wanglab/gogpt-training-data huggingface dataset:
Protein: Cis-aconitate decarboxylase (CAD) (EC 4.1.1.6) (Aconitate decarboxylase) (Aconitate decarboxylase 1) (Cis-aconitic acid decarboxylase) (Immune-responsive gene 1 protein) (P54987)
Organism: Mus musculus (Mouse)
Function: Cis-aconitate decarboxylase that catalyzes production of itaconate and is involved in the inhibition of the inflammatory response. Acts as a negative regulator of the Toll-like receptors (TLRs)-mediated inflammatory innate response by stimulating the tumor necrosis factor alpha-induced protein TNFAIP3 expression via reactive oxygen species (ROS) in LPS-tolerized macrophages. Involved in antimicrobial response of innate immune cells; ACOD1-mediated itaconic acid production contributes to the antimicrobial activity of macrophages by generating itaconate, leading to alkylation of proteins, such as TFEB. Involved in antiviral response following infection by flavivirus in neurons: ACOD1-mediated itaconate production inhibits the activity of succinate dehydrogenase, generating a metabolic state in neurons that suppresses replication of viral genomes. Plays a role in the embryo implantation.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:19014335}.
Interaction partners:
- Aspartate aminotransferase, mitochondrial
- C-type lectin domain family 4 member E
- Tumor necrosis factor
- Interleukin-1 beta
- C-X-C motif chemokine 10
Sequence:
MMLKSVTESFAGMIHGLKVNHLTDGIIRRSKRMILDSLGVGFLGTGTEVFHKVTQYSKIYSSNTSSTVWGRPDFRLPPTYAAFVNGVAVHSMDFDDTWHPATHPSGAVLPVLTALSEALPQIPKFSGLDLLLAFNVGIEVQGRLMHFSKEAKDIPKRFHPPSVVGTLGSAAAASKFLGLSLTKCREALAIAVSHAGAPIANAATQTKPLHIGNAAKHGMEATFLAMLGLQGNKQILDLGSGFGAFYANYSPEDLPSLDSHIWLLDQQDVAFKSFPAHLATHWVADAAAAVRKHLVTPERALFPADHIERIVLRIPDVQYVNRPFPDSEHEARHSFQYVACASLLDGSITVPSFHSQQVNRPQVRELLKKVKLEHPPDNPPSFDTLYCEISITLKDGTTFTERSDTFYGHWRKPLSQEDLRNKFRANASKMLCRDTVESLITVVEKLEDLEDCSVLTRLLKGPSVQDEASKLSSMSSFDHTTLPRFTNI
Protein: Poly(A) ribonuclease POP2 (EC 3.1.13.4) (CCR4-associated factor 1) (P39008)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acts as probably catalytic component of the CCR4-NOT core complex, which in the nucleus seems to be a general transcription factor, and in the cytoplasm the major mRNA deadenylase involved in mRNA turnover. In vitro, POP2 has 3'-exoribonuclease activity with a preference for poly(A) RNAs, but also degrades poly(U) and poly(C) RNAs. Is part of a glucose-sensing system involved in growth control in response to glucose availability.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11239395}. Nucleus {ECO:0000269|PubMed:11239395}.
Interaction partners:
- General negative regulator of transcription subunit 5
- General negative regulator of transcription subunit 3
- Protein CAF40
- General negative regulator of transcription subunit 4
- General negative regulator of transcription subunit 2
- ATP-dependent RNA helicase DHH1
- CCR4-Not complex 3'-5'-exoribonuclease subunit Ccr4
- General negative regulator of transcription subunit 1
- DNA-directed RNA polymerase II subunit RPB1
- Protein CAF130
Sequence:
MQSMNVQPRVLAVGGEQFFSQRQASEQHQQQNMGPQVYSPKVNRARMFPQGMPVNTINGSVNQEMNNAYLLKQKNEPLLTQQQQQQQQQQQPFNIGTPVSVASLPPGLNVLQQQQQQQQQQQQQQQGVGLNRPLASQLPKHLTNQSMPPIFLPPPNYLFVRDVWKSNLYSEFAVIRQLVSQYNHVSISTEFVGTLARPIGTFRSKVDYHYQTMRANVDFLNPIQLGLSLSDANGNKPDNGPSTWQFNFEFDPKKEIMSTESLELLRKSGINFEKHENLGIDVFEFSQLLMDSGLMMDDSVTWITYHAAYDLGFLINILMNDSMPNNKEDFEWWVHQYMPNFYDLNLVYKIIQEFKNPQLQQSSQQQQQQQYSLTTLADELGLPRFSIFTTTGGQSLLMLLSFCQLSKLSMHKFPNGTDFAKYQGVIYGIDGDQ
Protein: Galectin (G5EC10)
Organism: Caenorhabditis elegans
Interaction partners:
- Serine protease K12H4.7
- Galectin
- DUF19 domain-containing protein
- Putative serine protease F56F10.1
- Putative phospholipase B-like 2
- EGF-like domain-containing protein
- Galectin
- EGF-like domain-containing protein
- Galectin
Sequence:
MAAPILNPSVPGTFALPFGVRSGLQIAVNGLVKHKKDFVVNLISGGNIALHVNFRFEKQKIVAINAKIDNAWGNEISHANPLHHDQAFDLQIRVYPGYFHITTNGVLLGDFPHRLPFESIQAINLEGKVHINNVQYSQFH
Protein: Type III effector protein popp2 (Q8Y125)
Organism: Ralstonia nicotianae (strain ATCC BAA-1114 / GMI1000) (Ralstonia solanacearum)
Interaction partners:
- Type III effector protein avra
- Type III effector protein gala6
Sequence:
MKVSSANAGVPASSADNTSARPSQTNADTTPLGRRRRAPDDAPGSPPARRQRQDSPEDSAQTMFRRAGMTSLPPSPATSEHVPLLDNRPTLERMGVDHPLPGRTWYETGHTTASLADRTSTASAAQVASSSRSAGPATAARPQPTRTSAGQQATVGRLRTQVTGFLSGALGKLQALSAQNMDPELAQFRVLDVDRAIMPLLIVAENARNPGLNLVPLHMDMAEDEEVRTQPPMAGSRHIAEFVASARPGRYRAVIDDGSHTRAADIRKDASGTSVIVVDPLRKEKDESAYVDYADNVNMEFGEHAKCAFIPVDIQKSFFDCRILSLSLALKMHDKDDAFAAFHETLRNGGDPSHHVSRAQQTEELGATLVLDGAPLVDARMMKHGQAASSVSRYLGNHPEQSTVPVNKRNETLGERTTRHLVKRKVRNRADSEGRVTSGETKEITFSNSVEQKRIALLNRAASYVNSAPPPVVMRMAKLLQDSLLDTN
Protein: Direct IAP-binding protein with low pI (A0A0S2Z5P6)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
MAALKSWLSRSVTSFFRYRQCLCVPVVANFKKRCFSELIRPWHKTVTIGFGVTLCAVPIAQAVYTLTSLYRQYTSLLGKMNSEEEDEVWQVIIGARAEMTSKHQEYLKLETTWMTAVGLSEMAAEAAYQTGADQASITARNHIQLVKLQVEEVHQLSRKAETKLAEAQIEELRQKTQEEGEERAESEQEAYLRED
Protein: 6-phosphogluconate dehydrogenase, decarboxylating 2 (EC 1.1.1.44) (P53319)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH.
Interaction partners:
- Glucose-6-phosphate 1-dehydrogenase
- 6-phosphogluconolactonase 4
- 6-phosphogluconolactonase 3
- Probable gluconokinase
- Transketolase 2
- Ribulose-phosphate 3-epimerase
- 6-phosphogluconate dehydrogenase, decarboxylating 1
- Transaldolase NQM1
- Ribose-5-phosphate isomerase
- 6-phosphogluconolactonase-like protein 1
Sequence:
MSKAVGDLGLVGLAVMGQNLILNAADHGFTVVAYNRTQSKVDRFLANEAKGKSIIGATSIEDLVAKLKKPRKIMLLIKAGAPVDTLIKELVPHLDKGDIIIDGGNSHFPDTNRRYEELTKQGILFVGSGVSGGEDGARFGPSLMPGGSAEAWPHIKNIFQSIAAKSNGEPCCEWVGPAGSGHYVKMVHNGIEYGDMQLICEAYDIMKRIGRFTDKEISEVFDKWNTGVLDSFLIEITRDILKFDDVDGKPLVEKIMDTAGQKGTGKWTAINALDLGMPVTLIGEAVFARCLSAIKDERKRASKLLAGPTVPKDAIHDREQFVYDLEQALYASKIISYAQGFMLIREAARSYGWKLNNPAIALMWRGGCIIRSVFLAEITKAYRDDPDLENLLFNEFFASAVTKAQSGWRRTIALAATYGIPTPAFSTALAFYDGYRSERLPANLLQAQRDYFGAHTFRILPECASAHLPVDKDIHINWTGHGGNISSSTYQA
Protein: Odorant-binding protein 56e, isoform B (A0A0B4LFW3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MKVFFVFAALAALSLASAGLTDSQKAEAKQRAKACVKQEGITKEQAIALRSGNFADSDPKVKCFANCFLEQTGLVANGQIKPDVVLAKLGPIAGEANVKEVQAKCDSTKGADKCDTSYLLYKCYYENHAQF
Protein: Suppressor of presenilin-2 (Q18240)
Organism: Caenorhabditis elegans
Function: Potential corepressor protein, which may affect chromatin structure and/or transcription. May participate in the transcriptional repression of the presenilin protein hop-1.
Subcellular location: Nucleus {ECO:0000269|PubMed:11114162}.
Interaction partners:
- Histone H2A.V
- Probable histone chaperone asf-1
- Nucleosome assembly protein 1-like 1
- Suppressor of presenilin protein 3
- Probable histone chaperone asf-1-like protein
- Suppressor of presenilin protein 4
Sequence:
MSEEPAAKRMKNADEFPNLRSEVAGPVKEKLIELDAIQHQLDVMSENAAEEVLKVEQIFNQKRLPIYEKRKKLTTKIDNFWQTAFLNHHLLSTAIPEEQEDLLAALRDLEVQEFEDLRSGFKIIMTFDPNEYFTNEVITKSYHLQSESPSTEITEIEWKENKKPPFPEDGDSAHTFLEWLTYAALPDSDEIAEVIKDDLYVNPLQYYVMPDMQEVEEDDIEDFLNEERGVDENGQRIPRRNISDSLKVDQDESADGQEGEDEEEEDMGEEEEDGVEEEAEGEEEEEDGAIEEEGGDENVEAHVAVNPENTAE
Protein: Polyribonucleotide nucleotidyltransferase (EC 2.7.7.8) (Polynucleotide phosphorylase) (PNPase) (P05055)
Organism: Escherichia coli (strain K12)
Function: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction. Also involved, along with RNase II, in tRNA processing. RNases II and R contribute to rRNA degradation during starvation, while RNase R and PNPase are the major contributors to quality control of rRNA during steady state growth.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01595, ECO:0000269|PubMed:16079137}. Note=Has also been isolated in association with the inner membrane.
Interaction partners:
- Ribonuclease E
- ATP-dependent RNA helicase RhlB
- RNA-binding protein Hfq
- Poly
- Transcription termination factor Rho
- Enolase
- Small ribosomal subunit protein uS15
- ATP-dependent RNA helicase SrmB
- Ribonuclease G
- Ribonuclease R
Sequence:
MLNPIVRKFQYGQHTVTLETGMMARQATAAVMVSMDDTAVFVTVVGQKKAKPGQDFFPLTVNYQERTYAAGRIPGSFFRREGRPSEGETLIARLIDRPIRPLFPEGFVNEVQVIATVVSVNPQVNPDIVAMIGASAALSLSGIPFNGPIGAARVGYINDQYVLNPTQDELKESKLDLVVAGTEAAVLMVESEAQLLSEDQMLGAVVFGHEQQQVVIQNINELVKEAGKPRWDWQPEPVNEALNARVAALAEARLSDAYRITDKQERYAQVDVIKSETIATLLAEDETLDENELGEILHAIEKNVVRSRVLAGEPRIDGREKDMIRGLDVRTGVLPRTHGSALFTRGETQALVTATLGTARDAQVLDELMGERTDTFLFHYNFPPYSVGETGMVGSPKRREIGHGRLAKRGVLAVMPDMDKFPYTVRVVSEITESNGSSSMASVCGASLALMDAGVPIKAAVAGIAMGLVKEGDNYVVLSDILGDEDHLGDMDFKVAGSRDGISALQMDIKIEGITKEIMQVALNQAKGARLHILGVMEQAINAPRGDISEFAPRIHTIKINPDKIKDVIGKGGSVIRALTEETGTTIEIEDDGTVKIAATDGEKAKHAIRRIEEITAEIEVGRVYTGKVTRIVDFGAFVAIGGGKEGLVHISQIADKRVEKVTDYLQMGQEVPVKVLEVDRQGRIRLSIKEATEQSQPAAAPEAPAAEQGE
Protein: Peripheral plastid protein 1, putative (Q8I5T1)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MIYYIRKVAINFLFLYIINFCLLHYLKECNTSNYSRILKEQNGKKYIYYNLSKKKNNGIIKGGSKHNGHLFINNYKKKRNVKYKINKYKPCSIFSFFKKKDKNDKNDKNDKTHMKDNSNLENKEKGEIGKDKEQKEKEKEKIIILKDNKKLDEKKKKELQKEEKKTKLTNVLKQNNKNKNNNNKNNNNKNNNNNNNNNNNNNNMDDTLKKDKQTELIKKDNLNNKNDVKKKKIDLNINNIDTNSRDILKNENKYKKHLENVKDKFIISLNQIFCSYMNSLDKKENFKYFFEKILQNVEKNFHTYTFIIDIEKMNNQQIKKTYMINNINCFNEIMNIIQENLYNILVFKIQYLKVKAINDIKEIISNKKNMNDYISYSNNINKIIQIYEEQLTKLCPLNYIFTLYNNFMENNNYLLNFSYQLPLYKYKNIIDSNIEYLRTFSNDLTKHKKKSLYNEIEKNKNYQSILQIIDNQQKQIEVLQEQLETSIDGINGKYSPFNCALAYRIPDTNLNISTQYVKGKFNVKVNCIPDDSLHLLGSYGFVKGLPYGNLGLSLSLNF
Protein: Zinc finger protein 777 (Q9ULD5)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional repression. Inhibits cell proliferation through CDKN1A/p21 induction by down-regulation of NIBAN1/FAM129A at low cell density.
Subcellular location: Nucleus {ECO:0000269|PubMed:25560148}.
Interaction partners:
- Zinc finger protein 212
Sequence:
MENQRSSPLSFPSVPQEETLRQAPAGLPRETLFQSRVLPPKEIPSLSPTIPRQGSLPQTSSAPKQETSGRMPHVLQKGPSLLCSAASEQETSLQGPLASQEGTQYPPPAAAEQEVSLLSHSPHHQEAPVHSPEAPEKDPLTLSPTVPETDMDPLLQSPVSQKDTPFQISSAVQKEQPLPTAEITRLAVWAAVQAVERKLEAQAMRLLTLEGRTGTNEKKIADCEKTAVEFANHLESKWVVLGTLLQEYGLLQRRLENMENLLKNRNFWILRLPPGSNGEVPKVPVTFDDVAVHFSEQEWGNLSEWQKELYKNVMRGNYESLVSMDYAISKPDLMSQMERGERPTMQEQEDSEEGETPTDPSAAHDGIVIKIEVQTNDEGSESLETPEPLMGQVEEHGFQDSELGDPCGEQPDLDMQEPENTLEESTEGSSEFSELKQMLVQQRNCTEGIVIKTEEQDEEEEEEEEDELPQHLQSLGQLSGRYEASMYQTPLPGEMSPEGEESPPPLQLGNPAVKRLAPSVHGERHLSENRGASSQQQRNRRGERPFTCMECGKSFRLKINLIIHQRNHIKEGPYECAECEISFRHKQQLTLHQRIHRVRGGCVSPERGPTFNPKHALKPRPKSPSSGSGGGGPKPYKCPECDSSFSHKSSLTKHQITHTGERPYTCPECKKSFRLHISLVIHQRVHAGKHEVSFICSLCGKSFSRPSHLLRHQRTHTGERPFKCPECEKSFSEKSKLTNHCRVHSRERPHACPECGKSFIRKHHLLEHRRIHTGERPYHCAECGKRFTQKHHLLEHQRAHTGERPYPCTHCAKCFRYKQSLKYHLRTHTGE
Protein: Gap junction delta-2 protein (Connexin-36) (Cx36) (Gap junction alpha-9 protein) (O70610)
Organism: Rattus norvegicus (Rat)
Function: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.
Subcellular location: Cell membrane; Multi-pass membrane protein. Cell junction, gap junction.
Interaction partners:
- Tight junction protein ZO-1
- Gap junction alpha-1 protein
- Mitogen-activated protein kinase 3
- Mitogen-activated protein kinase 7
- Mitogen-activated protein kinase 1
- Cyclin-dependent kinase 1
- Gap junction gamma-1 protein
- Gap junction beta-2 protein
- Multiple PDZ domain protein
- Afadin
Sequence:
MGEWTILERLLEAAVQQHSTMIGRILLTVVVIFRILIVAIVGETVYDDEQTMFVCNTLQPGCNQACYDRAFPISHIRYWVFQIIMVCTPSLCFITYSVHQSAKQRERRYSTVFLALDRDPAESIGGPGGTGGGGSGGSKREDKKLQNAIVNGVLQNTETTSKETEPDCLEVKELAPHPSGLRTAARSKLRRQEGISRFYIIQVVFRNALEIGFLVGQYFLYGFSVPGLYECNRYPCIKEVECYVSRPTEKTVFLVFMFAVSGICVVLNLAELNHLGWRKIKLAVRGAQAKRKSVYEIRNKDLPRVSVPNFGRTQSSDSAYV
Protein: L-tyrosine/L-aspartate decarboxylase (TDC/ADC) (EC 4.1.1.11) (EC 4.1.1.25) (Q60358)
Organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Function: Catalyzes the decarboxylation of L-tyrosine to produce tyramine for methanofuran biosynthesis. Can also catalyze the decarboxylation of L-aspartate to produce beta-alanine for coenzyme A (CoA) biosynthesis.
Interaction partners:
- Tyramine--L-glutamate ligase
- Probable aspartate aminotransferase
- 4-phosphopantoate--beta-alanine ligase
- Histidinol-phosphate aminotransferase
- ethyl]phenoxymethyl}furan-2-yl)methanamine synthase
- Argininosuccinate synthase
- 
- Putative asparagine synthetase 1
- Putative asparagine synthetase 2
- Adenylosuccinate synthetase
Sequence:
MRNMQEKGVSEKEILEELKKYRSLDLKYEDGNIFGSMCSNVLPITRKIVDIFLETNLGDPGLFKGTKLLEEKAVALLGSLLNNKDAYGHIVSGGTEANLMALRCIKNIWREKRRKGLSKNEHPKIIVPITAHFSFEKGREMMDLEYIYAPIKEDYTIDEKFVKDAVEDYDVDGIIGIAGTTELGTIDNIEELSKIAKENNIYIHVDAAFGGLVIPFLDDKYKKKGVNYKFDFSLGVDSITIDPHKMGHCPIPSGGILFKDIGYKRYLDVDAPYLTETRQATILGTRVGFGGACTYAVLRYLGREGQRKIVNECMENTLYLYKKLKENNFKPVIEPILNIVAIEDEDYKEVCKKLRDRGIYVSVCNCVKALRIVVMPHIKREHIDNFIEILNSIKRD
Protein: H(+)/Cl(-) exchange transporter 4 (Chloride channel protein 4) (ClC-4) (Chloride transporter ClC-4) (P51793)
Organism: Homo sapiens (Human)
Function: Strongly outwardly rectifying, electrogenic H(+)/Cl(-)exchanger which mediates the exchange of chloride ions against protons. The CLC channel family contains both chloride channels and proton-coupled anion transporters that exchange chloride or another anion for protons. The presence of conserved gating glutamate residues is typical for family members that function as antiporters.
Subcellular location: Early endosome membrane {ECO:0000250|UniProtKB:P51794}; Multi-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000269|PubMed:28972156}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:17023393, ECO:0000269|PubMed:28972156}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:28972156}; Multi-pass membrane protein {ECO:0000255}. Recycling endosome membrane {ECO:0000269|PubMed:28972156}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to late endosome membrane, lysosome membrane and recycling endosome membrane in the presence of CLCN3. {ECO:0000269|PubMed:28972156}.
Interaction partners:
- Amelogenin, X isoform
Sequence:
MVNAGAMSGSGNLMDFLDEPFPDVGTYEDFHTIDWLREKSRDTDRHRKITSKSKESIWEFIKSLLDAWSGWVVMLLIGLLAGTLAGVIDLAVDWMTDLKEGVCLSAFWYSHEQCCWTSNETTFEDRDKCPLWQKWSELLVNQSEGASAYILNYLMYILWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHVACCCGNFFSSLFSKYSKNEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTLRSINPFGNSRLVLFYVEYHTPWYMAELFPFILLGVFGGLWGTLFIRCNIAWCRRRKTTRLGKYPVLEVIVVTAITAIIAYPNPYTRQSTSELISELFNDCGALESSQLCDYINDPNMTRPVDDIPDRPAGVGVYTAMWQLALALIFKIVVTIFTFGMKIPSGLFIPSMAVGAIAGRMVGIGVEQLAYHHHDWIIFRNWCRPGADCVTPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAVTSKWVADAFGKEGIYEAHIHLNGYPFLDVKDEFTHRTLATDVMRPRRGEPPLSVLTQDSMTVEDVETLIKETDYNGFPVVVSRDSERLIGFAQRRELILAIKNARQRQEGIVSNSIMYFTEEPPELPANSPHPLKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVTRSGRLLGIITKKDVLRHMAQMANQDPESIMFN
Protein: Catechol O-methyltransferase (EC 2.1.1.6) (O88587)
Organism: Mus musculus (Mouse)
Function: Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones. Also shortens the biological half-lives of certain neuroactive drugs, like L-DOPA, alpha-methyl DOPA and isoproterenol.
Subcellular location: [Isoform Soluble]: Cytoplasm {ECO:0000250|UniProtKB:P22734}.; SUBCELLULAR LOCATION: [Isoform Membrane-bound]: Cell membrane {ECO:0000250|UniProtKB:P22734}; Single-pass type II membrane protein {ECO:0000255}; Extracellular side {ECO:0000250|UniProtKB:P22734}.
Interaction partners:
- Amine oxidase [flavin-containing] A
- Amine oxidase [flavin-containing] B
- Aromatic-L-amino-acid decarboxylase
- Dopamine beta-hydroxylase
- Cytochrome P450 1A1
- Cytochrome P450 1B1
- Phenylethanolamine N-methyltransferase
- Aldehyde dehydrogenase, dimeric NADP-preferring
- Aldehyde dehydrogenase family 3 member B3
- All-trans-retinol dehydrogenase [NAD
Sequence:
MLLAAVSLGLLLLAFLLLLRHLGWGLVAIGWFEFVQQPVHNLLMGGTKEQRILRHVQQHAKPGDPQSVLEAIDTYCSEKEWAMNVGDAKGQIMDAVIREYRPSLVLELGAYCGYSAVRMARLLPPGARLLTMEINPDYAAITQQMLDFAGLQDKVSILIGASQDLIPQLKKKYDVDTLDMVFLDHWKDRYLPDTLLLEECGLLRKGTVLLADNVIVPGTPDFLAYVRGSSSFECTHYSSYLEYMKVVDGLEKAVYQGPGSSPVKS
Protein: Aromatic amino acid transport protein AroP (Aromatic amino acid:H(+) symporter AroP) (General aromatic amino acid permease) (General aromatic transport system) (P15993)
Organism: Escherichia coli (strain K12)
Function: Permease that is involved in the active transport across the cytoplasmic membrane of all three aromatic amino acids, phenylalanine, tyrosine and tryptophan.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:3015892, ECO:0000269|PubMed:9150230}; Multi-pass membrane protein {ECO:0000269|PubMed:9150230}.
Interaction partners:
- HTH-type transcriptional regulatory protein TyrR
- Tryptophan-specific transport protein
- Tyrosine-specific transport system
- Low affinity tryptophan permease
- Aromatic-amino-acid aminotransferase
- Shikimate kinase 2
- Aromatic amino acid exporter YddG
- Phospho-2-dehydro-3-deoxyheptonate aldolase, Tyr-sensitive
Sequence:
MMEGQQHGEQLKRGLKNRHIQLIALGGAIGTGLFLGSASVIQSAGPGIILGYAIAGFIAFLIMRQLGEMVVEEPVAGSFSHFAYKYWGSFAGFASGWNYWVLYVLVAMAELTAVGKYIQFWYPEIPTWVSAAVFFVVINAINLTNVKVFGEMEFWFAIIKVIAVVAMIIFGGWLLFSGNGGPQATVSNLWDQGGFLPHGFTGLVMMMAIIMFSFGGLELVGITAAEADNPEQSIPKATNQVIYRILIFYIGSLAVLLSLMPWTRVTADTSPFVLIFHELGDTFVANALNIVVLTAALSVYNSCVYCNSRMLFGLAQQGNAPKALASVDKRGVPVNTILVSALVTALCVLINYLAPESAFGLLMALVVSALVINWAMISLAHMKFRRAKQEQGVVTRFPALLYPLGNWICLLFMAAVLVIMLMTPGMAISVYLIPVWLIVLGIGYLFKEKTAKAVKAH
Protein: Fast muscle troponin T isoform TnnT3b (Fast troponin T isoform b) (Troponin T type 3b (skeletal, fast)) (Q7ZZW4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MSDTEDVGVEEYDEEEKPKFKPSAPKIPDGDKVDFDDIQKKRQNKDLVELQALIDAHFEHRKKEEEELIALKDRIEKRRSERAEQQRIRAEKDKERQARREEERLRKEEADAKKRADEDAKKKSALSNMGSQYSSYLQKADSKRGGKKQTEREKKKKILAERRKPLNIDHMNEDKLREKAKELWDWLYSLEAEKFEHMEKLKRQKYEVTTQRKRVEELSKYSKKGAAARRRK
Protein: Mszf84 (Zinc finger protein 950) (O88244)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
EKPYECNQCGEAFVYHSHLQIHKTMHTGEKPFQCNQCDKAFVYNNHLLVHKRIHTGE
Protein: RE06111p (Q8SY24)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MALSSKNAKIAKSLVDNGMANINAVNMEGFSLLKSALKNGDAFSANFLLDQNCLLDLPSKPSSDTALHIICNYGPDNTPEIMEVVKKILQRQLNINIQNIKGETPLHIAIARRNVEMVKLLLKVPNIDINLRTYDEKCALELSLSMGDHEFLIASILLSMGARTDRTNSKTGDSLLQVFALDRHRGEKSAIFLADFADLDHINFRGLTALHIAALNNMPNLVKKLIVNGASSNLKHIDCGLKSALHIAVEANAIDALEAFVELKNKSHDIDFNCQDINGDSPLSLCLSLKRTTLVPTLIRGGSDVNGKNKNNLSPLHQSIKNEDSDISLFLLEQGADITALTENLDSALDLSIKHDLSEVVDALCRRGIALSINKNGESPLWSALEKGYEDEAKILVRHGIDTDCWDEGPEGCRQTLLHRAIDENKESVAIFLIQSQCDLDSSRQPGPNGEGGDEAQDKASPLHLCCHWGQTKVLQTLIDHGANVNLIDAESKSPLHVAIESQYDEIISILLCHPDIDLKLRDKSGNTPFATALDFRNHNAAQRILDRFPTAAEQMDIRGRNFLHLAILKDDLESVLFLLAIQVDVNSRVHDANQSSPLHLAAASQNEMITRNLILAGARMNERDAVQKLPLHIAIERGNLPAVSALIQNNADYDATDADGNNALHIAVRCAQFFIVRELLTESRVNAEATNLKGRNPLHELCRVVEDSTAGLICELFLESMPKYPINIPDMDGNTPLLLSFMRGQSPLCKILVKAGACLGTENKDGINIFNFKLATDQLLHNLLDQLPQESPWAESDYCQHCTNRFTITMRKHHCRHCGRVLCSKCSCNDVPILKFGINKPVRVCTVCFNVLQCGNGSLS
Protein: 2S albumin-like cysteine protease inhibitor (AaCI-2S) (C0HLT8)
Organism: Araucaria angustifolia (Brazilian pine tree)
Function: Cysteine protease inhibitor that likely functions in defense against insects by inhibiting cysteine proteases in the midgut of herbivore insects such as C.maculatus. Selectively inhibits cathepsin L, as well as papain, ficin and bromelain with lower efficiency. Shows antitumor activity, inhibiting the growth of prostate cancer cell lines PC3 and DU145, and the gastric cancer cell line Hs746T. No activity against cathepsin B or serine proteases (trypsin, human plasma kallikrein and elastase).
Interaction partners:
Sequence:
ERRCDPRRLSDCEDFVRGRSKGGRGEKECRLSERCCTELQKMPRECRCEAVEGMYKEAERKERGEGEQRQRLERARALPGLCSIEPSYCEIRPS
Protein: Gram-negative bacteria-binding protein 3 (Q9NHA8)
Organism: Drosophila melanogaster (Fruit fly)
Function: Involved in the recognition of invading microorganisms. Binds specifically to beta-1,3-glucan and activates the phenoloxidase cascade (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q8MU95}.
Interaction partners:
- Modular serine protease
- Serine protease persephone
- Peptidoglycan-recognition protein SA
- Spaetzle-processing enzyme
- Peptidoglycan-recognition protein SD
- Protein spaetzle
- Protein immune deficiency
Sequence:
MADALRFVAWSCCLQLLFLLLGVQGYEVPKAKIDVFYPKGFEVSIPDEEGITLFAFHGKLNEEMEGLEAGTWARDIVKAKNGRWTFRDRITALKPGDTLYYWTYVIYNGLGYREDDGSFVVNGYSGNNASPHPPVVPVSTTPWTPPADPDIDIRLGCTTPKTEVNGAPTRCAGQLVFVDEFNAAKLDPNKWKAERRFSGQPDYEFNVYVDDAPETLCLANGHVVLSTNTMKKQFKKGSGESLDLGEKCTGQANTHDCVRNGRTLNDGLPPMVTAQFSSKDFSFKYGRVEVRAKMPRAQWVTPQIWLQPRRPIYGVDDYRSGQLRIAYTRPNGGNLDLYGAAVLFADEPLRSVKNCLKPGTGNNSEDWSDSFHNYTLEWTPRELRWLVDGKEWCVQGSAKGSFSETTAAGKSLPQAQKLEEGTGLAPFDQEFYLTFGLSVGGFNEYQHEIKPWNERAPQAQKAFWKEVKKIRDHWLDEGHMKIDYVKVYSL
Protein: Nuclear receptor subfamily 2, group C, member 2, isoform CRA_a (Testicular nuclear receptor 4) (F2YGU2)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU004334}.
Interaction partners:
Sequence:
MTSPSPRIQIISTDSAVASPQRIQGSEPASGPLSVFTSLNKEKIVTDQQTGQKIQIVTAVDASGSPKQQFILTSPDGAGTGKVILASPETSSAKQLIFTTSDNLVPGRIQIVTDSASVERLLGKTDVQRPQVVEYCVVCGDKASGRHYGAVSCEGCKGFFKRSVRKNLTYSCRSNQDCIINKHHRNRCQFCRLKKCLEMGMKMESVQSERKPFDVQREKPSNCAASTEKIYIRKDLRSPLIATPTFVADKDGARQTGLLDPGMLVNIQQPLIREDGTVLLATDSKAETSQGALGTLANVVTSLANLSESLNNGDTSEIQPEDQSASEITRAFDTLAKALNTTDSSSSPSLADGIDTSGGGSIHVISRDQSTPIIEVEGPLLSDTHVTFKLTMPSPMPEYLNVHYICESASRLLFLSMHWARSIPAFQALGQDCNTSLVRACWNELFTLGLAQCAQVMSLSTILAAIVNHLQNSIQEDKLSGDRIKQVMEHIWKLQEFCNSMAKLDIDGYEYAYLKAIVLFSPDHPGLTSTSQIEKFQEKAQMELQDYVQKTYSEDTYRLARILVRLPALRLMSSNITEELFFTGLIGNVSIDSIIPYILKMETAEYNGQITGASL
Protein: Rhoptry neck protein 6 (O96229)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MQYFFLVFLAVLAKGFLRNKEHANLINSYNDIVEDINIKKEEKSSSEPPFIPIKNKIDNVHTKNNNQYNLHNNKSNKTHLTYGTHTSFLQNCTINDCVDVDNKDSEINNITKEKDDNNNNNGTKQIEEKNKINKSDLHRQNELNLQSGKNEQDINKNEKGKQDISNSNAENKKDVKEGVKELEEKKKEEKISDDHKVEENKKSDDHKVEENKKSDDHKVEENKKSDDHKIEEVKKVEEHEEDEEEDKKEKKSENKNKDENKDENDEDNDEISDEDEVDDDVEEDKNENDDIDDDKKETDKTHLEEEENEIIEKEFSDKKKNGKNKDTKKEKSKDTEKEKSKDIEKEKSKDKEKEKSKDKEKEKGKDKEKEKSKDIEKEKEKDKDIEKEKSKDTAKEKEKDKDIEKEKSKDMEKLKNKQNDEKKKDDNEKKKNDKQDIHDDNDDENDMEEIEENDDEEDEDEDMENKKKKKKGKNGNENGNENGSENGNENGNENGNENENKNESENENENENENENGNENENEKENEKDKNIKEIENVTNANKENYEKINKNSEITITKSNIDIYNNNRNNDIDKVNNHIFTNQQKKHNLHNEQNKFNETLNVSTNHKNHYEEKKKYESNMFNVDKRMHKNLTSMDTILHNLNDKLSHHKDLKNRELKLKFEAMSRIKEYKIYNELIQKSVEILTLRLTKINDELKKLKDISENALQKYINEKGYGLMKHYNFPEYNKLEEEKIMKRSKITWNEKKSHHLYCPMECNKERCYNRPRGPTQCYKLEQIGRNIETICEPFINEHNGTCRPDFHHCAIAEPERNKKYSIYATDDVHFVPSQFVTIKGYNLHECLQFLVVKKNSTCGPMTIEKNLMESEEILKEPVLSKVLYNEILFENIKISTPGEYNICLAQFYQDPEKDDILSENSSNKYKKKKKNDMKVLGIDTIGTLYVLPLHEKQKTG