wanglab/gogpt-training-data huggingface dataset:
Protein: Selenocysteine insertion sequence-binding protein 2-like (SECIS-binding protein 2-like) (Q93073)
Organism: Homo sapiens (Human)
Function: Binds SECIS (Sec insertion sequence) elements present on selenocysteine (Sec) protein mRNAs, but does not promote Sec incorporation into selenoproteins in vitro.
Interaction partners:
Sequence:
MDRAPTEQNVKLSAEVEPFIPQKKSPDTFMIPMALPNDNGSVSGVEPTPIPSYLITCYPFVQENQSNRQFPLYNNDIRWQQPNPNPTGPYFAYPIISAQPPVSTEYTYYQLMPAPCAQVMGFYHPFPTPYSNTFQAANTVNAITTECTERPSQLGQVFPLSSHRSRNSNRGSVVPKQQLLQQHIKSKRPLVKNVATQKETNAAGPDSRSKIVLLVDASQQTDFPSDIANKSLSETTATMLWKSKGRRRRASHPTAESSSEQGASEADIDSDSGYCSPKHSNNQPAAGALRNPDSGTMNHVESSMCAGGVNWSNVTCQATQKKPWMEKNQTFSRGGRQTEQRNNSQVGFRCRGHSTSSERRQNLQKRPDNKHLSSSQSHRSDPNSESLYFEDEDGFQELNENGNAKDENIQQKLSSKVLDDLPENSPINIVQTPIPITTSVPKRAKSQKKKALAAALATAQEYSEISMEQKKLQEALSKAAGKKNKTPVQLDLGDMLAALEKQQQAMKARQITNTRPLSYTVVTAASFHTKDSTNRKPLTKSQPCLTSFNSVDIASSKAKKGKEKEIAKLKRPTALKKVILKEREEKKGRLTVDHNLLGSEEPTEMHLDFIDDLPQEIVSQEDTGLSMPSDTSLSPASQNSPYCMTPVSQGSPASSGIGSPMASSTITKIHSKRFREYCNQVLCKEIDECVTLLLQELVSFQERIYQKDPVRAKARRRLVMGLREVTKHMKLNKIKCVIISPNCEKIQSKGGLDEALYNVIAMAREQEIPFVFALGRKALGRCVNKLVPVSVVGIFNYFGAESLFNKLVELTEEARKAYKDMVAAMEQEQAEEALKNVKKVPHHMGHSRNPSAASAISFCSVISEPISEVNEKEYETNWRNMVETSDGLEASENEKEVSCKHSTSEKPSKLPFDTPPIGKQPSLVATGSTTSATSAGKSTASDKEEVKPDDLEWASQQSTETGSLDGSCRDLLNSSITSTTSTLVPGMLEEEEDEDEEEEEDYTHEPISVEVQLNSRIESWVSETQRTMETLQLGKTLNGSEEDNVEQSGEEEAEAPEVLEPGMDSEAWTADQQASPGQQKSSNCSSLNKEHSDSNYTTQTT
Protein: Sugar transporter ERD6-like 17 (Sugar-porter family protein 1) (Q94CI7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Sugar transporter.
Subcellular location: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- At2g34355
- Major facilitator superfamily protein
- Major facilitator superfamily protein
Sequence:
MVMEEGRSIEEGLLQLKNKNDDSECRITACVILSTFVAVCGSFSFGVATGYTSGAETGVMKDLDLSIAQFSAFGSFATLGAAIGALFCGNLAMVIGRRGTMWVSDFLCITGWLSIAFAKEVVLLNFGRIISGIGFGLTSYVVPVYIAEITPKHVRGTFTFSNQLLQNAGLAMIYFCGNFITWRTLALLGALPCFIQVIGLFFVPESPRWLAKVGSDKELENSLFRLRGRDADISREASEIQVMTKMVENDSKSSFSDLFQRKYRYTLVVGIGLMLIQQFSGSAAVISYASTIFRKAGFSVAIGTTMLGIFVIPKAMIGLILVDKWGRRPLLMTSAFGMSMTCMLLGVAFTLQKMQLLSELTPILSFICVMMYIATYAIGLGGLPWVIMSEIFPINIKVTAGSIVTLVSFSSSSIVTYAFNFLFEWSTQGTFFIFAGIGGAALLFIWLLVPETKGLSLEEIQVSLIHQPDERNQT
Protein: KH domain-containing protein (O25768)
Organism: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Interaction partners:
- RNA-binding protein KhpB N-terminal domain-containing protein
- Small ribosomal subunit protein bS16
- Ribosome maturation factor RimM
- Large ribosomal subunit protein bL19
- Small ribosomal subunit protein uS4
- Small ribosomal subunit protein uS15
- tRNA
- Large ribosomal subunit protein bL20
- Small ribosomal subunit protein bS18
- Small ribosomal subunit protein uS9
Sequence:
MHESDPLNTPFSQADCKDYSHCVATFLEKYLKKVVSFPQALSVEHTLLEDKVKQITIYTHPSDMGHVIGKEGKMVSAIKAFISGVKAKDGFSYKIVVFASKNGDKNPHVLGDQTP
Protein: Cerevisin (EC 3.4.21.48) (Proteinase YSCB) (Vacuolar protease B) (PrB) (P09232)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Vacuolar proteinase B involved in protein degradation in the vacuole. Among other substrates, acts on carboxypeptidase Y (cpY/PRC1) to activate it by processing its Pro-peptide. Required for meiosis and spore formation, and for optimal survival in stationary phase.
Subcellular location: Vacuole.
Interaction partners:
- Saccharopepsin
- Carboxypeptidase Y
- Carboxypeptidase Y inhibitor
- Subtilisin-like protease 3
- SCF-associated factor 1
- Vacuolar aminopeptidase 1
- Aspartic proteinase 3
- Alpha-mannosidase
- Carboxypeptidase S
- Orotidine 5'-phosphate decarboxylase
Sequence:
MKLENTLFTLGALGSISAALVIPNLENAADHHELINKEDHHERPRKVEFTKDDDEEPSDSEDKEHGKFHKKGRKGQDKESPEFNGKRASGSHGSAHEGGKGMKPKHESSNDDDNDDKKKKPHHKGGCHENKVEEKKMKGKKVKGKKHHEKTLEKGRHHNRLAPLVSTAQFNPDAISKIIPNRYIIVFKRGAPQEEIDFHKENVQQAQLQSVENLSAEDAFFISTKDTSLSTSEAGGIQDSFNIDNLFSGYIGYFTQEIVDLIRQNPLVDFVERDSIVEATEFDTQNSAPWGLARISHRERLNLGSFNKYLYDDDAGRGVTSYVIDTGVNINHKDFEKRAIWGKTIPLNDEDLDGNGHGTHCAGTIASKHYGVAKNANVVAVKVLRSNGSGTMSDVVKGVEYAAKAHQKEAQEKKKGFKGSTANMSLGGGKSPALDLAVNAAVEVGIHFAVAAGNENQDACNTSPASADKAITVGASTLSDDRAYFSNWGKCVDVFAPGLNILSTYIGSDDATATLSGTSMASPHVAGLLTYFLSLQPGSDSEFFELGQDSLTPQQLKKKLIHYSTKDILFDIPEDTPNVLIYNGGGQDLSAFWNDTKKSHSSGFKQELNMDEFIGSKTDLIFDQVRDILDKLNII
Protein: Nuclease S1 (EC 3.1.30.1) (Deoxyribonuclease S1) (Endonuclease S1) (Single-stranded-nucleate endonuclease) (P24021)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Function: Hydrolyzes only single-stranded DNA and RNA without apparent specificity for bases.
Interaction partners:
Sequence:
MPRLLPISAATLALAQLTYGWGNLGHETVAYIAQSFVASSTESFCQNILGDDSTSYLANVATWADTYKYTDAGEFSKPYHFIDAQDNPPQSCGVDYDRDCGSAGCSISAIQNYTNILLESPNGSEALNALKFVVHIIGDIHQPLHDENLEAGGNGIDVTYDGETTNLHHIWDTNMPEEAAGGYSLSVAKTYADLLTERIKTGTYSSKKDSWTDGIDIKDPVSTSMIWAADANTYVCSTVLDDGLAYINSTDLSGEYYDKSQPVFEELIAKAGYRLAAWLDLIASQPS
Protein: Exostosin like glycosyltransferase 2 (C9JEG3)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004648}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004648}.
Interaction partners:
Sequence:
MRTWNSGGTKCCHICKLPGRVMGIRVLRLSLVVILVLLLVAGALTALLPSVKEDKMLMLRREIKSQGKSTMDSFTLIMQTYNRTDLLLKLLNHYQAVPNLHKVIVVWNNIGEKAPDELWNSLGPHPIPVIFKQQTANRMRNRLQVFPELETNAVLMVDDDTLISTPDLVFAFSVWQQFPDQIVGFVPRKHVSTSSGIYSYGSFEMQAPGSGNGDQYSMVLIGASFFNSKYLELFQRQPAAVHALIDDTQNCDDIAMNFIIAKHIGK
Protein: Eukaryotic translation initiation factor 3 subunit H-B (eIF3h-B) (Eukaryotic translation initiation factor 3 subunit 3-B) (eIF-3-gamma-B) (eIF3 p40 subunit B) (Q5PR67)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03007}.
Interaction partners:
- Eukaryotic translation initiation factor 3, subunit F
- Eukaryotic translation initiation factor 3 subunit M
- FAU ubiquitin-like and ribosomal protein S30 fusion a ubiquitously expressed
- FAU ubiquitin-like and ribosomal protein S30 fusion b
- Eukaryotic translation initiation factor 3 subunit D
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit E-A
- Eukaryotic translation initiation factor 3 subunit K
- Eukaryotic translation initiation factor 3 subunit L
- Eukaryotic translation initiation factor 3 subunit G
Sequence:
MASRKETPNGKTLDTPVKQIQIEGLVVMKIIKHYQEEGQGSEVVQGVLLGLVVEDQLEITNCFPFPQHTEDDADFDEVQYQMEMMRSLRHVNIDHLHVGWYQSTLYGSFVSRALLDSQFSYQHAIEESVVLIYDPIKTAQGSLCLKAYRLTPKLMEICKEKDFSSEGLKKASVGYEHMFEEVPIVIKNSHLINVLLWELEEKSTAADKHELLSLSSSSHLEKSLQMLMDRVDDMSQDIVKYNNYSRSLSKQQQQKHQYVQRRQQENAQRQSRGEPPLPEEDLTKMFKPPQPPPRMDTLLIASQINTYCQTIKEFTSQNLGKLFMAEALQGPSS
Protein: LD10058p (Q7K140)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNLHVAATTTPLPLLMSTSGAMYTAAKAKSSPAVGHRLIDDSSSQQQPSFMSFKLNHDRSLPDTDSTDVDVEDQEADLDGEEHDDHEAEGEEEHDEHDNFEEHARELSNDNDGDIKEHVFPLSDNELHPEVHSIEEVQQQLQQEDADADSAPAPAAAEDNESSQHDAEADGEHEQDGAEGETDLENETPVDLIKANEPLAMPSSTESPAAAIEERIKQIAQDFQKMASSQELQPKEELTPQSSLSLNDLIRTLRPNEQQIIPQIDSDYSNAMRVLGKPMAANN
Protein: Myc-associated zinc finger protein (MAZI) (Pur-1) (Purine-binding transcription factor) (P56670)
Organism: Mesocricetus auratus (Golden hamster)
Function: Transcriptional regulator (By similarity). Acts as a transcriptional activator that binds to purine-rich GAGA sites found in the promoter of many genes including insulin I and II and islet amyloid polypeptide.
Subcellular location: Nucleus.
Interaction partners:
- E3 ubiquitin-protein ligase TRAF7
Sequence:
FPVLGLDSRGVGGLMNSFPPPQGHAQNPLQVGAELQSRFFASQGCAQSPFQAAPAPPPTPQAPAAEPLQVDLLPVLAAAQESAAAAAAAAAAAAAVVTAPPAPAAASTVDTAALKQPPAPPPPPPAVSAPAAEAAPPAAAATIAAAAATAVVAPTSTVAVAPVASVLEKKTKSKGPYICALCAKEFKNGYNLRRHEAIHTGAKAGRVPSGAMKMPTMVPLSLLSVPQLSGASGGGGEAGAGGGTTAVAAGGVVTTTASGKRIRKNHACEMCGKAFRDVYHLNRHKLSHSDEKPYQCPVCQQRFKRKDRMSYHVRSHDGAVHKPYNCSHCGK
Protein: Paired box 6 (A0A1W2PRU4)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MGADGMYDKLRMLNGQTGSWGTRPGWYPGTSVPGQPTQDGCQQQEGGGENTNSISSNGEDSDEAQMRLQLKRKLQRNRTSFTQEQIEALEKEFERTHYPDVFARERLAAKIDLPEARIQVWFSNRRAKWRREEKLRNQRRQASNTPSHIPISSSFSTSVYQPIPQPTTPVSSFTSGSMLGRTDTALTNTYSALPPMPSFTMANNLPMQPPVPSQTSSYSCMLPTSPSVNGRSYDTYTPPHMQTHMNSQPMGTSGTTSTGLISP
Protein: Collagen alpha-6(IV) chain (Q14031)
Organism: Homo sapiens (Human)
Function: Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen.
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane.
Interaction partners:
- Collagen alpha-5
- CD44 antigen
- Platelet glycoprotein VI
- Integrin alpha-5
- Integrin alpha-2
- Multifunctional procollagen lysine hydroxylase and glycosyltransferase LH3
- Integrin alpha-1
- Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1
- Probable E3 ubiquitin-protein ligase MID2
- Ribose-phosphate pyrophosphokinase 1
Sequence:
MLINKLWLLLVTLCLTEELAAAGEKSYGKPCGGQDCSGSCQCFPEKGARGRPGPIGIQGPTGPQGFTGSTGLSGLKGERGFPGLLGPYGPKGDKGPMGVPGFLGINGIPGHPGQPGPRGPPGLDGCNGTQGAVGFPGPDGYPGLLGPPGLPGQKGSKGDPVLAPGSFKGMKGDPGLPGLDGITGPQGAPGFPGAVGPAGPPGLQGPPGPPGPLGPDGNMGLGFQGEKGVKGDVGLPGPAGPPPSTGELEFMGFPKGKKGSKGEPGPKGFPGISGPPGFPGLGTTGEKGEKGEKGIPGLPGPRGPMGSEGVQGPPGQQGKKGTLGFPGLNGFQGIEGQKGDIGLPGPDVFIDIDGAVISGNPGDPGVPGLPGLKGDEGIQGLRGPSGVPGLPALSGVPGALGPQGFPGLKGDQGNPGRTTIGAAGLPGRDGLPGPPGPPGPPSPEFETETLHNKESGFPGLRGEQGPKGNLGLKGIKGDSGFCACDGGVPNTGPPGEPGPPGPWGLIGLPGLKGARGDRGSGGAQGPAGAPGLVGPLGPSGPKGKKGEPILSTIQGMPGDRGDSGSQGFRGVIGEPGKDGVPGLPGLPGLPGDGGQGFPGEKGLPGLPGEKGHPGPPGLPGNGLPGLPGPRGLPGDKGKDGLPGQQGLPGSKGITLPCIIPGSYGPSGFPGTPGFPGPKGSRGLPGTPGQPGSSGSKGEPGSPGLVHLPELPGFPGPRGEKGLPGFPGLPGKDGLPGMIGSPGLPGSKGATGDIFGAENGAPGEQGLQGLTGHKGFLGDSGLPGLKGVHGKPGLLGPKGERGSPGTPGQVGQPGTPGSSGPYGIKGKSGLPGAPGFPGISGHPGKKGTRGKKGPPGSIVKKGLPGLKGLPGNPGLVGLKGSPGSPGVAGLPALSGPKGEKGSVGFVGFPGIPGLPGIPGTRGLKGIPGSTGKMGPSGRAGTPGEKGDRGNPGPVGIPSPRRPMSNLWLKGDKGSQGSAGSNGFPGPRGDKGEAGRPGPPGLPGAPGLPGIIKGVSGKPGPPGFMGIRGLPGLKGSSGITGFPGMPGESGSQGIRGSPGLPGASGLPGLKGDNGQTVEISGSPGPKGQPGESGFKGTKGRDGLIGNIGFPGNKGEDGKVGVSGDVGLPGAPGFPGVAGMRGEPGLPGSSGHQGAIGPLGSPGLIGPKGFPGFPGLHGLNGLPGTKGTHGTPGPSITGVPGPAGLPGPKGEKGYPGIGIGAPGKPGLRGQKGDRGFPGLQGPAGLPGAPGISLPSLIAGQPGDPGRPGLDGERGRPGPAGPPGPPGPSSNQGDTGDPGFPGIPGPKGPKGDQGIPGFSGLPGELGLKGMRGEPGFMGTPGKVGPPGDPGFPGMKGKAGPRGSSGLQGDPGQTPTAEAVQVPPGPLGLPGIDGIPGLTGDPGAQGPVGLQGSKGLPGIPGKDGPSGLPGPPGALGDPGLPGLQGPPGFEGAPGQQGPFGMPGMPGQSMRVGYTLVKHSQSEQVPPCPIGMSQLWVGYSLLFVEGQEKAHNQDLGFAGSCLPRFSTMPFIYCNINEVCHYARRNDKSYWLSTTAPIPMMPVSQTQIPQYISRCSVCEAPSQAIAVHSQDITIPQCPLGWRSLWIGYSFLMHTAAGAEGGGQSLVSPGSCLEDFRATPFIECSGARGTCHYFANKYSFWLTTVEERQQFGELPVSETLKAGQLHTRVSRCQVCMKSL
Protein: TBC1 domain family member 1 (A0A8I5ZMX5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MEAITFTARKHPFPNEVSVDFGLQLVGSLPVHSLTTMPMLPWVVAEVRRLSGQCSKKEPGMKQVRLWVSPSGLRCEPDLRKSQPWDPLICSSIFECKPQRVHKLIHNSQDPSYFACLIKEDAAHQQSLCYVFKADDQTKVPEIISSIRQAGKIARQEELRCPSEFDDTFAKKFEVLFCGRVTVAHKKAPPALIDECIEKFNHVSCGRRIDWDAPTGQPSAPGARPMRKSFSQPGLRSLAFRKEFQDASLRSSTFSSFDNDIENHLIGGHNVVQPTDMEENRTMLFTIGQSEVYLISPDTKKIALEKNFKEISFCSQGIRHVDHFGFICRECSGGGGAGFHFVCYVFQCTNEALVDEIMMTLKQAFTVAAVQQTAKAPAQLCEGCPLQGLHKLCERIEGMNSSKTKLELQKHLTTLTNQEQAMIFEEVQKLRPRNEQRENELIISFLRCLYEEKQKEHSHTGEPKQTLQVAAENIGSELPPSASRFRLDSLKNRAKRSLTESLESILSRGNKARGLQDHSASVDLDSSTSSTLSNTSKELSMGDKEALPISESSFKLLGSSDDLSSDSESHIAEESALLSPQQAFRRRANTLSHFPVECPAPPEPAQTSPGVSQRKLMRYHSVSTETPHERNVDHLPGGESRCCPGQPSDPPPLPPRLNPSASSPNFFKYLKHNSSGEQSGNAVPKSVSYRNALRKKLHSSSSVPNFLKFLAPVDENNTCDFKNTNRDFESKANHLGDTDGTPVKARRHSWRQQIFLRVATPQKACDSPSRYEDYSELGELPPRSPLEPVCEDGPFGPVQEEKKKTSRELRELWKKAILQQILLLRMEKENQKLQASENDLLNKRLKLDYEEITPCLKEVTTVWEKMLSTPGRSKIKFDMEKVHSAVGQGVPRHHRGEIWKFLAEQFHLKHPFPSKQQPKDVPYKELLKKLTSQQHAILIDLGRTFPTHPYFSAQLGAGQLSLYNILKAYSLLDQEVGYCQGLSFVAGILLLHMSEEEAFKMLKFLMFDMGLRKQYRPDMIILQIQMYQLSRLLHDYHRDLYNHLEEYEIGPSLYAAPWFLTVFASQFPLGFVARVFDMIFLQGSEVIFKVALSLLGSHKPLILQHENLETIVDFIKNTLPNLGLVQMEKTISQVFEMDIAKQLQAYEVEYHVLQEELIDSSPLSDNQRMDKLEKTNSSLRKQNLDLLEQLQVANARIQSLEVTVEKLLTSESKLKQAVLTLEMERSALLQMVEELRRQMAQPSTAEPDCTRLEPTGD
Protein: RING-type domain-containing protein (Q387T9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSGLTSHNISATSIRVHGITRERDMCVFCRKRSSPPPNDPLAPVFAFFSLVDCRHYACQPCALVHCDNAGRHIRCPACCAISRLAQSGRRRGNRVDERVPIDDGVSSAASQSSKRVLAPPKRSLSVTDRRRRTSSVQFSTNLTSPSGQKEALSTGGSNTSLTLAAVGRLPTDPNYSKGKGDEGGTVAAFSEEERISVDLYTIKGTAAKRPRRTTAERARSQPLPPAEYRYLPPPTPFHRPPPLVIHTIEEEEEVAASFQLIVREIEQTIAATLVKEADERDTIGIAEAHRRNVLSKLREEDERKRFAAHHELNDEFSDAKLSPRTTTNASDGQVSETSDEGMSELSTQQDSIQKNYKQPIDQKAMITKERTGTPTAAEKQTKHQQQTITKQNTEEEKKEAKNENNKESKKKRRERVEVATWDSEQQLRLFEQLMDLARDEQQHRAKIQRDETRMHAEMERSEASDVATIKAAMEAMAESARREQEELLRDEKEERYTIQEDERRLRRNITRQSAELSLDVSMQHVQQRGKEDAQRELDMLRVALESTAVETTSRARLNLIVTEELRARDSLCSDEASERAMHAAEERRERVEVATWDSEQQLRLFEQLMDLARDEQQHRAKIQRDETRMHAEMERSEASDVATIKAAMEAMAESARREQEELLRDEKEERYTIQEDERRLRRNITRQSAELSLDVSMQHVQQRGKEDAQRELDMLRVALESTAVETTSRARLNLIVTEELRARDSLCSDEASERAMHAAEERRERVEVATWDSEQQLRLFEQLMDLARDEQQHRAKIQRDETRMHAEMERSEASDVATIKAAMEAMAESARREQEELLRDEKEERYTIQEDERRLRRNITRQSAELSLDVSMQHVQQRGKEDAQRELDMLRVALESTAVETTSRARLNLIVTEELRARDSLCSDEASERAMHAAEERRERVEVATWDSEQQLRLFEQLMDLARDEQQHRAKIQRDETRMHAEMERSEADGILACGAQSEGADSFEVASSGCDCVFRPSGADCASFSPYVCRGGGVLPLDVEIPVGLAYSAHGSTSAEVISVDYTSFLPIVGSDAQGESSLWNTLDDDGGVVFGDVCAGGDDVGIDVNDVESVHISRGCSTVLDAGGVGATAEVYALDEKWRDGTAVSAEPPRIPASRICRTCFSTDTSRCARCGTMVCSHCIPSGSFRQCCTLHHLTIINKRCRVMTETRVHARWECRRLFRQFRLEQRMRRRRENVVNTRGFDVVVLTPEQKGDNSNLHEVKTPPRVTRRFLNQENDSEEDAAWKSHYLESWPSDSGQMPPCGLKQERFDEFNDAENSMNLTADNEPKTERKRATAFFVPLGNSAEPRRPKPPTPRNYVPGIIHNCTKAPQSKRAVSRMRFRRLRRQNATGNTKNTTLNSAAAGRNVQEHRAASSSKPRPQESWARQRPVQRQGAFITADPVRGITRSGPTSNSWRRRNFRTKSRSPAGYGGKASACNFHGDRCGDAMALGRTYYDGNPVRSKGLAYVLDEEPPQRGYEPTPPTRLQSNRVVKSGVHSGEEHTRMGCQHEWEPDQQCVPLFEEFHASSSTPPWRPPFSRDPPPPRRNHRNTNIGGRTHRTLAPFPARQRLCHPRQRSAADLTRNASPGQACSRFHYNPLDDVDRAAFVGGPRGAQRQPPTSVAEPCITVHLFPPSSYGGGAGTSGRHPLRGPTARRHSSRAHRPSPARAASPPWRTDLNTPFICPPWNANRPDTFIAKPYTRTTCRR
Protein: 1,4-dihydroxy-2-naphthoyl-CoA synthase (DHNA-CoA synthase) (EC 4.1.3.36) (P9WNP5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Converts o-succinylbenzoyl-CoA (OSB-CoA) to 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA).
Interaction partners:
- Probable 2-succinylbenzoate--CoA ligase
- 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase
- o-succinylbenzoate synthase
- Putative esterase Rv1847
- Putative isochorismate synthase MenF
- 1,4-dihydroxy-2-naphthoate octaprenyltransferase
- Demethylmenaquinone methyltransferase
Sequence:
MVAPAGEQGRSSTALSDNPFDAKAWRLVDGFDDLTDITYHRHVDDATVRVAFNRPEVRNAFRPHTVDELYRVLDHARMSPDVGVVLLTGNGPSPKDGGWAFCSGGDQRIRGRSGYQYASGDTADTVDVARAGRLHILEVQRLIRFMPKVVICLVNGWAAGGGHSLHVVCDLTLASREYARFKQTDADVGSFDGGYGSAYLARQVGQKFAREIFFLGRTYTAEQMHQMGAVNAVAEHAELETVGLQWAAEINAKSPQAQRMLKFAFNLLDDGLVGQQLFAGEATRLAYMTDEAVEGRDAFLQKRPPDWSPFPRYF
Protein: Olfactory receptor 4F17 (Olfactory receptor 4F11) (Olfactory receptor 4F18) (Olfactory receptor 4F19) (Q8NGA8)
Organism: Homo sapiens (Human)
Function: Odorant receptor.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
Sequence:
MVTEFIFLGLSDSQGLQTFLFMLFFVFYGGIVFGNLLIVITVVSDSHLHSPMYFLLANLSLIDLSLSSVTAPKMITDFFSQRKVISFKGCLVQIFLLHFFGGSEMVILIAMGFDRYIAICKPLHYTTIMCGNACVGIMAVAWGIGFLHSVSQLAFAVHLPFCGPNEVDSFYCDLPRVIKLACTDTYRLDIMVIANSGVLTVCSFVLLIISYTIILMTIQHRPLDKSSKALSTLTAHITVVLLFFGPCVFIYAWPFPIKSLDKFLAVFYSVITPLLNPIIYTLRNKDMKTAIRQLRKWDAHSSVKF
Protein: DNA-(apurinic or apyrimidinic site) endonuclease 2 (EC 3.1.11.2) (AP endonuclease XTH2) (APEX nuclease 2) (APEX nuclease-like 2) (Apurinic-apyrimidinic endonuclease 2) (AP endonuclease 2) (Q9UBZ4)
Organism: Homo sapiens (Human)
Function: Functions as a weak apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents. Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends. Also displays double-stranded DNA 3'-5' exonuclease, 3'-phosphodiesterase activities. Shows robust 3'-5' exonuclease activity on 3'-recessed heteroduplex DNA and is able to remove mismatched nucleotides preferentially. Shows fairly strong 3'-phosphodiesterase activity involved in the removal of 3'-damaged termini formed in DNA by oxidative agents. In the nucleus functions in the PCNA-dependent BER pathway. Required for somatic hypermutation (SHM) and DNA cleavage step of class switch recombination (CSR) of immunoglobulin genes. Required for proper cell cycle progression during proliferation of peripheral lymphocytes.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00764, ECO:0000269|PubMed:11376153, ECO:0000269|PubMed:19443450}. Cytoplasm. Mitochondrion {ECO:0000305|PubMed:11376153}. Note=Together with PCNA, is redistributed in discrete nuclear foci in presence of oxidative DNA damaging agents. {ECO:0000269|PubMed:19443450}.
Interaction partners:
- DNA repair nuclease/redox regulator APEX1
- DNA topoisomerase 3-alpha
- Tyrosyl-DNA phosphodiesterase 1
- Uracil-DNA glycosylase
- Flap endonuclease 1
- DNA repair endonuclease XPF
- N-glycosylase/DNA lyase
- Endonuclease III-like protein 1
- Proliferating cell nuclear antigen
Sequence:
MLRVVSWNINGIRRPLQGVANQEPSNCAAVAVGRILDELDADIVCLQETKVTRDALTEPLAIVEGYNSYFSFSRNRSGYSGVATFCKDNATPVAAEEGLSGLFATQNGDVGCYGNMDEFTQEELRALDSEGRALLTQHKIRTWEGKEKTLTLINVYCPHADPGRPERLVFKMRFYRLLQIRAEALLAAGSHVIILGDLNTAHRPIDHWDAVNLECFEEDPGRKWMDSLLSNLGCQSASHVGPFIDSYRCFQPKQEGAFTCWSAVTGARHLNYGSRLDYVLGDRTLVIDTFQASFLLPEVMGSDHCPVGAVLSVSSVPAKQCPPLCTRFLPEFAGTQLKILRFLVPLEQSPVLEQSTLQHNNQTRVQTCQNKAQVRSTRPQPSQVGSSRGQKNLKSYFQPSPSCPQASPDIELPSLPLMSALMTPKTPEEKAVAKVVKGQAKTSEAKDEKELRTSFWKSVLAGPLRTPLCGGHREPCVMRTVKKPGPNLGRRFYMCARPRGPPTDPSSRCNFFLWSRPS
Protein: Eisosome protein SEG2 (Stability of eisosomes guaranteed protein 2) (P34250)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Likely plays only a minor role in eisosome assembly.
Subcellular location: Cell membrane {ECO:0000269|PubMed:22869600}; Peripheral membrane protein {ECO:0000269|PubMed:22869600}; Cytoplasmic side {ECO:0000269|PubMed:22869600}. Note=Localizes to eisosomes.
Interaction partners:
- Uncharacterized protein YGR130C
- Eisosome protein 1
- PX domain-containing protein LEC1
- Sphingolipid long chain base-responsive protein PIL1
Sequence:
MIQESSPDALAAAAAIGNALSYNGRTVDKSKIPQYNQSFTSRTTSIAGINRYTMLSNSRTNSRMLLMNGNVRQYSKRTSSLPNQGHKNTSNNSAGRRQHRAHEDAETTFREFGGKQSSKVLNISSSTGQNSKSRTTSLGNSGSTIRTIKKYIPGPRGLMAVEVPVEVEPPRYSLSNRSNQRGGRAYSLPTRNNKTSLMHRNKTTKKAGSQEKKSESGGKSKNDYHGKVLSKMHTTSLKQRHNNVPLIPTTMNEETEQELQEDLHDPLEFKPMIISDDENSFIEPSVLDRSIPKKDKSGLSGREKKEEIETLLKEVHSLEEKISNIEIAKLNEEEREQSLILELRKVKLDEERRMELLKRELNIVKENADLEAQELKLIESKRKQHFHKGQEVASEVKSITIRQPTLSEPKPAYVPPEDVEKEPSTLSNQTQNIENAENIDSVDAEGNLVDPILLGSLNNSNFHMNSDNEVRCIADSNSLTGSELSDYNYIEGSATDLRATAKTSVESEIGGNQVGLKIPQDDDSEKQEERTKGKKSGLVDTNCFLVQKEDQEEALSDNEPESSEKFPSTSGIENVKLEDETGSVMDKNNGPNNDKDDDDDKDNDNDDDDDKDDDVNDDDKDENVDDDENVDDDDDDDDDDDDEYHDSYDVIMRDPVQIEQDISDVPSLKHPSEYSTETEDNKKKEQNSENAEVSQSGTNMAKYLRGANPYLTNTSSDTFSLDSENVNSKSSTDTTRVAPDLLKSSLQPQLRSDLKQSAVPSSTSSSIYSIETSPNIDSSTGKTASNTKTNSHGPPTSISKQKYDQSSSHQIPVMSPKRLDDKRKITNRSCLRTLRGSSNEATLSHNIVYPASDSSSSPPYHSKKPSNPPSSGNLASHEASKCFPKAPQASTTSRRLPDHVPLYIDKNNSALYPKEPPARKSSFEKERPAKDNLGFRSMSLREPLITKNATATAAENLDVEEKKEKGGHVSRKSWTFGLPSPLKRRTSHSTHTTNETEIVNPMTNFKNKTNENDMPILANKKSCNNDDSSPYTASSMNTNDVSEAGTEGHRFSLFGNKSQLSNRNISGGTATLESSNPDLPTALPLSVPVTIIDKNGEIHKLHNDDAAIKDKSHDRHGHSKFGRKLKKIFGRK
Protein: Aspartate kinase (EC 2.7.2.4) (Aspartokinase) (C3JXY0)
Organism: Pseudomonas fluorescens (strain SBW25)
Function: Involved in the biosynthesis of L-aspartate-beta-semialdehyde which is a central intermediate in the biosynthesis of different amino acids (L-lysine, L-methionine, L-threonine). Catalyzes the phosphorylation of the beta-carboxyl group of L-aspartate to yield 4-phospho-L-aspartate.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Homoserine dehydrogenase
- Aspartate-semialdehyde dehydrogenase
- Diaminopimelate decarboxylase
- Argininosuccinate synthase
- Aspartate-semialdehyde dehydrogenase
- Threonine synthase
- Homoserine O-succinyltransferase
- Adenylosuccinate synthetase
- Aspartate ammonia-lyase
- 4-hydroxy-tetrahydrodipicolinate reductase
Sequence:
MALIVQKFGGTSVGSVERIEQVADKVKKFRDAGDDLVVVLSAMSGETNRLIDLAKAISGDQQPLPRELDVIVSTGEQVTIALLAMALNKRGVPAVSYTGSQVRILTDSAHTKARILQIDDQKIRTDLKAGRVVVVAGFQGVDEQGNITTLGRGGSDTTGVALAAALKADECQIYTDVDGVYTTDPRVVSVAQRLDKITFEEMLEMASLGSKVLQIRAVEFAGKYNVPLRVLHSFKEGPGTLITIDEEESMEQPIISGIAFNRDEAKLTIRGVPDTPGVAFKILGPISGANIEVDMIVQNVSHDNTTDFTFTVHRNEYDAAERILQNTAKEIGAREVVGDTKIAKVSIVGVGMRSHAGVASRMFEALAKESINIQMISTSEIKVSVVIEEKYLELAVRALHTAFELDAPARQGE
Protein: Protease LasA (EC 3.4.24.-) (Staphylolytic protease) (P14789)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Involved in proteolysis and elastolysis (degradation of the host protein elastin). Has staphylolytic activity (degrades pentaglycine cross-links in cell wall peptidogylcan), preferring Gly-Gly-|-X substrates where X is Ala or Gly. Enhances the elastolytic but not proteolytic activity of elastase (lasB) and elastolytic activity of other proteases. Degradation of host elastin is likely to contribute to the pathogenicity of P.aeruginosa. While either His-317 or His-356 can abstract a proton in the hydrolysis reaction, the same residue performs both functions in a given catalytic cycle, with the other stabilizing the catalytic intermediate.
Subcellular location: Secreted {ECO:0000269|PubMed:11179971, ECO:0000269|PubMed:1597429, ECO:0000269|PubMed:2110137, ECO:0000269|PubMed:9642203}. Note=Secreted in an Xcp-dependent fashion (a type II secretion pathway). {ECO:0000269|PubMed:9642203}.
Interaction partners:
- Elastase
- 3-
- Chitin-binding protein CbpD
- HTH-type quorum-sensing regulator RhlR
- PA-I galactophilic lectin
- Serralysin
- Acyl-homoserine-lactone synthase
- Acyl-homoserine-lactone synthase
- Aminopeptidase
- Transcriptional activator protein LasR
Sequence:
MQHKRSRAMASPRSPFLFVLLALAVGGTANAHDDGLPAFRYSAELLGQLQLPSVALPLNDDLFLYGRDAEAFDLEAYLALNAPALRDKSEYLEHWSGYYSINPKVLLTLMVMQSGPLGAPDERALAAPLGRLSAKRGFDAQVRDVLQQLSRRYYGFEEYQLRQAAARKAVGEDGLNAASAALLGLLREGAKVSAVQGGNPLGAYAQTFQRLFGTPAAELLQPSNRVARQLQAKAALAPPSNLMQLPWRQGYSWQPNGAHSNTGSGYPYSSFDASYDWPRWGSATYSVVAAHAGTVRVLSRCQVRVTHPSGWATNYYHMDQIQVSNGQQVSADTKLGVYAGNINTALCEGGSSTGPHLHFSLLYNGAFVSLQGASFGPYRINVGTSNYDNDCRRYYFYNQSAGTTHCAFRPLYNPGLAL
Protein: Candida glabrata strain CBS138 chromosome B complete sequence (Q6FXC8)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Candida glabrata strain CBS138 chromosome I complete sequence
- Protein HIR2
- Candida glabrata strain CBS138 chromosome K complete sequence
Sequence:
MMQDHQKSGVSSSQDLFDLFEQGNDIDFETAYQMLSGTLEESEPLQFMHKGPRQQEVSTPIANILPPLDPIKPATPNVMSNTTPYEYANTNLIKTPHDNNILFSPDNHTKSMFSLDGHTTNHGISNNQKSYYNFDGIRSKHTGFEGSVLPHFYESKLTSPQRLLTESPHLPTISQNFLTRSPIFTSQPFENHQNIGIPPMIQEKLHNNFGFPQKGLDDHFKSPELLSSYESHAIENFLDNLVASDPFHNDKNDIDFKIGNDKAAVHEDMNNKGNILSAEIINNNKCNSSIDVTQNRINSTLHKNSNSSDIVHNREDYKNTDLTTNHKIKKIPVPKDYPTKNIELPGIVISDDDIPADIRHDMAKVRKWKHVRLEKLRRTHSKNAFDDLIKLIETPHPNLDKRIPKYKLLGLVMNDIKGLLEANEKLEKLLNS