCPPLGDDILSCLREKSFSKTVNSLRSEVDSSRVDFDKNLSYDQDHGVEIGDIVVEEDSLSDAWKKVSQKLVDACSIVLKQKGTLNFLCKHVDRETSEINWDTMNEKDNVILSLSKFCCSLAPCSVTCGEKDKSEFAAVVDALSRWLDQNRFGLDADFVQEMIEHMPGAESCTNYRTLKSRSSSSVPITVAEGALVVKPKGGENVKDEVFGEISRKAKKPKLNGGHGVRNLHPPPGRPMCLRLPPGLVGDFLQVSEVFWRFHEILGFEEAFSPENLEQELINPVFDGLFLDKPGKDDKRSEINFTDKDSTATKLFSLFDESRQPFPAKNTSASELKEKKAGDSSDFKISDSSRGSCVGALLTRAHISLLQVLICELQSKVAAFVDPNFDSGESRSRRGRKKDDSTLSAKRNKLHMLPVNEFTWPELARRYILSLLSMDGNLESAEIAARESGKVFRCLQGDGGLLCGSLTGVAGMEADSMLLAEAIKKISGSLTSENDVLSVEDDDSDGLDATETNTCSGDIPEWAQVLEPVKKLPTNVGTRIRKCVYEALERNPPEWAKKILEHSISKEIYKGNASGPTKKAVLSLLADIRGGDLVQRSIKGTKKRTYISVSDVIMKKCRAVLRGVAAADEDKVLCTLLGRKLLNSSDNDDDGLLGSPAMVSRPLDFRTIDLRLAAGAYDGSTEAFLEDVLELWSSIRVMYADQPDCVDLVATLSEKFKSLYEAEVVPLVQKLKDYRKLECLSAEMKKEIKDIVVSVNKLPKAPWDEGVCKVCGVDKDDDSVLLCDTCDAEYHTYCLNPPLIRIPDGNWYCPSCVIAKRMAQEALESYKLVRRRKGRKYQGELTRASMELTAHLADVMEEKDYWEFSAEERILLLKLLCDELLSSSLVHQHLEQCAEAIIEMQQKLRSLSSEWKNAKMRQEFLTAKLAKVEPSILKEVGEPHNSSYFADQMGCDPQPQEGVGDGVTRDDETSSTAYLNKNQGKSPLETDTQPGESHVNFGESKISSPETISSPGRHELPIADTSPLVTDNLPEKDTSETLLKSVGRNHETHSPNSNAVELPTAHDASSQASQELQACQQDLSATSNEIQNLQQSIRSIESQLLKQSIRRDFLGTDASGRLYWGCCFPDENPRILVDGSISLQKPVQADLIGSKVPSPFLHTVDHGRLRLSPWTYYETETEISELVQWLHDDDLKERDLRESILWWKRLRYGDVQKEKKQAQNLSAPVFATGLETKAAMSMEKRYGPCIKLEMETLKKRGKKTKVAEREKLCRCECLESILPSMIHCLICHKTFASDDEFEDHTESKCIPYSLATEEGKDISDSSKAKESLKSDYLNVKSSAGKDVAEISNVSELDSGLIRYQEEESISPYHFEEICSKFVTKDCNRDLVKEIGLISSNGIPTFLPSSSTHLNDSVLISAKSNKPDGGDSGDQVIFAGPETNVEGLNSESNMSFDRSVTDSHGGPLDKPSGLGFGFSEQKNKKSSGSGLKSCCVVPQAALKRVTGKALPGFRFLKTNLLDMDVALPEEALRPSKSHPNRRRAWRVFVKSSQSIYELVQATIVVEDMIKTEYLKNEWWYWSSLSAAAKISTLSALSVRIFSLDAAIIYDKPITPSNPIDETKPIISLPDQKSQPVSDSQERSSRVRRSGKKRKEPEGS
Protein: Electrogenic aspartate/glutamate antiporter SLC25A12, mitochondrial (Solute carrier family 25 member 12) (F1LX07)
Organism: Rattus norvegicus (Rat)
Function: Mitochondrial electrogenic aspartate/glutamate antiporter that favors efflux of aspartate and entry of glutamate and proton within the mitochondria as part of the malate-aspartate shuttle. Also mediates the uptake of L-cysteinesulfinate by mitochondria in exchange of L-glutamate and proton. Can also exchange L-cysteinesulfinate with aspartate in their anionic form without any proton translocation.
Subcellular location: Mitochondrion inner membrane {ECO:0000305|PubMed:4436323, ECO:0000305|PubMed:486467}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MAVKVHTTKRGDPHELRNIFLQYASTEVDGEHYMTPEDFVQRYLGLYNDPNSNPKIVQLLAGVADQTKDGLISYQEFLAFESVLCAPDSMFIVAFQLFDKSGNGEVTFENVKEIFGQTIIHHHIPFNWDCEFIRLHFGHNRKKHLNYVEFTQFLQELQLEHARQAFALKDKSKSGMISGLDFSDVMVTIRSHMLTPFVEENLVSAAGGSTSHQVSFSYFNAFNSLLNNMELVRKIYSTLAGTRKDIEVTKEEFASAITYGVVTPINVGILYFINNVHISTGRLTLADIERIAPLAEGALPYNLAELQRQQSPGLGRPIWLQIAESAYRFTLGSVAGAVGATAVYPIDLVKTRMQNQRGTGSVVGELMYKNSFDCFKKVLRYEGFFGLYRGLIPQLIGVAPEKAIKLTVNDFVRDKFTRRDGSIPLPAEILAGGCAGGSQVIFTNPLEIVKIRLQVAGEITTGPRVSALNVLQDLGLFGLYKGAKACFLRDIPFSAIYFPVYAHCKLLLADENGHVGGINLLTAGAMAGVPAASLVTPADVIKTRLQVAARAGQTTYSGVIDCFRKILREEGPSAFWKGTAARVFRSSPQFGVTLVTYELLQRWFYIDFGGLKPSGSEPTPKSRIADLPPANPDHIGGYRLATATFAGIENKFGLYLPKFKSPGVAAAQPKVAAAAQ
Protein: Transcriptional activator CadC (Membrane-integrated pH sensor CadC) (P23890)
Organism: Escherichia coli (strain K12)
Function: Regulates the lysine- and pH-dependent expression of the lysine decarboxylase CadA and the cadaverine-lysine antiporter CadB. At low external pH, and in the presence of external lysine, CadC activates transcription of the cadBA operon by binding directly to two sites, Cad1 and Cad2, within the cadBA promoter region (Pcad). Preferentially binds to AT-rich regions within the Cad1 promoter.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:24946151, ECO:0000269|PubMed:7830562}; Single-pass membrane protein {ECO:0000269|PubMed:24946151}. Note=Membrane insertion requires the SecA translocase. {ECO:0000269|PubMed:24946151}.
Interaction partners:
- Lysine-specific permease LysP
- Cadaverine/lysine antiporter
- Arsenical resistance operon repressor
- Inducible lysine decarboxylase
Sequence:
MQQPVVRVGEWLVTPSINQISRNGRQLTLEPRLIDLLVFFAQHSGEVLSRDELIDNVWKRSIVTNHVVTQSISELRKSLKDNDEDSPVYIATVPKRGYKLMVPVIWYSEEEGEEIMLSSPPPIPEAVPATDSPSHSLNIQNTATPPEQSPVKSKRFTTFWVWFFFLLSLGICVALVAFSSLDTRLPMSKSRILLNPRDIDINMVNKSCNSWSSPYQLSYAIGVGDLVATSLNTFSTFMVHDKINYNIDEPSSSGKTLSIAFVNQRQYRAQQCFMSIKLVDNADGSTMLDKRYVITNGNQLAIQNDLLESLSKALNQPWPQRMQETLQKILPHRGALLTNFYQAHDYLLHGDDKSLNRASELLGEIVQSSPEFTYARAEKALVDIVRHSQHPLDEKQLAALNTEIDNIVTLPELNNLSIIYQIKAVSALVKGKTDESYQAINTGIDLEMSWLNYVLLGKVYEMKGMNREAADAYLTAFNLRPGANTLYWIENGIFQTSVPYVVPYLDKFLASE
Protein: Lipoprotein lipase (LPL) (EC 3.1.1.34) (A0A060VY20)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Cell membrane {ECO:0000256|RuleBase:RU362020}; Peripheral membrane protein {ECO:0000256|RuleBase:RU362020}; Extracellular side {ECO:0000256|RuleBase:RU362020}. Secreted {ECO:0000256|RuleBase:RU362020}. Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498, ECO:0000256|RuleBase:RU362020}. Note=Newly synthesized LPL binds to cell surface heparan proteoglycans and is then released by heparanase. Subsequently, it becomes attached to heparan proteoglycan on endothelial cells. Locates to the plasma membrane of microvilli of hepatocytes with triglyceride-rich lipoproteins (TRL). Some of the bound LPL is then internalized and located inside non-coated endocytic vesicles. {ECO:0000256|RuleBase:RU362020}.
Interaction partners:
- triacylglycerol lipase
- Uncharacterized protein
- AAA+ ATPase domain-containing protein
- Diacylglycerol kinase iota-like domain-containing protein
- Phosphatidic acid phosphatase type 2/haloperoxidase domain-containing protein
- Diacylglycerol kinase
- Phosphatidic acid phosphatase type 2/haloperoxidase domain-containing protein
- Diacylglycerol kinase
- Uncharacterized protein
- Diacylglycerol kinase
Sequence:
MGKENTYLVTVWIILANICASFSSTPEQTLFGNNNSTEWLEDFTDIVSKFSLRTAEVPDDDLCYIVPGQPLTIPECEFNPETQTFVVIHGWTVTGLFESWVPKLVTALYEREPKANVIVVDWLTRAQQHYPTSAAYTKLVGRDVAKFVNWLQKTLDYPWEKIHLLGYSLGAHVAGIAGFLTNHKVSRITGLDPAGPTFEHADNQTTLSPDDALFVDVLHTNTRGSPDRSIGIQRPVGHVDIYPNGGTFQPGCDLQNTMMMIATTGIHNMDQIVKCSHERSIHLFIDSLVNAAEHQTMAYRCSSKEAFMKGMCLNCRKNRCNKVGYGVNKVRLPRSTKMYLKTRETMPFKLFHYQVKVHFFSSEKLDYTEQPMKISLYGTHDEKTDIPYIMPFLNTNSTVSFLLTTDVDIGELLMVKLRWEKDAYFSWSDWWGNSNFHIRKMRVKAGETQSKVIFSAKDGEFAYLVRGKDDAVFVKSKEDNMSRKEKTMHRLKMQGSLFKKNTA
Protein: Microtubule-associated protein TORTIFOLIA1 (Microtubule-associated protein SPIRAL2) (Protein CONVOLUTA) (Q9T041)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plant-specific microtubule-associated protein (MAP) that regulates the orientation of cortical microtubules and the direction of organ growth. Determines microtubule organization by modulating microtubule severing.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15324671, ECO:0000269|PubMed:15557095, ECO:0000269|PubMed:18577573}. Note=Bound to microtubules.
Interaction partners:
- Protein SPIRAL1
- Peptidyl-prolyl cis-trans isomerase FKBP12
- Katanin p60 ATPase-containing subunit A1
- Peptide deformylase 1A, chloroplastic/mitochondrial
- Peroxidase 60
- sn-2 acyl-lipid omega-3 desaturase
- CLIP-associated protein
- Tubulin alpha-4 chain
- Tubulin alpha-2 chain
- Protein KINESIN LIGHT CHAIN-RELATED 1
Sequence:
MSTPTTSGSAAKPTRPARSSSLATRSCSNSGSLTSFQAMVELKQKILTSISKLADRDTYQIAVEDLEKTIQSLTPETLPMFLNCLYDSCSDPKPAVKKECLHLLSYVCSLHCDSTAAHLTKIIAQIVKRLKDSDSGVRDACRDTIGALSGIYLKGKEEGTNTGSASLAVGLFVKPLFEAMGEQNKVVQSGASMCMARMVESAASPPVTSFQKLCPRICKLLSNSSFLAKASLLPVVSSLSQVGAIAPQSLESLLESIHDCLGSTDWVTRKAAAETLTALASHSSGLIKEKTDSTITVLETCRFDKIKPVRESVTEALQLWKKISGKYVDGASDDSKLSASEQLGSEKNGEKRSNLADLMKKEASDGSTLSPDSASKGKGCFPEKAVGLLKKKAPVLSDKDFNPEFFQRLERRQSVEVVVPRRCKNNDEEESGLDDLNAMGSSNRLKNTQADDKQVKGRFDGNGSQARTSGDDKAGVVNGKETPGHHAPVSNTDNQSEGSFTSNRGNWSAIQRQLLQLERQQTNLMNMLQEFIGGSHDSMVTLEGRVRGLERIVEDMARDLSISSGRRANLTAGFGKYNSFANYPTGKYNGRAPGERGSQTDGAMRGRMWNSDMADDWFIPPHAASRNGQAGPRRSPRSEQYENEHMGNGRRGWDNKASGTIRFGEGPSARSVWQASKDEATLEAIRVAGEDGAVPRPTRVAVAPEAEAMGDDDNEGQERDPIWVSWSNAMHSLRVGDIDAAYAEVLCAGDQHLVIKLMDKTGPSLDQMSNEIANEALNFISQFLLDHSLYDICLSWSQQLLELVLQDGADTFGVPMELKTEILYNLQDACSTMDPPEDWEGPAPEQLVVQLASVWEIDLQQFDK
Protein: ERC protein 2 (O15083)
Organism: Homo sapiens (Human)
Function: Thought to be involved in the organization of the cytomatrix at the nerve terminals active zone (CAZ) which regulates neurotransmitter release. Seems to act together with BSN. May recruit liprin-alpha proteins to the CAZ.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12923177}. Synapse {ECO:0000269|PubMed:12923177}. Presynaptic active zone {ECO:0000269|PubMed:12923177}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12923177}. Note=In neurons, localized to synapses, and colocalizes with PCLO. Localized to the active zone of presynaptic density (By similarity). {ECO:0000250}.
Interaction partners:
- Regulating synaptic membrane exocytosis protein 1
- Pericentrin
- Calmodulin-like protein 6
- Calmodulin-like protein 3
- Calmodulin-like protein 5
- Calmodulin-like protein 4
- Calmodulin-1
- Gamma-tubulin complex component 3
- Regulating synaptic membrane exocytosis protein 2
- Gamma-tubulin complex component 2
Sequence:
MYGSARTITNLEGSPSRSPRLPRSPRLGHRRTSSGGGGGTGKTLSMENIQSLNAAYATSGPMYLSDHEGVASTTYPKGTMTLGRATNRAVYGGRVTAMGSSPNIASAGLSHTDVLSYTDQHGGLTGSSHHHHHQVPSMLRQVRDSTMLDLQAQLKELQRENDLLRKELDIKDSKLGSSMNSIKTFWSPELKKERVLRKEEAARMSVLKEQMRVSHEENQHLQLTIQALQDELRTQRDLNHLLQQESGNRGAEHFTIELTEENFRRLQAEHDRQAKELFLLRKTLEEMELRIETQKQTLNARDESIKKLLEMLQSKGLPSKSLEDDNERTRRMAEAESQVSHLEVILDQKEKENIHLREELHRRSQLQPEPAKTKALQTVIEMKDTKIASLERNIRDLEDEIQMLKANGVLNTEDREEEIKQIEVYKSHSKFMKTKIDQLKQELSKKESELLALQTKLETLSNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKGTLAGEIRDMKDMLEVKERKINVLQKKIENLQEQLRDKDKQLTNLKDRVKSLQTDSSNTDTALATLEEALSEKERIIERLKEQRERDDRERLEEIESFRKENKDLKEKVNALQAELTEKESSLIDLKEHASSLASAGLKRDSKLKSLEIAIEQKKEECSKLEAQLKKAHNIEDDSRMNPEFADQIKQLDKEASYYRDECGKAQAEVDRLLEILKEVENEKNDKDKKIAELESLTLRHMKDQNKKVANLKHNQQLEKKKNAQLLEEVRRREDSMADNSQHLQIEELMNALEKTRQELDATKARLASTQQSLAEKEAHLANLRIERRKQLEEILEMKQEALLAAISEKDANIALLELSASKKKKTQEEVMALKREKDRLVHQLKQQTQNRMKLMADNYDDDHHHYHHHHHHHHHRSPGRSQHSNHRPSPDQDDEEGIWA
Protein: N-terminal amidohydrolase 1, isoform C (N-terminal amidohydrolase 1, isoform D) (SP2637) (Q7KIS4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Protein N-terminal glutamine amidohydrolase
- Arginyl-tRNA--protein transferase 1
- E3 ubiquitin-protein ligase UBR1
Sequence:
MVLVLNGVLQDDCPMDTNSLFLQHPVYRDYAQQLHSIQAKSVGPVGLLYVGQREMAASAPHDKHVNIIGADDATTCIIVVVRHSGSGAVALAHFDGSGVDEAVCTMVSRVQELAVGYPEGRIELQLIGGYRDAKGYGEDVFFSIMQSFHNHLLEIDLTQACVGELNTMMRGEINCPIIYGVGVNIKTGEIFPASFPDRGPDRELRDARIFMGAQSVLDIYDSSLGMLRIGPFNYDPLRGADLWLSQTDEFLLQHLSSSPDVEPPHFAPQTRATIRFIQENQFPAVTVFRDNRPRYFRRDDATGFWVLVRY
Protein: Phosphorylase b kinase regulatory subunit (F1M1C9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004342, ECO:0000256|RuleBase:RU364123}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004342, ECO:0000256|RuleBase:RU364123}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004342, ECO:0000256|RuleBase:RU364123}.
Interaction partners:
- Phosphorylase b kinase gamma catalytic chain, liver/testis isoform
- Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoform
- Phosphorylase b kinase regulatory subunit
- Calmodulin-1
- Phosphorylase b kinase regulatory subunit alpha, skeletal muscle isoform
- Calmodulin-like protein 3
- Calmodulin-like protein 4
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit alpha
- Glycogen phosphorylase, liver form
Sequence:
MRSRSNSGVRLDGYARLVQQTILCYQNPVTGLLSASHDQKDAWVRDNIYSILAVWGLGMAYRKNADRDEDKAKAYELEQNVVKLMRGLLQCMMRQVDKVEKFKHTQSTKDSLHAKYNTATCSTVVGDDQWGHLQVDATSLFLLFLAQMTASGLRIIFTLDEVAFIQNLVFYIEAAYKVADYGMWERGDKTNQGIPELNASSVGMAKAALEAIDELDLFGAHGGRKSVIHVLPDEVEHCQSILFSMLPRASTSKEIDAGLLSIISFPAFAVEDVHLVNVTKNEIISKLQGRYGCCRFLRDGYKTPREDPHRLHYDPAELKLFENIECEWPVFWTYLIIDGVFNGDAVQVQEYREALEGILIRGKDGIHLVPELYAIPPDKVDEEYKNPHTVDRIPLGKLPHLWGQSLYILSSLLAEGFLATGEIDPLNRRFSTSVKPDVVVQVAVLAENSHIKGLLKQHGINVQSIADVHPIRVQPGRILSHIYAKLGQNKNMKLSGRPYRHIGVLGTSKLYVIRNHIFTFTPQVKRANMVVRGGVCLY