wanglab/gogpt-training-data huggingface dataset:
Protein: Malate-2H(+)/Na(+)-lactate antiporter (P54571)
Organism: Bacillus subtilis (strain 168)
Function: Couples proton uptake and Na(+) efflux to the substrate-product malate/lactate antiport, in an electroneutral malate-2H(+)/Na(+)-lactate exchange. Plays a role in supporting growth to high density on malate at reduced protonmotive force.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- NAD-dependent malic enzyme 1
- Na
- Citrate/malate-proton symporter
- Aspartate ammonia-lyase
- L-asparaginase 1
Sequence:
MKDVRLPTLFEIIIVLGVFLALVLSFTVFLDLPIQLALFVSWFIAMLLGIRLGYSYKDLQNAIVHGISNGLEAVLILVSVGALIGTWIAGGVVPTLIYYGLEFIHPSIFLLATLIICSIMSVATGTSWGTVGTAGIAMIAIGEGLGIPLPLVAGAILSGAYFGDKLSPLSDSTVLASSLSKVDVLAHVRAMLYLSIPAYVITAILFTVVGFMYGGKNIDLDKVEFLKSSLQNTFDIHIWMLIPAVLVIVLLAMKKPSMPVIVIGALLGAIWAVVFQGMDIAHAIATAYNGFSIKTDVEFLNGLLNRGGIVGMLDSLVVIIFGLGFGGLLEKLGVLKVIVSTFEKKLTSAGNVTLSTLIVAFLANIFGCAMYVSLILTPKIMEDSYDRLHLDRRVLSRNSEVGGTLTSGMVPWSDNGIYMAGILGVSTFSYLPFMWLSFVAIGLAIIYGYTGKFIWYTKNNTVKAEKLG
Protein: Long-chain-fatty-acid--AMP ligase FadD26 (FAAL) (EC 6.2.1.59) (Acyl-AMP synthetase) (Q7TXM1)
Organism: Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Function: Catalyzes the activation of long-chain fatty acids as acyl-adenylates (acyl-AMP), which are then transferred to the multifunctional polyketide synthase PpsA for further chain extension. Catalyzes the adenylation of the long-chain fatty acids eicosanoate (C20) or docosanoate (C22), and potentially the very-long-chain fatty acid lignocerate (C24). Involved in the biosynthesis of phthiocerol dimycocerosate (DIM A) and phthiodiolone dimycocerosate (DIM B).
Interaction partners:
Sequence:
MPVTDRSVPSLLQERADQQPDSTAYTYIDYGSDPKGFADSLTWSQVYSRACIIAEELKLCGLPGDRVAVLAPQGLEYVLAFLGALQAGFIAVPLSTPQYGIHDDRVSAVLQDSKPVAILTTSSVVGDVTKYAASHDGQPAPVVVEVDLLDLDSPRQMPAFSRQHTGAAYLQYTSGSTRTPAGVIVSHTNVIANVTQSMYGYFGDPAKIPTGTVVSWLPLYHDMGLILGICAPLVARRRAVLMSPMSFLRRPARWMQLLATSGRCFSAAPNFAFELAVRRTSDQDMAGLDLRDVVGIVSGSERIHVATVRRFIERFAPYNLSPTAIRPSYGLAEATLYVAAPEAGAAPKTVRFDYEQLTAGQARPCGTDGSVGTELISYGSPDPSSVRIVNPETMVENPPGVVGEIWVHGDHVTMGYWQKPKQTAQVFDAKLVDPAPAAPEGPWLRTGDLGVISDGELFIMGRIKDLLIVDGRNHYPDDIEATIQEITGGRAAAIAVPDDITEQLVAIIEFKRRGSTAEEVMLKLRSVKREVTSAISKSHSLRVADLVLVSPGSIPITTSGKIRRSACVERYRSDGFKRLDVAV
Protein: Core-binding factor subunit beta homolog bro-1 (BROther (Drosophila tx factor partner) homolog) (Q95ZL9)
Organism: Caenorhabditis elegans
Function: Transcriptional cofactor. Required for controlling cell proliferation in the seam cells, a stem cell-like lineage, acting in concert with Runt-related transcription factor 1 rnt-1, perhaps by repressing expression of cyclin-dependent kinase inhibitor cki-1. Represses expression of rnt-1. Regulates male tail development. May play a role in vulval and/or uterine morphogenesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17933794}. Nucleus {ECO:0000269|PubMed:17933794}.
Interaction partners:
- Runt-related transcription factor rnt-1
- Cullin-5
- RNA polymerase II transcription factor SIII p18 subunit
- Cytochrome c oxidase subunit 4
- BRO1 domain-containing protein
- Elongin-C
- Protein arginine N-methyltransferase 1
- Elongin-C
- Elongin-C
- Homeodomain-interacting protein kinase 1
Sequence:
MKRTTTDQQSSFQTDYFLTQLSHFTEAKFSLFEHAPLSERRERFRVHVERDEMPLTFCKTGINIPVKLEWSQTNGNEISFRSRPLVFNGIWVKVIGAMNSESLEGRVRFERFQREKRDRVISETFVFPEVEEEPIGLTDAEIAALRRDGLPI
Protein: GTP cyclohydrolase 1 (EC 3.5.4.16) (GTP cyclohydrolase I) (GTP-CH-I) (P30793)
Organism: Homo sapiens (Human)
Function: Positively regulates nitric oxide synthesis in umbilical vein endothelial cells (HUVECs). May be involved in dopamine synthesis. May modify pain sensitivity and persistence. Isoform GCH-1 is the functional enzyme, the potential function of the enzymatically inactive isoforms remains unknown.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12176133, ECO:0000269|PubMed:16778797, ECO:0000269|PubMed:2463916}. Nucleus {ECO:0000269|PubMed:16778797}.
Interaction partners:
- GTP cyclohydrolase 1 feedback regulatory protein
- 6-pyruvoyl tetrahydrobiopterin synthase
- Vacuolar protein sorting-associated protein VTA1 homolog
- Inosine triphosphate pyrophosphatase
- Tyrosine 3-monooxygenase
- Molybdenum cofactor biosynthesis protein 1
- Alkaline phosphatase, germ cell type
- Alkaline phosphatase, placental type
- Intestinal-type alkaline phosphatase
- Alkaline phosphatase, tissue-nonspecific isozyme
Sequence:
MEKGPVRAPAEKPRGARCSNGFPERDPPRPGPSRPAEKPPRPEAKSAQPADGWKGERPRSEEDNELNLPNLAAAYSSILSSLGENPQRQGLLKTPWRAASAMQFFTKGYQETISDVLNDAIFDEDHDEMVIVKDIDMFSMCEHHLVPFVGKVHIGYLPNKQVLGLSKLARIVEIYSRRLQVQERLTKQIAVAITEALRPAGVGVVVEATHMCMVMRGVQKMNSKTVTSTMLGVFREDPKTREEFLTLIRS
Protein: G-protein-signaling modulator 3 (Activator of G-protein signaling 4) (G18.1b) (Protein G18) (Q9Y4H4)
Organism: Homo sapiens (Human)
Function: Interacts with subunit of G(i) alpha proteins and regulates the activation of G(i) alpha proteins.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15096500}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Epidermal growth factor-like protein 8
- Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial
Sequence:
MEAERPQEEEDGEQGPPQDEEGWPPPNSTTRPWRSAPPSPPPPGTRHTALGPRSASLLSLQTELLLDLVAEAQSRRLEEQRATFYTPQNPSSLAPAPLRPLEDREQLYSTILSHQCQRMEAQRSEPPLPPGGQELLELLLRVQGGGRMEEQRSRPPTHTC
Protein: U-box domain-containing protein 9 (EC 2.3.2.27) (Plant U-box protein 9) (RING-type E3 ubiquitin transferase PUB9) (Q9SRT0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Functions as an E3 ubiquitin ligase (By similarity). May be involved in the abscisic acid-mediated signaling pathway, at least during germination.
Subcellular location: Nucleus {ECO:0000269|PubMed:18552232}. Cell membrane {ECO:0000269|PubMed:18552232}. Note=Relocates from nucleus to plasma membrane when phosphorylated.
Interaction partners:
- Transmembrane protein
- INCREASED PETAL GROWTH ANISOTROPY 1-like protein 1
Sequence:
MAKTGVFDSDPTAIAKAKELKREMKKLLIKIDDEDDLGVQTIDQLQDALSALREATMRKMAKSSSLEMLETVSCPEEFRCPLSNELMRDPVVLASGQTYDKLFIQKWLSSGNRTCPKTQQVLPHTALTPNLLIREMISKWCKKNGLETKSQYHPNLVNEDETVTRSDREIFNSLLCKVSSSNLQDQKSAAKELRLLTRKGTEFRALFGESPDEITRLVNPLLHGSNPDEKLQEDVVTTLLNISIHDDSNKKLVCENPNVIPLLIDALRRGTVATRSNAAAAIFTLSALDSNKVLIGKSGILKPLIDLLEEGNPLAIKDVAAAIFTLCIAHENRSRAVRDGAVRVLGKKISNGLYVDELLAILAMLVTHWKAVEELGELGGVSWLLKITRESECKRNKENAIVILHTICFSDRTKWKEIKEEENAHGTITKLSREGTSRAQRKANGILDRLRKAMNLTHTA
Protein: Succinate-CoA ligase subunit beta (EC 6.2.1.-) (Q499V7)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
AIAAQAGKLLRERSLRPRLLAVRSQAGHLTPRRWLNLQEYQSKKLMSEHGVRVQRFFVASTAKEAQEAAKRLNAKEIVLKAQILAGGRGKGVFDSGLKGGVHLTKDPKVVGQLAQQMIGYNLATKQTPKEGVKVNKVMVAEALDISRETYLAILMDRSHNGPVLVGSPQGGVDIEEVAASSPELIFKEQIDIFEGIKDSQAQRMAENLGFLGSLKNQAADQIKKLYHLFLKIDATQVEVNPFGETPEGQVVCFDAKINFDDNAEFRQKDIFAMDDKSENEPIENEAARYDLKYIGLDGNIACFVNGAGLAMATCDIIFLNGGKPANFLDLGGGVKESQVYQAFKLLTSDPKVEAILVNIFGGIVNCAIIANGITKACQELELKVPLVVRLEGTNVQEAQNILKSSGLPITSAVDLEDAAKKAVASVAKK
Protein: Ubiquitin carboxyl-terminal hydrolase 17-like protein A (USP17-A) (EC 3.4.19.12) (Deubiquitinating enzyme 1) (Ubiquitin carboxyl-terminal hydrolase DUB-1) (Ubiquitin thioesterase DUB-1) (Ubiquitin-specific-processing protease DUB-1) (Q61068)
Organism: Mus musculus (Mouse)
Function: Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes. Has deubiquitinating enzyme activity for DNAH5, suggesting a role in the regulation of DNAH5 degradation by the ubiquitin-proteasome pathway. Has growth-suppressing activity; induces arrest in G1 phase upon controlled expression.
Interaction partners:
- Zinc finger protein 352
- 2 cell stage variable group member 1A
Sequence:
MVVALSFPEADPALSSPDAPELHQDEAQVVEELTVNGKHSLSWESPQGPGCGLQNTGNSCYLNAALQCLTHTPPLADYMLSQEHSQTCCSPEGCKLCAMEALVTQSLLHSHSGDVMKPSHILTSAFHKHQQEDAHEFLMFTLETMHESCLQVHRQSKPTSEDSSPIHDIFGGWWRSQIKCLLCQGTSDTYDRFLDIPLDISSAQSVKQALWDTEKSEELCGDNAYYCGKCRQKMPASKTLHVHIAPKVLMVVLNRFSAFTGNKLDRKVSYPEFLDLKPYLSEPTGGPLPYALYAVLVHDGATSHSGHYFCCVKAGHGKWYKMDDTKVTRCDVTSVLNENAYVLFYVQQANLKQVSIDMPEGRINEVLDPEYQLKKSRRKKHKKKSPFTEDLGEPCENRDKRAIKETSLGKGKVLQEVNHKKAGQKHGNTKLMPQKQNHQKAGQNLRNTEVELDLPADAIVIHQPRSTANWGRDSPDKENQPLHNADRLLTSQGPVNTWQLCRQEGRRRSKKGQNKNKQGQRLLLVC
Protein: Alpha/beta superfamily hydrolase, putative (AFU_orthologue AFUA_2G16580) (Q5B6Q6)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Small ribosomal subunit protein eS1
- 40S ribosomal protein S3
- 40S ribosomal protein S25
- 40S ribosomal protein S15
- 40S ribosomal protein S10b
- 40S ribosomal protein S7
Sequence:
MRIVQPTLAISGALALAVPSSAQNMSFGANNFYHSPIATAIAGNLFILNNISLTDARPAIVVSHPMDAVKEQSANLYATKLAEAGFVTVSLDLPFWGGSEGEPRNVVSPEPYAEAFSAAFVSVDRERIGAVGICGSGGFLISAAKIDPRIKAVAAASMHDMGAVNRHGLQHSQFLAARKRVMASAAQQRWVEVDGGATQYTSGTLEVLTANSTDIERGTTFTAPRGASSRPRAQRGI
Protein: CB1 cannabinoid receptor-interacting protein 1 (CRIP-1) (Q96F85)
Organism: Homo sapiens (Human)
Function: Suppresses cannabinoid receptor CNR1-mediated tonic inhibition of voltage-gated calcium channels.
Interaction partners:
- Cannabinoid receptor 1
Sequence:
MGDLPGLVRLSIALRIQPNDGPVFYKVDGQRFGQNRTIKLLTGSSYKVEVKIKPSTLQVENISIGGVLVPLELKSKEPDGDRVVYTGTYDTEGVTPTKSGERQPIQITMPFTDIGTFETVWQVKFYNYHKRDHCQWGSPFSVIEYECKPNETRSLMWVNKESFL
Protein: LIM homeobox transcription factor 1-beta (LIM/homeobox protein 1.2) (LMX-1.2) (LIM/homeobox protein LMX1B) (O88609)
Organism: Mus musculus (Mouse)
Function: Transcription factor involved in the regulation of podocyte-expressed genes. Essential for the specification of dorsal limb fate at both the zeugopodal and autopodal levels.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
Interaction partners:
- LIM domain-binding protein 1
- Paired box protein Pax-2
- Nuclear receptor subfamily 4 group A member 2
- T-cell leukemia homeobox protein 3
- Homeobox protein Nkx-2.2
Sequence:
MDIATGPESLERCFPRGQTDCAKMLDGIKMEEHALRPGPATLGVLLGSDCPHPAVCEGCQRPISDRFLMRVNESSWHEECLQCAACQQALTTSCYFRDRKLYCKQDYQQLFAAKCSGCMEKIAPTEFVMRALECVYHLGCFCCCVCERQLRKGDEFVLKEGQLLCKGDYEKEKDLLSSVSPDESDSVKSEDEDGDMKPAKGQGSQSKGSGDDGKDPRRPKRPRTILTTQQRRAFKASFEVSSKPCRKVRETLAAETGLSVRVVQVWFQNQRAKMKKLARRHQQQQEQQNSQRLGQEVLSSRMEGMMASYTPLAPPQQQIVAMEQSPYGSSDPFQQGLTPPQMPGNDSIFHDIDSDTSLTSLSDCFLGSSDVGSLQARVGNPIDRLYSMQSSYFAS
Protein: Heme oxygenase 1 (HO-1) (EC 1.14.14.18) [Cleaved into: Heme oxygenase 1 soluble form] (P09601)
Organism: Homo sapiens (Human)
Function: Catalyzes the oxidative cleavage of heme at the alpha-methene bridge carbon, released as carbon monoxide (CO), to generate biliverdin IXalpha, while releasing the central heme iron chelate as ferrous iron. Affords protection against programmed cell death and this cytoprotective effect relies on its ability to catabolize free heme and prevent it from sensitizing cells to undergo apoptosis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19556236, ECO:0000269|PubMed:22419571, ECO:0000269|PubMed:27184847}; Single-pass type IV membrane protein {ECO:0000255}; Cytoplasmic side {ECO:0000269|PubMed:22419571}.
Interaction partners:
- Biliverdin reductase A
- Nuclear factor erythroid 2-related factor 2
- NADPH--cytochrome P450 reductase
- Ferrochelatase, mitochondrial
- Flavin reductase
- Ceruloplasmin
- Frataxin, mitochondrial
- Hephaestin
- Kelch-like ECH-associated protein 1
- NAD
Sequence:
MERPQPDSMPQDLSEALKEATKEVHTQAENAEFMRNFQKGQVTRDGFKLVMASLYHIYVALEEEIERNKESPVFAPVYFPEELHRKAALEQDLAFWYGPRWQEVIPYTPAMQRYVKRLHEVGRTEPELLVAHAYTRYLGDLSGGQVLKKIAQKALDLPSSGEGLAFFTFPNIASATKFKQLYRSRMNSLEMTPAVRQRVIEEAKTAFLLNIQLFEELQELLTHDTKDQSPSRAPGLRQRASNKVQDSAPVETPRGKPPLNTRSQAPLLRWVLTLSFLVATVAVGLYAM
Protein: Variant surface glycoprotein (VSG, atypical), putative (Q38CN1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
Sequence:
MQRLALALLVIIGPKLAAGENMVYGENRAEHAALCAFIRMADRAVAVPTVEPLDKDDYNYIQELNFTLSPAEWQAKFYKEAERKTVHDNADSAGIKDADEAEFWDDWKAAAEALKQGEDNQKVKQAVTPELTKTAKQLAAVQLAAIALEVKQLLKRYPNVNPEAAKYQSASPTAAIMAAALGQGDAKATNIDASKPFSATVSGNRQTVCEVKTSGVRPATALATLTCICHKDNGNPVTDGACTEKAEASTAWTSSATPPDSSDYQKLAKSCGAPPQEPITTTELEHAIATVRALIHTDGTNGYLGAFRGTDCSGASNSGMCIKFTGLVASPEKENELQWLTTIKTIATNLKHLEQAKAAAATAAISHSRALAAAMDKLSTKFSDSVETAINVRCETHNKSKTECLGAKCKWGGKKEDDGPCTPTEDQVAEQPARSTETEGAPKEGAAATGCARHGDDKTACENDKTGDKQNCAWRIGKDNEDDKEKEKFRSSSFLLNKQLALSMVAEFVSLIASQNLKIIRVLLIFMKIMNIS
Protein: Splicing factor 3A, putative (Q584V9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- U2 small nuclear ribonucleoprotein B, putative
- PRP1 splicing factor N-terminal domain-containing protein
- Spliceosome-associated protein, putative
- Sm protein B
- SURP motif domain-containing protein
- Probable eukaryotic initiation factor 4A
- Uncharacterized protein
- Pre-mRNA-processing factor 19
- Splicing factor 3B subunit 10
- Small nuclear ribonucleoprotein SmD1
Sequence:
MFGGVLEKIRLFEADIERHIDSIVQQLLIEDISNKRHQLLRDYFIIQQAEAVEPIAEKLLDIYLDQDDIVSAQEAPAEGEAVYSNALKEFEARIADIREYHRTFRDVPTVKCELDLPDVNALDNVFTLAERYGSCLDLEAHYHRYSNFMLSTSKRALETNHTVGTAWPGRVEYLTFVTSVINIILNDVDPYRKVYGFWSYKEFVEELLKYLVHFHKRVLVMESDVLESTLAKCDADAEEFWSKLVEHKKSVVTISSTAVALPGTSGKSVSSLHAPAPLRRYVKAFALWPITYVESVTPSEIEKPPSLEEVKAVVHIEAKIVVLLQTLLFEHLQETEKVLLRDYSKTVEELEWERDNMQAEFLRSVEEAKKRCATTVEGSVVQAAQHEVAVAFAPEEGKEVPTANGVLAPGTKAGDTNDQLLDSDGKPVARWLVCLQQLHKRFYCEVCGGTVYIGPKVFKDHFGAERHAEGLRRLGVTLHLKNYEGISSIRKVIEMRDKVMGNSRSLRKRIHADQEDEEMQDAQGNVITAGAYRKFQMSRKTG
Protein: UTP--glucose-1-phosphate uridylyltransferase (EC 2.7.7.9) (Q9XUS4)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MAQRHVSVGCFSTFSEAEAKSSEEWKTSTKLEALGSMEGELAHLLSTCKPETLNHNKTELSGFRNLFARFLRAKPTVDWSKIEPLPEGAIRPYKSLGHVVDKELIASQLRKLVVVKLNGGLGTSMGCKGPKSVISVRNDLTFLDLTMQQIQTLNKTYGVDVPLVLMNSFNTNEDTQKVLKKYANVKVSVHTFSQSQYPRINRETLLPIVKSLEADDNECWYPPGHGNFYEAFHNSGLLDKFLADGKEYCFLSNIDNMGATVDLSILNFVLNPSPDQTAPEFLMEVTDKTRADVKGGTLIQYEGRLMLLEIAQVPKDYVDEFKSISKFRIFNTNNLWAKLDAMRKIVVENKLEMEVIVNPKHLDRGLDVIQLETAAGAAIKSFSGAVGVNVPRSRFLPVKKTSDLLLLMSNLYDIDNGSLTLSHQRSFPTTPLVKLGSSFDKVKDYLGRFNGIPDLLELDHLTVSGDVWFGKDVSLKGTVIIIANHGDRIDIPPGSILENKIVSGNLRILEH
Protein: Perilipin (A0A8I6AJS7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Lipid droplet {ECO:0000256|ARBA:ARBA00004502}.
Interaction partners:
Sequence:
MGGAARRYLTVAGPPCCAVILDRADLLVSQLSCSASLYSRRKNGISSSGSTTVAVANTYACKGLDRMEARLPILNQPTSEIVANARGAVTGAKDVVTTTMAGAKDSVASTVSGVVDKTKGAVTGSVERTKSVVNGGIDTVLGMVQLMSSGVENAISKSELLVDQYLPLTQKELEMEAKKVEGFDMVQKQRYYERLESLSTKICTRAYHQALGRIKDAKQKGQETISQLHSTVHLIEFARKNVHSANQKIQDKLSVSWVEWKRIVGYDDTDESHCAEHIESHTLSMARNLTQQLHTTCQTLLFNVQGLPQNIQDQAKHLGVMAGDIYSAFRNVTSFKEVSDGVLTSSKGQLQKMKESLDEVMDYLVNNTPLNWLVGPFYPQSTEVDKASLKVQQSELTTQ
Protein: Tomosyn, isoform C (Tomosyn, isoform F) (Tomosyn, isoform I) (Q9VYK6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004202}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Syntaxin-1A
- Syntaxin-4
- Synaptosomal-associated protein 25
- Complexin
- Synaptosomal-associated protein
- Synaptobrevin
- Unc-13, isoform E
- Gamma-soluble NSF attachment protein
- Gamma-soluble NSF attachment protein
- HL02043p
Sequence:
MKKFTFKGVLDGFRQSVQPQATRQEQEIQEQLKADHFTLKKTFRHGFPYSPTSFAFDPVQKLLAIGDKSGYIRILGRPGVDAHAKHEGESECAVLFAQFLVNEGALVTVTADDTIHLWSIRQKTPRIVQSLKFQRERVTCIHLPVGSKWLYVGTEKGNIHVVHIDTFALSGYIINWNKAIEVVRTSHPGAVIALCDNPLDANKLLIAFECGLLVLWDLKAKCAELRWQAAEAVKSLAWHYEGKYFVSSHTDGSICSWPTKPQAKPQSQVCPHAKINKDGNAEKCKPIYKVDLKSSATGETFTIFSGGMPSEKGSKSNCITVMVGKATTVLEMEHAVCDFITLCENPWPCETQEPYAIAVLLQYDLVLIDLLTPGFPCFESPYPMDLHESPVTCCTYLTDCPSDLVPAFYSVGRTTTSKKSCFSEREWPISGGEWSPASCSYSEIVITGHQDGSLKFWDSGAGTLQILYKLKTAKMFEKPRSHVAHSHPESDNPLAVHLIFLCSESRRLCVAGAMGQVMLFKFRKVESTSEVLVLEIPILYENFDDIYGTSPECDFLTGHQVQKAESSDSDKTAECSLKVRNGAQRKPPGFQSQLVCLTTGPNRRNVQVTSLCISSSYGLMAYGTEYGLVIIDIIQKICLLSVACPDLYGAHDPYSRTPKSPKRIENKEEQSRSPSSDQLNDTTSPDSPSLEFVPEAGETSAHDGVATATSSRPSSPDPVVNSARETLLSGSAAATAAAAASAAVMMAKSPQRDDAAPKELQDRRKSMSWKTFNLKRQLSKVNMKIGGLNVNTDMESLKNSSIFYTPKEVSPEAATPPATEEEATPEGKEDESLDDGEMATNAGAAAAASPSPAVRGKFRSSTTDSPDEGASSSIASGIRRVDFEQPAGVEVERPNNLPLADAPAPLKPARQKFKEKSRDQRLLSVPNIKYQPRDSRGGARNLKNDVSPLMGGGGGGGGVVGASSGIGGSVAGGKKIHKLDGTFSRSRSSSMSSIDMSSSESVTCLAFIESYAKRNDILTLVPTLWIGTSFGSILTLFITMPERDVRKSQPVLITINGGPVVRLKGSITSMSFLDSYGSIIPYTFETWRDEKRDNKDRTPTKSSSRTSPTFTPTTANTLSNTSVAGGASAGGGAGGGGGAGGGAASGGAAAGGPAGGGAGAGSAAGAAGGVGSGVTSGGGMSSSSASSSGISGSVSTGLETLTDRQYIVIASEKQTKVFDVANQCCINRIQLSEMDFAVKAETITMKDGSCLATYLSNGHLMVHSLPSLKLLLDTDFLPLMELSFQTKCKQGIVDPMLSIWGQQIIVHEDTTQISKIFCFSHKGHGLYMASPTEIQKFTISSEFCQFILEMMGELYTVHEMPEQPKEGFFKGLFGGGAKLLDREELFGEQSGKPNRSVARHIPGPNLEQLGQRASTAASEISRAHQLAMERGEKLNLLEERAERMANTAQDFSGTAHQLMLKYKDKKWYQL
Protein: Probable trehalose-phosphate phosphatase E (AtTPPE) (EC 3.1.3.12) (Trehalose 6-phosphate phosphatase) (Q67X99)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Removes the phosphate from trehalose 6-phosphate to produce free trehalose. Trehalose accumulation in plant may improve abiotic stress tolerance (By similarity).
Interaction partners:
- Trehalase
- Alpha,alpha-trehalose-phosphate synthase 1
- Probable alpha,alpha-trehalose-phosphate synthase 10
- Probable alpha,alpha-trehalose-phosphate synthase 2
- Probable alpha,alpha-trehalose-phosphate synthase 4
- Probable alpha,alpha-trehalose-phosphate synthase 11
- Probable alpha,alpha-trehalose-phosphate synthase 3
- Alpha,alpha-trehalose-phosphate synthase 6
- Alpha,alpha-trehalose-phosphate synthase 5
- Sucrose synthase 6
Sequence:
MVRFIEENITKMLETKAISNSEVLYVGGDDGDTSPTTKVLHDFQINSGGGLIRSWVDSMRACSPTRPKSFNSQSCWIKEHPSALNMFEEILHKSEGKQIVMFLDYDGTLSPIVDDPDRAFMSKKMRNTVRKLAKCFPTAIVSGRCREKVSSFVKLTELYYAGSHGMDIKGPEQGSKYKKENQSLLCQPATEFLPVINEVYKKLVENTQSIPGAKVENNKFCASVHFRCVEENKWSDLAHQVRSVLKNYPKLMLTQGRKVLEIRPIIKWDKGKALEFLLESLGYDNCTDVFPIYIGDDRTDEDAFKILRDKKQGLGILVSKYAKETNASYSLQEPDEVMVFLERLVEWKQSRCGA
Protein: Renin (EC 3.4.23.15) (Angiotensinogenase) (Renin-like aspartic protease) (Renin-like aspartic protease EOC51) (SVAP EOC51) (Snake venom aspartic protease EOC51) (Q18DC9)
Organism: Echis ocellatus (Ocellated saw-scaled viper)
Function: Renin is a highly specific endopeptidase, whose only known function is to generate angiotensin I from angiotensinogen in the plasma, initiating a cascade of reactions that produce an elevation of blood pressure and increased sodium retention by the kidney (Probable). This protein is also found in snake venom and shown to specifically cleave human and porcine angiotensinogen into angiotensin I. It does not have general protease activity, no cleavage of alpha or beta casein. May be directly responsible for elevation of blood pressure in the victims of envenomation.
Subcellular location: Secreted {ECO:0000269|PubMed:28734982}.
Interaction partners:
Sequence:
MLRSWEFVLLISCFLCFSSDALQRISLKKMPSIRETLQEMGMKVADVLPSLKHRISYLDEGLHNKTASTILTNFRDTQYYGEISIGTPAQIFKVVFDTGSSNLWVPSRQCSPLYSACVSHNRYDSSESSTYKPKGTKITLTYAQGYIKGFFSQDIVRVADIPIIQFFTEAIALPSIPFIFARFDGVLGMGYPKQAIGGVIPVFDNIMSEKVLSENVFSVYYSRHSESNTGGEIILGGSDPSHYTGDFHYVSTSREGYWHVDLKGVSIENKIVLCHDGCTATIDTGTSFISGPASSISVLMETIGATLSDGDYVIDCKKINLLPDITFHLGDMTYSLSSSTYVLKFSDETECTVAFMAVDIPPPLGPLWLLGATFIKQYYIEFDRQNNRIGFATSF
Protein: Protein POLAR LOCALIZATION DURING ASYMMETRIC DIVISION AND REDISTRIBUTION (Q6NQ99)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Regulates asymmetric cell division (ACD), especially in stomatal-lineage cells. Acts as a stomatal lineage scaffold which regulates subcellular localization and transient polarization of kinases (e.g. ASK7/BIN2 and ASK3/SK12) involved in ACD in a BASL-dependent manner. Promotes the differentiation of both pavement cells and stomata.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21963668, ECO:0000269|PubMed:30429609}. Cytoplasm, cell cortex {ECO:0000269|PubMed:21963668, ECO:0000269|PubMed:30429609}. Note=Localized throughout the plasma membrane in asymmetric cell division (ACD) precursors (PubMed:30429609). Transient polar localization and segregation unevenly (distal to the newly divided meristemoid and parallel to the division plane) during meristemoid asymmetric divisions in a BASL-dependent manner (PubMed:21963668, PubMed:30429609). Present in the cytoplasm of meristemoids and cell periphery in stomatal lineage ground cells (SLGCs), in a polarized pattern (PubMed:21963668, PubMed:30429609). {ECO:0000269|PubMed:21963668, ECO:0000269|PubMed:30429609}.
Interaction partners:
- F18B13.13 protein
- Protein TOO MANY MOUTHS
- Golgin
- Protein indeterminate-domain 16
- Protein BREAKING OF ASYMMETRY IN THE STOMATAL LINEAGE
- LRR receptor-like serine/threonine-protein kinase ERECTA
- Protein EPIDERMAL PATTERNING FACTOR 2
- Protein QUA-QUINE STARCH
- Dynamin-related protein 3A
- 3-ketoacyl-CoA thiolase 1, peroxisomal
Sequence:
MEGSRRRRGDGCTIVQCYTPRRFVGRWLSGLRSSKGKRDAGEEQEDDTRRYQLAPIRCSTSLNQLVMQDNKQNCRLNKSKEPETNTFESQSRESPLEVGIGSFLLYLVVASKTELDKMTNLRMQMEMFLLNAKEQLQKKDTPMSSNEASGFQFSPQEFSNLASSIFQESSSSVLQEEYTEFEVSEPEDYRRGTDCNSKLQAEVGRLPLGEKAEDRQTKHQIQRQCKLKDNEVTKSHIPEMVVSDERYGVCPYELDKKLHELLETRQQEELVKLETALNRVERRLQEKETEVSWWKDAARLLAQRVPESSRSGLEWCNPDSSTCSERSVPRSYEACSIHRTSFSR
Protein: Probable isoaspartyl peptidase/L-asparaginase 2 (EC 3.4.19.5) (L-asparagine amidohydrolase 2) [Cleaved into: Isoaspartyl peptidase/L-asparaginase 2 subunit alpha; Isoaspartyl peptidase/L-asparaginase 2 subunit beta] (Q8GXG1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts in asparagine catabolism and also in the final steps of protein degradation via hydrolysis of a range of isoaspartyl dipeptides.
Interaction partners:
- Asparagine synthetase 1
- Asparagine synthetase 3
- Asparagine synthetase 2
- Aspartate aminotransferase, cytoplasmic isozyme 2
- Aspartate aminotransferase, mitochondrial
- Aspartate aminotransferase, cytoplasmic isozyme 1
- Aspartate carbamoyltransferase, chloroplastic
- Aspartate aminotransferase 3, chloroplastic
- Aspartate aminotransferase, chloroplastic
- Adenylosuccinate synthetase, chloroplastic
Sequence:
MGGWAIAVHGGAGIDPNLPAERQEEAKQLLTRCLNLGIIALRSNVSAIDVVELVIRELETDPLFNSGRGSALTEKGTVEMEASIMDGTKRRCGAVSGITTVKNPISLARLVMDKSPHSYLAFSGAEDFARKQGVEIVDNEYFVTDDNVGMLKLAKEANSILFDYRIPPMGCAGAAATDSPIQMNGLPISIYAPETVGCVVVDGKGHCAAGTSTGGLMNKMMGRIGDSPLIGAGTYASEFCGVSCTGEGEAIIRATLARDVSAVMEYKGLNLQEAVDYVIKHRLDEGFAGLIAVSNKGEVVCGFNSNGMFRGCATEDGFMEVAIWE
Protein: Methylmalonate-semialdehyde/malonate-semialdehyde dehydrogenase [acylating], mitochondrial (MMSDH) (EC 1.2.1.27) (Aldehyde dehydrogenase family 6 member A1) (Malonate-semialdehyde dehydrogenase [acylating]) (Q07536)
Organism: Bos taurus (Bovine)
Function: Plays a role in valine and pyrimidine metabolism. Binds fatty acyl-CoA.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q02253}.
Interaction partners:
- 3-hydroxyisobutyrate dehydrogenase, mitochondrial
- Propionyl-CoA carboxylase beta chain, mitochondrial
- 4-aminobutyrate aminotransferase, mitochondrial
- Trifunctional enzyme subunit beta, mitochondrial
- Peroxisomal bifunctional enzyme
- Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
- Propionyl-CoA carboxylase alpha chain, mitochondrial
- Ethylmalonyl-CoA decarboxylase
- 4-trimethylaminobutyraldehyde dehydrogenase
- Aldehyde dehydrogenase, mitochondrial
Sequence:
MAAVAVAAAAAALRARILQVSSKVNSSWQPASSFSSSSVPTVKLFIDGKFIESKSDKWIDIHNPATNEVIGRVPESTKAEMDAAVSSCKRTFPAWADTSILSRQQVLLRYQQLIKENLKEIARLIMLEQGKTLADAEGDVFRGLQVVEHACSVTSLMLGDTMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLFQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNQAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAILVGEAKKWLPELVERAKKLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRSIKVKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETDTLDEAIKIVNDNPYGNGTAIFTTNGATARKYSHLVDVGQVGVNVPIPVPLPMFSFTGSRASFRGDTNFYGKQGIQFYTQLKTITSQWKEEDASLSSPAVVMPTMGR