wanglab/gogpt-training-data huggingface dataset:
Protein: Protein PUTATIVE RECOMBINATION INITIATION DEFECT 1 (AtPRD1) (Protein PRD1) (O23277)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in DNA cleavage that forms the double-strand breaks (DSB) that initiate meiotic recombination.
Subcellular location: Nucleus {ECO:0000269|PubMed:17762870}.
Interaction partners:
- Meiotic recombination protein SPO11-1
- Putative recombination initiation defects 3
- Protein MULTIPOLAR SPINDLE 1
- Protein DOUBLE-STRAND BREAK FORMATION
- Transcription coactivator
- Meiotic recombination protein SPO11-2
- Type 2 DNA topoisomerase 6 subunit B-like
- Protein transport protein SEC24 B
- Protein transport protein SEC24 C
- Protein transport protein SEC31 homolog B
Sequence:
MFFQHSQLQNSDHLLHESMADSNHQSLSPPCANGHRSTISLRDDQGGTFCLICFSNLVSDPRIPTVHVSYALHQLSIAISEPIFLRTLLSSHIHFLVSPLVHALSSIDDAPIAIQIMDMISLLCSVEESSIGEDFVERISDQLSSGALGWSRRQLHMLHCFGVLMSCENININSHIRDKEALVCQLVEGLQLPSEEIRGEILFALYKFSALQFTEQNVDGIEVLSLLCPKLLCLSLEALAKTQRDDVRLNCVALLTILAQQGLLANSHSNSASSMSLDEVDDDPMQTAENVAARPCLNVLFAEAIKGPLLSTDSEVQIKTLDLIFHYISQESTPSKQIQVMVEENVADYIFEILRLSECKDQVVNSCLRVLDLFSLAEHSFRKRLVIGFPSVIRVLHYVGEVPCHPFQIQTLKLISSCISDFPGIASSSQVQEIALVLKKMLERYYSQEMGLFPDAFAIICSVFVSLMKTPSFGETADVLTSLQESLRHSILASLSLPEKDSTQILHAVYLLNEVYVYCTASTSINKTICIELRHCVIDVCTSHLLPWFLSDVNEVNEEATLGIMETFHSILLQNSDIQAKEFAELLVSADWFSFSFGCLGNFCTDNMKQRIYLMLSSLVDILLEQKTGSHIRDALHCLPSDPQDLLFLLGQASSNNQELASCQSAALLIFHTSSIYNDRLADDKLVLASLEQYIILNKTSLICAISDSPALLNLVNLYGLCRSLQNERYQISYSLEAERIIFHLLNEYEWDLGSINIHLESLKWLFQQESISKSLIYQIQKISRNNLIGNEVHNVYGDGRQRSLTYWFAKLISEGDNYAATLLVNLLTQLAEKEEQENDVISILNLMNTIVSIFPTASNNLSMNGIGSVIHRLVSGFSNSSLGTSFRTLLLLVFNILTSVQPAVLMIDESWYAVSIKLLNFLSLRDTAIKQNHEDMVVIGILSLVLYHSSDGALVEASRNIVSNSYLVSAINTVVDVACSKGPALTQCQDETNIGEALAFTLLLYFFSLRSLQIVLAGAVDWQTFFGTSTSLETLPVVCIHCHNLCRLMHFGAPQIKLIASYCLLELLTGLSEQVDIKKEQLQCSSSYLKSMKAVLGGLVFCDDIRVATNSALCLSMILGWEDMEGRTEMLKTSSWYRFIAEEMSVSLAMPCSASSTYVNHHKPAVYLTVAMLRLKNKPVWLRTVFDESCISSMIQNLNGINISREIVILFRELMQAELLNSQQVTKLDRAFQECRKQMHRNGTRDETVEEQVQRKIPSIHDHSEFCNYLVHLMVSNSFGHPSESETYTQKKKQILDEMEQFSELISTREGRVSPIQEETRQMQTERIV
Protein: Muscleblind-like splicing regulator 1 (F1M9N4)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAVSVTPIRDTKWLTLEVCREFQRGTCSRPDTECKFAHPSKSCQVENGRVIACFDSLKGRCSRENCKYLHPPPHLKTQLEINGRNNLIQQKNMAMLAQQMQLANAMMPGAPLQPVNLMQQSFQKRGGDCISRWEGSPYYTGSDTNYQYCTVEPMFSVAPSLATNASAAFNPYLGPVSPSLVPAEILPTAPMLVTGNPGVPVPAAAAAAAQKLMRTDRLEVCREYQRGNCNRGENDCRFAHPADSTMIDTNDNTVTVCMDYIKGRCSREKCKYFHPPAHLQAKIKAAQYQVNQAAAAQAAATAAAMTQSAVKSLKRPLEATFDLGIPQAVLPPLPKRPALEKTNGATAVFNTGIFQYQQALANMQLQQHTAFLPPGKGVVPMVHGATPATVSAATTSATSVPFAATATANQVLSYPIIS
Protein: 2-methylcitrate synthase (2-MCS) (MCS) (EC 2.3.3.5) (Citrate synthase) (EC 2.3.3.16) (I6Y9Q3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the Claisen condensation of propionyl-CoA and oxaloacetate (OAA) to yield 2-methylcitrate (2-MC) and CoA. Also catalyzes the condensation of oxaloacetate with acetyl-CoA.
Interaction partners:
- 2-methylcitrate dehydratase
- Aconitate hydratase A
- Malate dehydrogenase
- Malate synthase G
- Acetyl-coenzyme A synthetase
- Probable malate:quinone oxidoreductase
- Multifunctional 2-oxoglutarate metabolism enzyme
- Pyruvate carboxylase
- HTH-type transcriptional regulator PrpR
- Fumarate hydratase class II
Sequence:
MTGPLAAARSVAATKSMTAPTVDERPDIKKGLAGVVVDTTAISKVVPQTNSLTYRGYPVQDLAARCSFEQVAFLLWRGELPTDAELALFSQRERASRRVDRSMLSLLAKLPDNCHPMDVVRTAISYLGAEDPDEDDAAANRAKAMRMMAVLPTIVAIDMRRRRGLPPIAPHSGLGYAQNFLHMCFGEVPETAVVSAFEQSMILYAEHGFNASTFAARVVTSTQSDIYSAVTGAIGALKGRLHGGANEAVMHDMIEIGDPANAREWLRAKLARKEKIMGFGHRVYRHGDSRVPTMKRALERVGTVRDGQRWLDIYQVLAAEMASATGILPNLDFPTGPAYYLMGFDIASFTPIFVMSRITGWTAHIMEQATANALIRPLSAYCGHEQRVLPGTF
Protein: Alpha-2,8-sialyltransferase 8B (EC 2.4.3.-) (Sialyltransferase 8B) (SIAT8-B) (Sialyltransferase St8Sia II) (ST8SiaII) (Sialyltransferase X) (STX) (Q07977)
Organism: Rattus norvegicus (Rat)
Function: May transfer sialic acid through alpha-2,8-linkages to the alpha-2,3-linked and alpha-2,6-linked sialic acid of N-linked oligosaccharides of glycoproteins and may be involved in PSA (polysialic acid) expression.
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q92186}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q92186}. Secreted {ECO:0000250|UniProtKB:Q92186}. Cell membrane {ECO:0000250|UniProtKB:Q92186}. Note=Also trafficks to the cell surface. {ECO:0000250|UniProtKB:Q92186}.
Interaction partners:
Sequence:
MQLQFRSWMLAALTLLVVFLIFADISEIEEEIGNSGGRGTIRSAVNSLHSKSNRAEVVINGSSLPAVADRSNESLKHSIQPASSKWRHNQTLSLRIRKQILKFLDAEKDISVLKGTLKPGDIIHYIFDRDSTMNVSQNLYELLPRTSPLKNKHFQTCAIVGNSGVLLNSGCGQEIDTHSFVIRCNLAPVQEYARDVGLKTDLVTMNPSVIQRAFEDLVNATWREKLLQRLHGLNGSILWIPAFMARGGKERVEWVNALILKHHVNVRTAYPSLRLLHAVRGYWLTNKVHIKRPTTGLLMYTLATRFCNQIYLYGFWPFPLDQNQNPVKYHYYDSLKYGYTSQASPHTMPLEFKALKSLHEQGALKLTVGQCDGAT
Protein: Heavy metal-responsive transcription factor-1 (Q9GRX2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNDQEKQHQQQQQHYFHSEWKTTANSHGNSLSDSRDYDTNSSRNSLSGSPPVTSNCSSSGSLDFDRPLAQLLEPKLEADGLGIIHGDNYSIYGSQTAESTSGEQQSSDEALSRYRCNYENCYRSYSTIGNLRTHLKTHTGDYSFKCPEDGCHKAFLTSYSLKIHVRVHTKVKPYECEVSGCDKAFNTRYRLHAHLRLHNGETFNCELCQKCFTTLSDLKKHMRTHTQERPYKCPEDDCGKAFTASHHLKTHRRTHTGEKPYPCQEDSCQKSFSTSHSLKSHKKTHQRQLQNKGRKKRPLKTQQTKCSDQEQKDPQQEEQEEEEFIKEDQPEMTLLNPGSHCSETTSTDSGVVLQTLTPQDHLSNVFILQGNEPLILPETSQAYQLSYAAEEEIPSPWIDAGVLVSKPIIPMAPLTDACVALPTEMPSFVNLKPTFGNAVSGNMGDPQPETMDVDPTVETSLPTPTLELNQPNIEELLKQDSFENEEDMETESLLNDILMTIDNNSALLQATLQQASQVPSDASGLVELDIRDNKPTLKQITADAGICNCTNCKCDQTKSCHGGDCGAAAAQQTTRTGAPTTTTTTTTMNSSGGKRICGSVVPTKKVSKRETEMNQNIEDVALLLQNLASMSSGGSSGGGGGCCGGGAVKPAPSGGGCCGEPKAPKPVNDGCGCARPSAPSSGGCCGSGVASTPKPTGGCCSGNQKPAPTATAASSPSCCCSGKGEVQEPPVISSASSAPAAAVKGNACTCKSPAEGVANGCCVVICIKTLQALRKVLTRRNLNLMLCPQQN
Protein: Translation initiation factor eIF2B subunit beta (eIF2B GDP-GTP exchange factor subunit beta) (B3H7H1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}.
Interaction partners:
- Translation initiation factor eIF2B subunit gamma
- Translation initiation factor eIF2B subunit alpha
- Translation initiation factor eIF2B subunit alpha
- Translation initiation factor eIF2B subunit delta
- Translation initiation factor eIF2B subunit epsilon
- Translation initiation factor eIF2B subunit delta
- Translation initiation factor eIF2B subunit delta
- Translation initiation factor eIF2B subunit epsilon
- Translation initiation factor eIF2B subunit epsilon
- Eukaryotic translation initiation factor 2 subunit alpha
Sequence:
MPDVQSTVVEFVNKLRKRKIEGSQATAKYTVELLRSVISHQRVPHANQAAALIDAVKAVGEQLIAANPVELAVGNVVRRVLHIIREEDLSLTTAAMGGLDLLDASDDDDVDNCKGIGFPAMSAAVVAAAARSTLRPPSLQTLLEGTPESATVPYTSSSGADSESKSKSADKSSLTRKLKHDVIEGVNQLIQEIAGCHEQIAEQAIEHIHQNEVILTLGSSRTVLEFLCAAKEKKRSFRVFVAEGAPRYQGHLLAKELVARGLQTTVITDSAVFAMISRVNMVIIGAHAVMANGGVIGPVGVNMAALAAQKHAVPFVVLAGSHKLCPLYPHNPEVLLNELRSPSELLDFGEFSDCLDFGAGSGSLQVVNPTFDYVPPNLVSLFITDTGGHNPSYMYRLIADYYSADDLVM
Protein: V-type ATP synthase beta chain (V-ATPase subunit B) (Q56404)
Organism: Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The V-type beta chain is a regulatory subunit.
Interaction partners:
Sequence:
MDLLKKEYTGITYISGPLLFVENAKDLAYGAIVDIKDGTGRVRGGQVIEVSEEYAVIQVFEETTGLDLATTSVSLVEDVARLGVSKEMLGRRFNGIGKPIDGLPPITPEKRLPITGLPLNPVARRKPEQFIQTGISTIDVMNTLVRGQKLPIFSGSGLPANEIAAQIARQATVRPDLSGEGEKEEPFAVVFAAMGITQRELSYFIQEFERTGALSRSVLFLNKADDPTIERILTPRMALTVAEYLAFEHDYHVLVILTDMTNYCEALREIGAAREEIPGRRGYPGYMYTDLATIYERAGVVEGKKGSVTQIPILSMPDDDRTHPIPDLTGYITEGQIQLSRELHRKGIYPPIDPLPSLSRLMNNGVGKGKTREDHKQVSDQLYSAYANGVDIRKLVAIIGEDALTENDRRYLQFADAFERFFINQGQQNRSIEESLQIAWALLSMLPQGELKRISKDHIGKYYGQKLEEIWGAPQALD
Protein: Huntingtin interacting protein 1 related (F1MUI0)
Organism: Bos taurus (Bovine)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Clathrin heavy chain 1
- Src-like-adapter 2
- Epsin 1
- Cyclin-G-associated kinase
- Epsin 2
- Huntingtin
- Clathrin light chain A
- Clathrin light chain B
- Src substrate cortactin
- Hematopoietic lineage cell-specific protein
Sequence:
MNSIKNVPARVLNRRPGHSLEAEREQFDKTQAISISKAINTQEAPVKEKHARRIILGTHHEKGAFTFWSYAIGLPLPSSAILSWKFCHVLHKVLRDGHPNVLHDCQRYRSNIREIGDLWGHLHDRYGQLVNIYTKLLLTKIAFHLKHPQFPAGLEVTDEVLEKAAGTDVNNIFQLTVEMFDYMDCELKLSESVFRQLNTAIAVSQMSSGQCRLAPLIQVIQDCSHLYHYTVKLMFKLHSCLPADTLQGHRDRFHEQFHSLRNFFRRASDMLYFKRLIQIPRLPEGPPNFLRASALAEHIKPVVVIPEEAPEDEEPENLIEISTGPPAGEPAVVADLFEQTFGPPNGSMKDDRDLQIEALKREVEMLRSELDKIKLEAQRFISQLKGQVNALEAELEEQRKQKQKALVDNEQLRHELAQLRAAQVEGERNQGLREEAEKKASATEARYNKLKEKHSELVNTHAELLRKNADTAKQLTVTQQSQEEVARVKEQLVFQVEQVKRESEMKLEEQSDQLEKLKRELEAKAGELVRVQEALSRTEQSGSELSSRLDALSADRDELSRVVQQREADLLAAQSLAREKEAALSQERQRISRERDELQGRLADKESQEQGLQQRLLDEQFAMLRATAAEAERILQDAVGKLDDPLHLRCTSSPDYLVSRAQAALDAVSALEKGHAQYLTSRADASGLVAALTRFSHLTADTIVHGSATSHLAPTDPADRLIDTCRECGARALELMGQLQEQQALLQARPGLVRTPLQGILQLGQELKPKSLDVREEELGAMVDKEMAATSAAIEDAVRRIEDMMNQARHASSGVKLEVNERILNSCTDLMKAIRLLVTASTSLQKEIVESGRGAATQQEFYAKNSRWTEGLISASKAVGWGATQLVESADKVVLHTGKYEELIVCSHEIAASTAQLVAASKVKADKHSPHLSRLQECSRTVNEMAANVVASTKSGQEQVEDRDTMDFSGLSLIKLKKQEMETQLDKKDGSYAAQVVN
Protein: Actin-related protein 2 (Actin-like protein ARP2) (Actin-like protein 2) (P32381)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Functions as ATP-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the pointed end of the daughter actin filament (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, actin patch {ECO:0000269|PubMed:11248049, ECO:0000269|PubMed:9210376}.
Interaction partners:
- Actin-related protein 2/3 complex subunit 5
- Actin-related protein 3
- Actin-related protein 2/3 complex subunit 4
- Actin-related protein 2/3 complex subunit 2
- Actin-related protein 2/3 complex subunit 1
- Proline-rich protein LAS17
- Actin-related protein 2/3 complex subunit 3
- Actin
- Cofilin
- Protein AIM7
Sequence:
MDPHNPIVLDQGTGFVKIGRAGENFPDYTFPSIVGRPILRAEERASVATPLKDIMIGDEASEVRSYLQISYPMENGIIKNWTDMELLWDYAFFEQMKLPSTSNGKILLTEPPMNPLKNREKMCEVMFEKYDFGGVYVAIQAVLALYAQGLSSGVVVDSGDGVTHIVPVYESVVLSHLTRRLDVAGRDVTRHLIDLLSRRGYAFNRTADFETVRQIKEKLCYVSYDLDLDTKLARETTALVESYELPDGRTIKVGQERFEAPECLFQPGLVDVEQPGVGELLFNTVQSADVDIRSSLYKAIVLSGGSSMYPGLPSRLEKELKQLWFSRVLHNDPSRLDKFKVRIEDPPRRKHMVFIGGAVLASIMADKDHMWLSKQEWQESGPSAMTKFGPR
Protein: Glutathione transport system permease protein GsiC (P75798)
Organism: Escherichia coli (strain K12)
Function: Part of the ABC transporter complex GsiABCD involved in glutathione import. Probably responsible for the translocation of the substrate across the membrane.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Glutathione-binding protein GsiB
- Glutathione import ATP-binding protein GsiA
- Glutathione transport system permease protein GsiD
- Dipeptide transport system permease protein DppC
- Nickel transport system permease protein NikC
- Probable D,D-dipeptide transport system permease protein DdpC
- Isoaspartyl peptidase
- Oligopeptide transport system permease protein OppC
- Probable D,D-dipeptide transport ATP-binding protein DdpF
- Probable D,D-dipeptide-binding periplasmic protein DdpA
Sequence:
MLNYVIKRLLGLIPTLFIVSVLVFLFVHMLPGDPARLIAGPEADAQVIELVRQQLGLDQPLYHQFWHYISNAVQGDFGLSMVSRRPVADEIASRFMPTLWLTITSMVWAVIFGMAAGIIAAVWRNRWPDRLSMTIAVSGISFPAFALGMLLIQVFSVELGWLPTVGADSWQHYILPSLTLGAAVAAVMARFTRASFVDVLSEDYMRTARAKGVSETWVVLKHGLRNAMIPVVTMMGLQFGFLLGGSIVVEKVFNWPGLGRLLVDSVEMRDYPVIQAEILLFSLEFILINLVVDVLYAAINPAIRYK
Protein: Lys-63-specific deubiquitinase BRCC36 (EC 3.4.19.-) (BRCA1-A complex subunit BRCC36) (BRCA1/BRCA2-containing complex subunit 3) (BRCA1/BRCA2-containing complex subunit 36) (BRISC complex subunit BRCC36) (P46737)
Organism: Mus musculus (Mouse)
Function: Metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Does not have activity toward 'Lys-48'-linked polyubiquitin chains (By similarity). Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs) (By similarity). In the BRCA1-A complex, it specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX, antagonizing the RNF8-dependent ubiquitination at double-strand breaks (DSBs) (By similarity). Catalytic subunit of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates (By similarity). Mediates the specific 'Lys-63'-specific deubiquitination associated with the COP9 signalosome complex (CSN), via the interaction of the BRISC complex with the CSN complex (By similarity). The BRISC complex is required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating NUMA1 (By similarity). Plays a role in interferon signaling via its role in the deubiquitination of the interferon receptor IFNAR1; deubiquitination increases IFNAR1 activity by enhancing its stability and cell surface expression (By similarity). Acts as a regulator of the NLRP3 inflammasome by mediating deubiquitination of NLRP3, leading to NLRP3 inflammasome assembly. Down-regulates the response to bacterial lipopolysaccharide (LPS) via its role in IFNAR1 deubiquitination (By similarity). Deubiquitinates HDAC1 and PWWP2B leading to their stabilization.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P46736}. Cytoplasm {ECO:0000250|UniProtKB:P46736}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:P46736}. Note=Localizes at sites of DNA damage at double-strand breaks (DSBs). Interaction with ABRAXAS2 retains BRCC3 in the cytoplasm. {ECO:0000250|UniProtKB:P46736}.
Interaction partners:
- BRISC complex subunit Abraxas 2
- BRISC and BRCA1-A complex member 2
- BRISC and BRCA1-A complex member 1
- BRCA1-A complex subunit RAP80
- BRCA1-A complex subunit Abraxas 1
- Breast cancer type 1 susceptibility protein homolog
- BRCA1-associated RING domain protein 1
- NACHT, LRR and PYD domains-containing protein 3
- Serine hydroxymethyltransferase, mitochondrial
- Breast cancer type 2 susceptibility protein homolog
Sequence:
MAVQVVQAVQAVHLESDAFLVCLNHALSTEKEEVMGLCIGELNDDIRSDSKFTYTGTEMRTVQEKMDTIRIVHIHSVIILRRSDKRKDRVEISPEQLSAASTEAERLAELTGRPMRVVGWYHSHPHITVWPSHVDVRTQAMYQMMDQGFVGLIFSCFIEDKNTKTGRVLYTCFQSIQAQKSSEYERIEIPIHIVPHITIGKVCLESAVELPKILCQEEQDAYRRIHSLTHLDSVTKIHNGSVFTKNLCSQMSAVSGPLLQWLEDRLEQNQQHLQELQQEKEELMEELSSLE
Protein: Protein HEG (Heart of glass) (Q6R8J2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Receptor component of the CCM signaling pathway which is a crucial regulator of heart and vessel formation and integrity. May act through the stabilization of endothelial cell junctions.
Subcellular location: [Isoform 1]: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Cell junction {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 3]: Secreted {ECO:0000305}.
Interaction partners:
- Krev interaction trapped protein 1
- Cerebral cavernous malformations protein 2 homolog
- Programmed cell death protein 10-A
- Ras-interacting protein 1
- Krueppel-like factor 2a
Sequence:
MMETCARRVLFTAALLVLSTVIAETFSTDSDTDNPLSTETFYSRASGLKQTSSWPGREATATAVDLSSGLGEMTEIPASVSITAAREGHSPKPLQTSTNAADWKTSTTSDETTEHLQSDTELTHNATAQWESPSSASHSITSHHPVTETRTVRDVTDLIDMDTTDSVSHTDSTYISTTNRVGERTLLSVISNSTFAYTQNSSISDAESQTSPWEEKTSGATQVNEETEETVSTVSEQTDPTFEGRNTTSATLETERSTLSQGTESQTGQPSVTGQTAKEVTDIDNPNSTPPLTVTSRDVEETDATSVSSETSYTQTSSDSASSILPFTSSEHNVTSTSQESHNSTLIYSTNTGGSTEFSTGSVSSTAHEETERSSTRIVDETTLHDVTSAPPVLEDVATTIDDSLSKFPSGQSPTIPKTDDQTNTQVVPTSTHRPQVTDEATDEVSTVYSSTTTLTTTTPSVTTRQLQPHYTTVQTQTQHTTIVTTDIIQVLRTTPSTAHHVPTLTTSGPQAPSTADSSDVTTLHLETSTATPGNTTAHGGRATTPFSKSSPGRTTVVVTTGHLTDKSTTETGSATTQMPLRTSASPGHVCGPKTCANGGHCVRSAEGSYYCQCLSAWTGPFCTEDVDECVNSPCPQGSVCVNTGGSFSCECDLGFDLEDGRSCTQVKTFLGTFTVNNSLHLRNLGLHELHREIQQLLNASLSIFHGYRRFTLGKRDGQGVQIPVVSMFSLSSNVTSADVFNSIQMSLNNCSRTYSHCPIKLQHQLSYHVESLCMAQKTKCDVQYSDCSDISGIPNCQCLPGYFKRNPEDMTCRDCGDGLKLVNGKCVECMFGFGGFNCNNFYKLIAVVVSPAGGALLLIVVIALIVTCCKKDKNDINKIIFKSGELQMSPYAEFPKSNRVSMEWGRETIEMQENGSTKNLLQMTDIYYSPALRNSDLERNGLYPFSGLPGSRHSCIYPAQWNPSFLSDDSRRRDYF
Protein: Oxygen-independent coproporphyrinogen III oxidase (CPO) (EC 1.3.98.3) (Coproporphyrinogen III dehydrogenase) (CPDH) (P0A1E1)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Involved in the heme biosynthesis. Catalyzes the anaerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen III to yield the vinyl groups in protoporphyrinogen IX.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P32131}.
Interaction partners:
- Oxygen-dependent coproporphyrinogen-III oxidase
- Uroporphyrinogen decarboxylase
- Protoporphyrinogen IX dehydrogenase [quinone]
- Coproporphyrinogen III oxidase and related FeS oxidoreductase
- Ferrichrome-binding periplasmic protein
- Delta-aminolevulinic acid dehydratase
- Der GTPase-activating protein YihI
- Ferrochelatase
- Glutamyl-tRNA reductase
- Porphobilinogen deaminase
Sequence:
MSEQQIDWDLALIQKYNYSGPRYTSYPTALEFSEDFEDAAFLQAVARYPERPLSLYVHIPFCHKLCYFCGCNKIVTRQQHKADQYLDALEQEIRHRAPLFADRHVSQLHWGGGTPTYLNKAQISRLMTLLRENFHFNTDAEISIEVDPREIELDVLDHLRAEGFNRLSMGVQDFNKEVQRLVNREQDEEFIFALLNHARDIGFTSTNIDLIYGLPKQTPESFAFTLKRVTELNPDRLSVFNYAHLPTLFAAQRKIKDADLPSAQQKLDILQETIVSLTQAGYQFIGMDHFARPDDELAVAQREGVLHRNFQGYTTQGDTDLLGMGVSAISMIGDGYMQNQKELKRYYQQVDERGNALWRGITLTRDDCIRRDVIKALICNFRLDFNAVEQQWGLHFAEYFAEDLQLLSPLAKDGLVDISEKGIQVTAKGRLLIRNICMCFDAYLRQKARMQQFSRVI
Protein: ORF 63 (P88954)
Organism: Human herpesvirus 8 type M
Interaction partners:
Sequence:
MDGTDALEKLTKGLSGGGGSLHQTKLLMEFQLRGLPVPALLNSSTTEQFLNTVAQLPTDLSKFIRDYRVFALVRAAYFLEPPSSIDPLEAARALGRLVDILSSQPPQNTAPAQPPTSDDTLNNCTLLKLLAHYADQIAGFKTPALPPVPPGIIGLFTCVEQMYHACFQKYWAAALPPMWILTYDPPTSPLQDWLIVAYGNKEGLLLPSGIPSEEVLAKTLVTEHHELFVSRSNSTETAVTMPVSKERALAIYRVFAKGEVVAENTPILAFTDVELSTLKPHYLFIYDFIIEALCKSYTYSCTQARLESFLSRGIDFMTDLGQYLDTATSGKQQLTHSQIKEIKYRLLSCGLSASACDVFRTVIMTLPYRPTPNLANLSTFMGMVHQLTMFGHYFYRCLGSYSPTGLAFTELQKILTRASAEQTERNPWRHPGISDIPLRWKISRALAFFVPPAPINTLQRVYAALPSQLMRAIFEISVKTTWGGAVPANLARDIDTGPNTQHISSTPPPTLKDVETYCQGLRVGDTEYDEDIVRSPLFADAFTKSHLLPILREVLENRLQKNRALFQIRWLIIFAAEAATGLIPARRPLARAYFHIMDILEERHSQDALYNLLDCIQELFTHIRQAVPDAQCPHAFLQSLFVFQFRPFVLKHQQGVTLFLDGLQTSLPPVISLANLGDKLCRLEFEYDSEGDFVRVPVAPPEQPPHVHLSHFKKTIQTIEQATREATVAMTTIAKPIYPAYIRLLQRLEYLNRLNHHILRIPFPQDALSELQETYLAAFARLTKLAADAANTCSYSLTKYFGVLFQHQLVPTAIVKKLLHFDEAKDTTEAFLQSLAQPVVQGQRQGAAGGSGVLTQKELELLNKINPQFTDAQANIPPSIKRSYSNKYDVPEVSVDWETYSRSAFEAPDDELRFVPLTLAGLRKLFVE
Protein: Squalene synthase 1 (PgSS) (PgSS1) (PgssA) (SQS 1) (SQS 4) (EC 2.5.1.21) (FPP:FPP farnesyltransferase SS1) (Farnesyl-diphosphate farnesyltransferase SS1) (O48666)
Organism: Panax ginseng (Korean ginseng)
Function: Component of the triterpene saponins (e.g. ginsenosides or panaxosides) and phytosterols biosynthetic pathways. Catalyzes the biosynthesis of squalene.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P53799}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MGSLGAILKHPEDFYPLLKLKFAARHAEKQIPPEPHWAFCYSMLHKVSRSFGLVIQQLGPQLRDAVCIFYLVLRALDTVEDDTSIPTEVKVPILMAFHRHIYDKDWHFSCGTKEYKVLMDEFHHVSNAFLELGSGYQEAIEDITMRMGAGMAKFICKEVETINDYDEYCHYVAGLVGLGLSKLFHASGAEDLATDSLSNSMGLFLQKTNIIRDYLEDINEIPKSRMFWPRQIWSKYVDKLEDLKYEENSAKAVQCLNDMVTDALVHAEDCLKYMSDLRGPAIFRFCAIPQIMAIGTLALCFNNTQVFRGVVKMRRGLTAKVIDQTKTMSDVYGAFFDFSCLLKSKVDNNDPNATKTLSRLEAIQKTCKESGTLSKRKSYIIESESGHNSALIAIIFIILAILYAYLSSNLLLNKQ
Protein: Beta-glucosidase 7 (Os3bglu7) (EC 3.2.1.21) (Q75I93)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Hydrolyzes p-nitrophenyl beta-D-glucoside, p-nitrophenyl beta-D-mannoside, p-nitrophenyl beta-D-galactoside, p-nitrophenyl beta-D-xyloside, p-nitrophenyl beta-D-fucoside, p-nitrophenyl beta-L-arabinoside, oligosaccharides, pyridoxine beta-D-glucoside and the cyanogenic glucosides amygdalin, prunasin and dhurrin. Possesses pyridoxine transglucosylation activity.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Os01g0542000 protein.
Sequence:
MAARRANCALVLVLALALLAARDAGAAAVPKPNWLGGLSRAAFPKRFVFGTATSAYQVEGMAASGGRGPSIWDAFAHTPGNVAGNQNGDVATDQYHRYKEDVNLMKSLNFDAYRFSISWSRIFPDGEGRVNQEGVAYYNNLINYLLQKGITPYVNLYHYDLPLALEKKYGGWLNAKMADLFTEYADFCFKTFGNRVKHWFTFNEPRIVALLGYDQGTNPPKRCTKCAAGGNSATEPYIVAHNFLLSHAAAVARYRTKYQAAQQGKVGIVLDFNWYEALSNSTEDQAAAQRARDFHIGWYLDPLINGHYPQIMQDLVKDRLPKFTPEQARLVKGSADYIGINQYTASYMKGQQLMQQTPTSYSADWQVTYVFAKNGKPIGPQANSNWLYIVPWGMYGCVNYIKQKYGNPTVVITENGMDQPANLSRDQYLRDTTRVHFYRSYLTQLKKAIDEGANVAGYFAWSLLDNFEWLSGYTSKFGIVYVDFNTLERHPKASAYWFRDMLKH
Protein: Anion exchange protein (M9PB60)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Basolateral cell membrane {ECO:0000256|ARBA:ARBA00004554}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004554}. Membrane {ECO:0000256|RuleBase:RU362035}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU362035}.
Interaction partners:
Sequence:
MAEKNEYIELPWTMNSSSGDDEAPKDPRTGGEDFTQQFTENDFEGHRAHTVYVGVHVPGGRRHSQRRRKHHHSGPGGGGGGGGGGGSIGGSGSVGGGAGKDNVSEKQQEVERPVTPPAQRVQFILGEDVDDGTHVSHPLFSEMGMLVKEGDEIEWKETARWIKFEEDVEEGGNRWSKPHVATLSLHSLFELRRLLVNGSVMLDMEAQNLEVMADLVCDHMVSAGTLPPGVKDKVKDALLRRHRHQHEYAKKTRLPIIRSLADMRNHSSSKNLGKSTPLHSLHGSAAGLDLTGTRPDQTPLYVSSKDQRGCYLAVPTEDMVKSPSNQSMARPGSGTELSEQQHKGNTHFMRKIPPGAEASNILVGEVDFLERTLSCFIRLSQAVVLGDLTEVPVPTRFVFILLGPPGSQSNFHEIGRAMATLMSDEIFHEVAYRARKRDHLLSGVDEFLDAVTVLPPGEWDPTIRIEPPAAIPSQEVRKRPPELPKEEVDEEEEEARLREENGLSRTGRLFGGLINDIKRKAPWYISDYKDALSMQCVASWIFLYFACLSPIITFGGLLAEATGKHMAAMESLVSGFVCGMGYGFFSGQPLTILGSTGPVLVFESIIYEFCLKMGWDYMTFRFWIGMWVAGICIVLTAIDASALVCYITRFTEENFATLIAFIFIYKAIENVMVIGKNFPVNQGIYDCVCTPPIGSNASVIDYAKYNWDSCESYNGTLVGGDCGTPPTENVFLMSVVLCAGTFLISTVLKEFKNALFFPSIVRQYISDFSVLIAIFAMSFFDYSLGVPTQKLEVPNELKPTLSTRGWLIPPFVEKNPWWSAIIAVFPALLGTILIFMDQQITAVIVNRKENKLKKGCGYHLDLFILSILIAICSMMGLPWFVAATVLSINHVNSLKLESECSAPGEKPQFLGVREQRVTHILIFLTIGVSVLLTPLLGNIPMPVLFGVFLYMGVASLKGLQFFDRILIMFMPAKYQPDYMFLRQVPIKRVHLFTMIQLACLIILWLIKSFSQTSILFPLMLVVMIGIRKALDLVFTRRELKILDDIMPEMTKRAAADDLHKLDAEVGLLARIFPWGKGSRSRVVTKPPGLDDGIVGSGGAVGAGLITCTTSNANEKEFEAQSSLLKK
Protein: Azurocidin 1 (A0A087WXP0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTAASCFQSQNPGVSTVVLGAYDLRRRERQSRQTFSISSMSENGYDPQQNLNDLMLLQLDREANLTSSVTILPLPLQNATVEAGTRCQVAGWGSQRSGGRLSRFPRFVNVTVTPEDQCRPNNVCTGVLTRRGGICNVSAPCGGRRGPERY
Protein: Ion-translocating oxidoreductase complex subunit A (EC 7.-.-.-) (Rsx electron transport complex subunit A) (P0A766)
Organism: Escherichia coli (strain K12)
Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane (By similarity). Required to maintain the reduced state of SoxR. Probably transfers electron from NAD(P)H to SoxR.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00459, ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00459}.
Interaction partners:
- Ion-translocating oxidoreductase complex subunit D
- Ion-translocating oxidoreductase complex subunit C
- Ion-translocating oxidoreductase complex subunit B
- Ion-translocating oxidoreductase complex subunit G
- Ion-translocating oxidoreductase complex subunit E
- Inner membrane protein YdgK
- FAD:protein FMN transferase
- Endonuclease III lyase)
- Probable pyruvate-flavodoxin oxidoreductase
Sequence:
MTDYLLLFVGTVLVNNFVLVKFLGLCPFMGVSKKLETAMGMGLATTFVMTLASICAWLIDTWILIPLNLIYLRTLAFILVIAVVVQFTEMVVRKTSPVLYRLLGIFLPLITTNCAVLGVALLNINLGHNFLQSALYGFSAAVGFSLVMVLFAAIRERLAVADVPAPFRGNAIALITAGLMSLAFMGFSGLVKL