wanglab/gogpt-training-data huggingface dataset:
Protein: Oxidation resistance protein 1 (Q0KIB9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
MSIIDSGKYRLRKDWASASIPSLVNIDEHDGDSGDTEGSLNATAPLPPQKPPRRSSLALGLFSSKSDKSQKRRSSIAVSFLRRDSSKNSTKDSYESAVRSEKSDGSGTPTSPEIVYSSEENIRASSPNDPGKQTFFEDGSQSPRPVLQGLNTSYEGPQNDRQRRRRSSLQTKLDRHRRKKMEYSNQRSLDSGMMCSESHSDLTNDSLAEGSGSFANRSRNGNDDEDDIIDPSHGEYFPREKRHSWWNIFVPDNFKNRSRRASQDVSSLSRSVDNLAIPVRRSKSRSVDHGLAAPFDLDSLRSKVEQRFESVDKLSRQKSSLPTIPTISYTVGNRDTLTSVAARFDTTPSELTHLNRLNSSFIYPGQQLLVPDKSAKDDASSSSTHDADGASLSGKSSPVERKLSGDESREKDILEGLRPGSPKPGHIERVGGSSQQQQAEEEANKSDDPVITQRFLKINVRHITDGQGVVGGVLLVTPNAVMFDPNVSDPLVIEHGPESYGVIAPMELVVNAAIFHDIAHMRVAGGAGQGLNSASGDAEKPEIYYPKPVLVEEDSKELPEQQSLLGEDGNKRLDAEIGSLEIADDQESLCSSTGRDGDAFPKAFDRERVEDSSMEAKDSAKTDALDDEDKKAGLGLSSTRSTLEERRKSLLDHHWAIPSKDRSSEDEGDNESNVTVDSGARVQDPHSANSSVSGVPLSQPPVAAAAAAAAVAPASAVVPLPPSGIDLEHLEQLSKQSCYDSGIDIREPVPNVQPIPKKTVYSDADIVLSSDWVPPKTIVPTHFSESPPRSTILGQSLDAGTGGAGGVRKKTSSVSFSVDDEAAQQAQAQSAALAVTDKQADKKNKMLKRLSYPLTWVEGLTGEGGAVPPGGVGSGSLNKSGDTDSAPNTGDSNQSVFSKVFSSSPITLVSELGGNLFSKTPSEDSGGSPVPPLTPHSTHSEGHMTYGRSSIGTFIRPHSSEGTSSSTKLKEAKQAPKLDYRSMVSMDDKPELFISVDKLIPRPARACLDPPLYLRLRMGKPIGKAIPLPTSVMSYGKNKLRAEYWFSVPKNRVDELYRFINTWVKHLYGELDEEQIKARGFELIQEDTEWTKSGTTKAGMGGGSQDGEEISDLTRESWEVLSMSTDEYRKTSLFATGSFDLDFPIPDLIGKTEILTEEHREKLCSHLPARAEGYSWSLIFSTSQHGFALNSLYRKMARLESPVLIVIEDTEHNVFGALTSCSLHVSDHFYGTGESLLYKFNPSFKVFHWTGENMYFIKGNMESLSIGAGDGRFGLWLDGDLNQGRSQQCSTYGNEPLAPQEDFVIKTLECWAFV
Protein: UDP-glucuronate:xylan alpha-glucuronosyltransferase 2 (UDP-GlcA:xylan glucuronyltransferase 2) (EC 2.4.1.-) (Glycogenin-like protein 2) (Plant glycogenin-like starch initiation protein 3) (Protein GLUCURONIC ACID SUBSTITUTION OF XYLAN 2) (AtGUX2) (Q8GWW4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Glycosyltransferase required for the addition of both glucuronic acid and 4-O-methylglucuronic acid branches to xylan in stem cell walls. In association with GUX1, is responsible for almost all of the substitutions of the xylan backbone in stem glucuronoxylan.
Subcellular location: Golgi apparatus membrane {ECO:0000305|PubMed:20852069, ECO:0000305|PubMed:21124849}; Single-pass type II membrane protein {ECO:0000305|PubMed:20852069, ECO:0000305|PubMed:21124849}.
Interaction partners:
- Beta-1,4-xylosyltransferase IRX9
- Probable beta-1,4-xylosyltransferase IRX14H
- Probable beta-1,4-xylosyltransferase IRX9H
- Probable beta-1,4-xylosyltransferase IRX10L
- Probable beta-1,4-xylosyltransferase IRX10
- Beta-1,4-xylosyltransferase IRX14
- Probable galacturonosyltransferase 12
- Protein IRREGULAR XYLEM 15
- Glucuronoxylan 4-O-methyltransferase 3
- Glucuronoxylan 4-O-methyltransferase 1
Sequence:
MTIMTMIMKMAPSKSALIRFNLVLLGFSFLLYTAIFFHPSSSVYFSSGASFVGCSFRDCTPKVVRGVKMQELVEENEINKKDLLTASNQTKLEAPSFMEEILTRGLGKTKIGMVNMEECDLTNWKRYGETVHIHFERVSKLFKWQDLFPEWIDEEEETEVPTCPEIPMPDFESLEKLDLVVVKLPCNYPEEGWRREVLRLQVNLVAANLAAKKGKTDWRWKSKVLFWSKCQPMIEIFRCDDLEKREADWWLYRPEVVRLQQRLSLPVGSCNLALPLWAPQGVDKVYDLTKIEAETKRPKREAYVTVLHSSESYVCGAITLAQSLLQTNTKRDLILLHDDSISITKLRALAAAGWKLRRIIRIRNPLAEKDSYNEYNYSKFRLWQLTDYDKVIFIDADIIVLRNLDLLFHFPQMSATGNDVWIYNSGIMVIEPSNCTFTTIMSQRSEIVSYNGGDQGYLNEIFVWWHRLPRRVNFLKNFWSNTTKERNIKNNLFAAEPPQVYAVHYLGWKPWLCYRDYDCNYDVDEQLVYASDAAHVRWWKVHDSMDDALQKFCRLTKKRRTEINWERRKARLRGSTDYHWKINVTDPRRRRSYLIG
Protein: Chloride channel protein (Q7JZ25)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361221}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361221}.
Interaction partners:
- GH26007p
Sequence:
MDDRKALITLDGESSAEDDPIILQKEAGPTSKAVQDFGLHQREEPSTSALARRATLSGNNHLLDDSQPLLMGNNSVPPDIPINGSAGSPNRNINSSEPIFHLRSRTAAASTPNYESLDYEVCENTLFQDEQRKRLTERFSLRKDIIRWIIFIQIGIITALIACTIDIIIEELSIRKYTFLYNSVKENVPLSDASDRDLLIPYLYWLLFSIVPVAFGAAMVTYIEPITAGSGIPQVKSYLNGVKIPRIVRIKTLAVKAIGVITSVVGGLAGGKEGPMIHAGAVVAAGISQGKSTTFLKDFRIFKAFRDDHEKRDFVLGGGAAGVSAAFGAPIGGMLFSLEEAASFWNQNLIWRTLVASIISVFTLNIVLSAYHGLNDFTFTGLFNLGKFDTPLKFDYFELPIFMILGVTGGLLGAAWNSLNTKINKFRKRFIPWKIGKVLEAVVVAMMGVTLACLMIYFINDCRPLGNDPTNNPVQLFCEDNEYNAVAALWFQTPEATVRSLFHDPPGSHKILTLALFTVVYYVLSCATFGLNVSLGVFIPTALVGAAWGRLLAMLTYYVFPQAEFLHPGKYALIGAAANLGGVLRMTISLSVILMETTGVETSFFFPLIIALISAKWVGDYFNEGIYDTQIQVNHVPMLTWEPLPQYKGLKAREILSKPVICIKIRDSANYIYEMLKKCDHNGFPVVDDVCGDRRSEGRVCGIILRSQLIVILLKSLYVENKRFWLPETSIQTFRDLYPRFPSIKSVRKLDEKINYTVDLSMFMNPSPIRVNPHDSVPRIFQIFRALGLRHLLVINHENRIAGIITRRDFIYK
Protein: Large ribosomal subunit protein mL42 (S4R2Z7)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
MAVAAVKWVMSKRTILKHLFPVQNGALYCVCHKSTYSPLPDDYNCNVELALTSDGRTIVCYHPSVDIPYEHTKPIPRPDPVHNNEETHDQVLKTRLEEKVEHLEEGPMIEQLSKMFFTTKHRWYPHGRGKVSLTVLRRLILNSWTQVILLPQLGL
Protein: Protein AHC1 (ADA HAT complex component 1) (Q12433)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Functions as component of the transcription regulatory histone acetylation (HAT) complex ADA. ADA preferentially acetylates nucleosomal histones H3 (at 'Lys-14' and 'Lys-18') and H2B. AHC1 is required for the overall structural integrity of the ADA complex.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- ADA histone acetyltransferase complex component 2
- SAGA complex subunit NGG1
- Histone acetyltransferase GCN5
- SAGA complex subunit SGF29
- SAGA complex subunit SPT7
- SAGA complex subunit ADA2
- SAGA complex subunit SGF73
- SAGA complex subunit SPT8
- SAGA complex subunit SGF11
- SAGA complex/transcription factor TFIID complex subunit TAF12
Sequence:
MMSPAQDKLQHQHHNPNSSSSSSSKMTNVYQVTTPKSPQDLENNMDEPFKMDTATSNPDKDSENTQRLKYECAKGEIQNVLNLHIMLNHKHVRHLRRNVQKVNAKLALLETLHKDTGLLNKIERTYQLKIKQHQQHSVLGGHFHDSTATENTNASNYNLSYPVLSDYNINCQPLSSSSNRNLSTTRIPHHHYHTRSKSNGLLLEPSALRPANSNIIDYRLTGSKSLSEAITKPTPVSLPHSNSDGISSPRSSSISPLDEQPGFQILPFKPSQMHLNHRRNYSSTCLTSNSGIIGKTENNEPIFRRYDGILVIITCSKCDRSGFTSAQGIVNHTRLKHSKLYSSQPLAVLNNQKLLPNDKQDPEILSKFKKLNLDPNKDYLPSDIAIPKPQSPINHSENHTRAPKTVKNTPHLEKLYQNKEDFKKLIDMVNETPDDLNEYLKQREIQLRYQKEQEEESSKSDDEASYVPSPSLSATATTTTTTDPPSPPVLSSSLQRKLLRKRKLSLNSSTPMEDLPLRERLRANPTDKKPRKAALLTNELEGPDPAAKSSSYYNLRSKSRLRGSHT
Protein: Lanosterol synthase (EC 5.4.99.7) (Q1G1A4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Converts oxidosqualene to lanosterol.
Interaction partners:
- Sterol 14-demethylase
- Delta
- Squalene epoxidase 2, mitochondrial
- Squalene epoxidase 6
- Squalene epoxidase 5
- Squalene epoxidase 3
- Squalene epoxidase 1
- Squalene epoxidase 4
- Ergosterol biosynthetic protein 28
- Delta
Sequence:
MWRLKLSEGDEESVNQHVGRQFWEYDNQFGTSEERHHINHLRSNFTLNRFSSKHSSDLLYRFQCWKEKGKGMERLPQVKVKEGEERLINEEVVNVTLRRSLRFYSILQSQDGFWPGDYGGPLFLLPALVIGLYVTEVLDGTLTAQHQIEIRRYLYNHQNKDGGWGLHVEGNSTMFCTVLSYVALRLMGEELDGGDGAMESARSWIHHHGGATFIPSWGKFWLSVLGAYEWSGNNPLPPELWLLPYSLPFHPGRMWCHCRMVYLPMSYLYGRRFVCRTNGTILSLRRELYTIPYHHIDWDTARNQCAKEDLYYPHPKIQDVLWSCLNKFGEPLLERWPLNNLRNHALQTVMQHIHYEDQNSHYICIGPVNKVLNMLCCWVESSNSEAFKSHLSRIKDYLWVAEDGMKMQGYNGSQLWDVTLAVQAILATNLVDDYGLMLKKAHNYIKNTQIRKDTSGDPGLWYRHPCKGGWGFSTGDNPWPVSDCTAEALKAALLLSQMPVNLVGEPMPEEHLVDAVNFILSLQNKNGGFASYELTRSYPELEVINPSETFGDIIIDYQYVECTSAAIQGLVLFTTLNSSYKRKEIVGSINKAVEFIEKTQLPDGSWYGSWGVCFTYATWFGIKGMLASGKTYESSLCIRKACGFLLSKQLCCGGWGESYLSCQNKVYTNLPGNKSHIVNTSWALLALIEAGQASRDPMPLHRGAKSLINSQMEDGDYPQQEILGVFNRNCMISYSAYRNIFPIWALGEYRKLMLSL
Protein: Tachykinin-related peptide 5 (TKRP-5) (P86567)
Organism: Banasa dimiata (Banasa stink bug) (Pentatoma dimiata)
Subcellular location: Secreted {ECO:0000269|PubMed:19084564, ECO:0000305}.
Interaction partners:
Sequence:
APLMGFQGVR
Protein: Dual specificity protein phosphatase lip-1 (EC 3.1.3.16) (EC 3.1.3.48) (Lateral signaling-induced phosphatase 1) (Mitogen-activated protein kinase phosphatase lip-1) (MAP kinase phosphatase lip-1) (V6CIV8)
Organism: Caenorhabditis elegans
Function: Dephosphorylates MAP kinase mpk-1.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12169634, ECO:0000269|PubMed:16319922}; Peripheral membrane protein {ECO:0000269|PubMed:12169634, ECO:0000269|PubMed:16319922}. Note=Localizes in rod-like structures at the plasma membrane of pachytene germline cells. {ECO:0000269|PubMed:12169634, ECO:0000269|PubMed:16319922}.
Interaction partners:
- Mitogen-activated protein kinase mpk-1
- Mitogen-activated protein kinase pmk-3
- Mitogen-activated protein kinase pmk-2
- Mitogen-activated protein kinase pmk-1
- Stress-activated protein kinase JNK
- GLH-binding kinase 1
- Stress-activated protein kinase jnk-1
- Tyrosine-protein phosphatase vhp-1
- Ack-related non-receptor tyrosine kinase
- Lateral signaling target 1 protein
Sequence:
MTTHLPSTSQNGEEISAEQFNRIFHERNVIVLDCRSNGDSVKRANRFFCSLRLPALLQRRLMGGSMRLSTVPDLKDLNNSPDQCPEVLLIPGDSEQDEQLSAALARNLKSNHYRHFVLGEPVKTLLSQFPTLRDAADENWNTTFQMNSMPGQASGQQASSGPLLNLNQLRLEGEDQGGKQRAEFPVKLTNFLYLGNAETAKNRDVLKKYSISHVINVTSNLPNTFEEDPNMRYLRISADDNASHNLTKFFPEAISFIDDARRNDSACLVHCLAGISRSVTICLAYLMKTEMCTLDSAYEWVQKRNASIAPNFHFMGQLTDYEKMLGLNSNRVGTYPSSAPRSPSCAIEAAAVSQVGGLLTPPPTSCSASPQSSNHSAKSFH
Protein: Biogenesis of lysosome-related organelles complex 1 subunit 5 (BLOC-1 subunit 5) (Protein Muted homolog) (Q18446)
Organism: Caenorhabditis elegans
Function: Component of the biogenesis of lysosome-related organelles complex-1 (BLOC-1) involved in gut granule biogenesis.
Interaction partners:
- Biogenesis of lysosome-related organelles complex 1 subunit 4
- Biogenesis of lysosome-related organelles complex 1 subunit 2
- Biogenesis of lysosome-related organelles complex 1 subunit 1
- Dysbindin protein homolog
- Biogenesis of lysosome-related organelles complex 1 subunit 6
- SNAPIN protein homolog
Sequence:
MATIPSVVREITLVGEQIFDHTQVVRAEIDRFVERFERNERHREFDGILRASHALVESSETPVEGLFDMGKMEHMTQCVDDITKKLQTLVEPKYQKEHDVYLEKVKEDQKKYVDVCREQAMNKMRSMTAHR
Protein: Protein SVS1 (Q12254)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for vanadate resistance.
Interaction partners:
- Protein PRY2
- Protein TOS6
Sequence:
MIFKILCSLLLVTSNFASALYVNETTSYTPYTKTLTPTYSVSPQETTLTYSDETTTFYITSTFYSTYWFTTSQSAAIISTPTASTPTASTPSLTTSTNEYTTTYSDTDTTYTSTLTSTYIITLSTESANEKAEQISTSVTEIASTVTESGSTYTSTLTSTLLVTVYNSQASNTIATSTAGDAASNVDALEKLVSAEHQSQMIQTTSADEQYCSASTKYVTVTAAAVTEVVTTTAEPVVKYVTITADASNVTGSANNGTHI
Protein: Monothiol glutaredoxin-S10 (AtGrxS10) (Protein ROXY 3) (Q9LIF1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May only reduce GSH-thiol disulfides, but not protein disulfides.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Cationic amino acid transporter 4
Sequence:
MDVVARLASQRAVVIFSKSTCCMSHAIKRLFYEQGVSPAIVEIDQDMYGKDIEWALARLGCSPTVPAVFVGGKFVGTANTVMTLHLNGSLKILLKEAGALWL
Protein: Uncharacterized protein (Q381A6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MKGKYMHSTVSYTRDHFTTEYGYPIREFHQNNPHEEQRRVQAVGFAVHHSRPSMVFFARALQECSMELHIGPYGQLTLSVGAEGEVIILRPRAGDVLCKLSEFPTYYELCRAFFAGSGAGPSALHPKKDFKRKQQLIDGHGRLLVLCASLLRQLLSSEARYPVVDTMSATRNRLRIIRILRALTSPGELRDISVSPISVDGEVSAMDFIERIVTASLRDLQVPSHRCKTSVPRSVLAGCIHFTLSTEVEGDALLVLEKLLLDFLCTPFHHGRNAVPAQTISARARLLLEDPATCLVPCLGSALTYSRSFPCGSFFLPTVAPTFNAHQGADTPHFVLDGRGTIGSGSRNCDGSCTDSATSGGRCYLVMLLVIDHEGGLLDFLHARPPPPPPTRSNESEVGEVEMGRPKGGARQIEGEWTSADQQKAQLEASRMLYDWAWANDVSVIITPSHAPPVMKTFGARYYAERNSHNGVVGAAPVFMVDEVDTTAFDAMIRRLQVCRRDTFSTSEDMCACPDVAVLRRGRLVLPDRLANVIIPARFVAHGDLETLLAPHFPFTGPKRVDSSAKRGLLLKIDGNTSSPTPACPHDAAVGEVGTMLLVSPSSHLQRSHIALLLKCAGCVLLAVDTSVAGRGWAAECGLGFVRAGGALQMSLARQMRAIAESLRSSAGGCQCQSASIPLTGDVPVLAAVLDVLSEALCELPRRVVGYVTDHHYPLRRAWLQFESDELWRRSENPRPSMRAVHNASALHVYIREDLAFYDDHINVTSYDRETQRRYFCKSDTESSGSDNSESEGPTSRVASGFCGSVDWNEGPATLSFVEPVAVTAGMLRAALTFVRLVLSSENTLEANV
Protein: Regulator of G-protein signaling 3 (RGS3) (C2PA) (Q9DC04)
Organism: Mus musculus (Mouse)
Function: Down-regulates signaling from heterotrimeric G-proteins by increasing the GTPase activity of the alpha subunits, thereby driving them into their inactive GDP-bound form. Down-regulates G-protein-mediated release of inositol phosphates and activation of MAP kinases.
Subcellular location: Cytoplasm {ECO:0000305}. Cell membrane {ECO:0000250|UniProtKB:P49796}; Peripheral membrane protein {ECO:0000250|UniProtKB:P49796}; Cytoplasmic side {ECO:0000250|UniProtKB:P49796}. Note=Long isoforms are cytoplasmic and associated with the plasma membrane. Short isoforms are nuclear. {ECO:0000250|UniProtKB:P49796}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:11301003}.; SUBCELLULAR LOCATION: [Isoform 3]: Nucleus {ECO:0000269|PubMed:12210723}.; SUBCELLULAR LOCATION: [Isoform 4]: Nucleus {ECO:0000305}.
Interaction partners:
- Ephrin-B2
- Ephrin-B1
- Ephrin-B3
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit beta-5
- Regulator of G-protein signaling 12
Sequence:
MNRFNGLCKVCSERRYRQITIRRGKDGFGFTICCDSPVRVQAVDSGGPAERAGLQQLDTVLQLNERPVEHWKCVELAHEIRSCPSEIILLVWRVVPQIKPGPDGGVLRRASCKSTHDLLSPPNKREKNCTHGAPVRPEQRHSCHLVCDSSDGLLLGGWERYTEVGKRSGQHTLPALSRTTTPTDPNYIILAPLNPGSQLLRPVYQEDTIPEEPGTTTKGKSYTGLGKKSRLMKTVQTMKGHSNYQDCSALRPHIPHSSYGTYVTLAPKVLVFPVFVQPLDLCNPARTLLLSEELLLYEGRNKTSQVTLFAYSDLLLFTKEEEPGRCDVLRNPLYLQSVKLQEGSSEDLKFCVLYLAEKAECLFTLEAHSQEQKKRVCWCLSENIAKQQQLAAPPTERKMFETEADEKEMPLVEGKGPGAEEPAPSKNPSPGQELPPGQDLPPSKDPSPSQELPAGQDLPPSKDPSPSQELPAGQDLPPSKDPSPSQELPVGQDLPPRKDSSGQEAAPGPESPSSEDIATCPKPPQSPETSTSKDSPPGQGSSPTTELPSCQGLPAGQESTSQDPLLSQEPPVIPESSASVQKRLPSQESPSSLGSLPEKDLAEQTISSGEPPVATGAVLPASRPNFVIPEVRLDNAYSQLDGAHGGSSGEDEDAEEGEEGGEGEEDEEDDTSDDNYGDRSEAKRSSLIETGQGAEGGFSLRVQNSLRRRTHSEGSLLQESRGPCFASDTTLHCSDGEGATSTWAIPSPRTLKKELGRNGGSMHHLSLFFTGHRKMSGTDLTECDEASRKRKSKNIAKDMKNKLAIFRRRNESPGAQPASKTDKTTKSFKPTSEEALKWSESLEKLLLHKYGLEVFQAFLRTEFSEENLEFWLACEDFKKVKSQSKMAAKAKKIFAEFIAIQACKEVNLDSYTREHTKENLQSITRGCFDLAQKRIFGLMEKDSYPRFLRSDLYLDLINQKKMSPPL
Protein: Protein EARLY-RESPONSIVE TO DEHYDRATION 7, chloroplastic (O48832)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
- Senescence/dehydration-associated protein At4g35985
- Senescence/dehydration-associated protein At3g51250
- Dehydrin ERD10
- Low-temperature-induced 78 kDa protein
- Dehydrin COR47
- Hyperosmolality-gated Ca2+ permeable channel 3.1
- Protein RESPONSE TO ABA AND SALT 1
- Cold-regulated 413 plasma membrane protein 1
- TRAF-like family protein
- Gb|AAF32477.1
Sequence:
MESSGDKQTSSLYPTVDTSNPEAPINPSSSSSTNNLYPSLDMNDLARNLFPEQPETSSIPVSAPPAATEEVILKISGAILHLIDKSYSVELACGDLEIIRIVQGENVVAVLASVSDEIQWPLTKDENSVKVDESHYFFTLRPTKEISHDSSDEEDGDGGKNTNEMLNYGLTIASKGQEHLLVELEKILEDYSSFSVQEVSEEAKEAGEKVLDVTVARETSPVELTGERKEIVERQCSAYWTTLAPNVEDYSGKAAKLIATGSGHLIKGILWCGDVTMDRLIWGNGFMKRRLSKAEKESEVHPDTLKRIRRVKRMTKMTESVANSILSGVLKVSGFFTSSVANTKVGKKFFSLLPGEVILASLDGFNKVCDAVEVAGRNVMSTSSTVTTELVDHKYGGKAAEATNEGLDAAGYALGTAWVAFKIRKAINPKSVLKPSTLAKTAIRSAASQKKA
Protein: Inhibin beta A chain (Activin beta-A chain) (P18331)
Organism: Rattus norvegicus (Rat)
Function: Inhibins and activins inhibit and activate, respectively, the secretion of follitropin by the pituitary gland. Inhibins/activins are involved in regulating a number of diverse functions such as hypothalamic and pituitary hormone secretion, gonadal hormone secretion, germ cell development and maturation, erythroid differentiation, insulin secretion, nerve cell survival, embryonic axial development or bone growth, depending on their subunit composition. Inhibins appear to oppose the functions of activins.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P08476}.
Interaction partners:
- Activin receptor type-2A
- Follistatin
- Inhibin alpha chain
- Activin receptor type-2B
- Activin receptor type-1B
- Inhibin beta B chain
- Activin receptor type-1C
- Follistatin-related protein 3
- Transforming growth factor beta-3 proprotein
- Transforming growth factor beta-2 proprotein
Sequence:
MPLLWLRGFLLASCWIIVRSSPTPGSEGHGAAPDCPSCALATLPKDGPNSQPEMVEAVKKHILNMLHLKKRPDVTQPVPKAALLNAIRKLHVGKVGENGYVEIEDDIGRRAEMNELMEQTSEIITFAESGTARKTLHFEISKEGSDLSVVERAEVWLFLKVPKANRTRTKVTIRLFQQQKHPQGSLDMGDEAEEMGLKGERSELLLSEKVVDARKSTWHIFPVSSSIQRLLDQGKSSLDVRIACEQCQESGASLVLLGKKKKKEVDGDGKKKDGSDGGLEEEKEQSHRPFLMLQARQSEDHPHRRRRRGLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSGYHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMRGHSPFANLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS
Protein: Xanthotoxol synthase (EC 1.14.14.-) (Cytochrome P450 CYP71AZ4) (Fraxetin synthase) (EC 1.14.14.-) (A0A2Z5D854)
Organism: Pastinaca sativa (Wild parsnip) (Anethum pastinaca)
Function: Involved in the biosynthesis of coumarins and furanocoumarins (FCs), natural products required for defense responses against attacks by predators with potential medical and agroindustrial usages such as anticoagulant, rodenticide and artificial vanilla substitutes. Catalyzes the conversion of psoralen into xanthotoxol and of 6-methoxycoumarin into scopoletin. Can also convert with a lower efficiency scopoletin into fraxetin and 7-methoxycoumarin into daphnetin-7-methylether, and use 7-methoxy-3-methylcoumarin as substrate.
Subcellular location: Microsome membrane {ECO:0000250|UniProtKB:Q6QNI4}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MDPAAIFLILAIPIASVYLLFYHKKRVNGLSSPPGPRGLPFIGHFYQIYKSECAHEYISNLSKQYGSLMTLHLGSVPALVVSSPKMAQEVLKTQDLVFCSRAQMTGSGKLSYNGLEMAFAPYGEHWRNVRKMCTLELFTQKRAQFNFRPVREDEVSRMVGRLSEAAAASEDVNAYECFTNFATSIISRVAFGKRYDEDNLGKEKFQRMVADIEAMFAAFFVSDFFPMFGWIDRLSGVKAVLDRNFNEMDTFYQELIDEHLKPDRPESLNGDLIDVMLKNKGSFLTMDSIKAILLNVFSGGIGTTGSALVFAMTALLRNQRVMKKAQEEVRSVIGKKEIVDEDDIQKLPYLRAVVKETLRLYPPGPLLIPRVAMESCVLGEDEDHMYMIKPNTIVYVNTWGIGRDPKYWKNPLEFMPERFFERPDLNYTGQQFEYLPFGSGRRICAGIIIGQNNVEVGLANLLYSFDWEPPTGKTFEDIDDQPCNGLTLAKKNPLYIRPKIYVHP
Protein: THUMP domain-containing protein (A0A0H2UNG1)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Interaction partners:
Sequence:
MKKEFNLIATVAAGLEAVVGREVRELGYDCQVENGRVRFQGDVRAIIETNLWLRAADRIKIIVGTFPAKTFEELFQGVFALDWENYLPLGARFPISKAKCVKSKLHNEPSVQAISKKAVVKKLQKHYARPEGVPLMENGPEFKIEVSILKDVATVMIDTTGSSLFKRGYRTEKGGAPIKENMAAAILQLSNWYPDKPLIDPTCGSGTFCIEAVMIARKMAPGLRRSFAFEEWNWISDRLIQEVRTEAAKKVDRELELDIMGCDIDARMVEIAKANAQVAGVAGDITFKQMRVQDLRSDKINGVIISNPPYGERLSDDAGVTKLYAEMGQVFAPLKTWSKFILTSDEAFESKYGSQADKKRKLYNGTLKVDLYQYFGQRVKRQEVK
Protein: Uncharacterized protein (H3BN11)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSFLLPKLTSKKEVDQAIKSTAEKVLVLRFGRDEDPVCLQLDDILSKTSSDLSKMAAIYLVDVDQTAVYTQYFDISYIPSTVFFFNGQHMKVDYGGEDPALRSIKAVRRTSPAGTLG
Protein: Bifunctional aspartate aminotransferase and L-aspartate beta-decarboxylase (EC 2.6.1.1) (EC 4.1.1.12) (Aspartate 4-decarboxylase) (Asd) (AsdP) (Q53IZ1)
Organism: Pseudomonas sp
Function: Bifunctional enzyme that has both L-aspartate decarboxylase and transaminase activity. Has high activity with L-aspartate, and much lower activity with D-aspartate, L-lysine and L-glutamine.
Interaction partners:
Sequence:
MSKDYRSLANLSPFELKDELIKVASGKANRLMLNAGRGNPNFLATTPRRAFFRLGLFAAAESELSYSYMTVGVGGLAKLDGIEGRFERFIAEHRDQEGVKFLGKSLSYVRDQLGLDPAAFLHEMVDGILGCNYPVPPRMLTVSEQIVRQYIVREMAGGAVPPESVDLFAVEGGTAAMAYIFESLRISGLLKAGDKVAIGMPVFTPYIEIPELAQYDLKEVPIHADPDNGWQYSDAELDKLKDPDVKIFFCVNPSNPPSVKMDQRSLDRVRAIVAEQRPDLLILTDDVYGTFADEFQSLFSVCPRNTLLVYSFSKYFGATGWRLGVIAAHKDNVFDHALSQLPESAKKALDHRYRSLLPDVRSLKFIDRLVADSRVVALNHTAGLSTPQQVQMVLFSLFALMDEADAYKQALKQLIRRREATLYRELGMPPLENPNSVNYYTLIDLQNVTCRLYGEAFSQWAVQQSSTGDMLFRVADETGIVLLPGRGFGSDRPSGRASLANLNEYEYAAIGRALRRLADELYEQYKALGKE
Protein: MICOS complex subunit Mic19 (Coiled-coil-helix-coiled-coil-helix domain-containing protein 3) (Q9CRB9)
Organism: Mus musculus (Mouse)
Function: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. Has also been shown to function as a transcription factor which binds to the BAG1 promoter and represses BAG1 transcription. Plays an important role in the maintenance of the MICOS complex stability and the mitochondrial cristae morphology.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:21081504}; Lipid-anchor {ECO:0000269|PubMed:21081504}; Intermembrane side {ECO:0000269|PubMed:21081504}. Cytoplasm {ECO:0000250|UniProtKB:Q9NX63}. Nucleus {ECO:0000250|UniProtKB:Q9NX63}. Mitochondrion {ECO:0000250|UniProtKB:Q9NX63}.
Interaction partners:
- MICOS complex subunit Mic60
- MICOS complex subunit Mic10
- MICOS complex subunit Mic25
- MICOS complex subunit Mic27
- MICOS complex subunit Mic26
- MICOS complex subunit MIC13
- Coiled-coil-helix-coiled-coil-helix domain containing 10
- Sorting and assembly machinery component 50 homolog
- DnaJ homolog subfamily C member 11
- Metaxin-2
Sequence:
MGGTASTRRVTFEADENENITVVKGIRLSENVIDRMKESSPSGSKSQRYSSVYGASVSDEDLKRRVAEELALEQAKKESEHQRRLKQARDLERERAAANEQLTRAVLRERISSEEERMKAKHLARQLEEKDRVMRKQDAFYKEQLARLEERSSEFYKVTTEEYQKAAEEVEAKFKRYEYHPVCADLQTKILQCYRQNTQQTLSCSALASQYMHCVNHAKQSMLEKGG
Protein: 4-hydroxy-2-oxoglutarate aldolase, mitochondrial (EC 4.1.3.16) (Dihydrodipicolinate synthase-like) (DHDPS-like protein) (Probable 2-keto-4-hydroxyglutarate aldolase) (Probable KHG-aldolase) (Q9DCU9)
Organism: Mus musculus (Mouse)
Function: Catalyzes the final step in the metabolic pathway of hydroxyproline.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q0P5I5}.
Interaction partners:
- Glyoxylate reductase/hydroxypyruvate reductase
- Alanine--glyoxylate aminotransferase
- 2-Hydroxyacid oxidase 1
- 2-Hydroxyacid oxidase 2
- Aspartate aminotransferase, mitochondrial
- Putative aspartate aminotransferase, cytoplasmic 2
- Aspartate aminotransferase, cytoplasmic
- D-amino-acid oxidase
- Hydroxyproline dehydrogenase
Sequence:
MLGPQIWASMRQGLSRGLSRNVKGKKVDIAGIYPPVTTPFTATAEVDYGKLEENLNRLATFPFRGFVVQGSTGEFPFLTSLERLEVVSRVRQAIPKDKFLIAGSGCESTQATVEMTVSMAQVGADVAMVVTPCYYRGRMSSAALIHHYTKVADVSPIPVVLYSVPANTGLELPVDAVVTLSQHPNIIGLKDSGGDVTRIGLIVHKTSKQDFQVLAGSAGFLLASYAVGAVGGICGLANVLGAQVCQLERLCLTGQWEAAQELQHRLIEPNTAVTRRFGIPGLKKTMDWFGYYGGPCRAPLQELSPTEEEALRLDFSNNGWL
Protein: 60S ribosomal protein L27 (Q9VBN5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Small ribosomal subunit protein eS7
- Large ribosomal subunit protein eL24
- Large ribosomal subunit protein uL2
- Large ribosomal subunit protein uL22
- Ubiquitin-ribosomal protein eS31 fusion protein
- Large ribosomal subunit protein eL34
- Large ribosomal subunit protein eL15
- Large ribosomal subunit protein eL39
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein eL38
Sequence:
MRKIMKQGKIVIVLSGRYAGRKAIIVKTHDDGTPEKPFGHALVAGIDRYPRKVTKKMGKNKLKKKSKVKPFLKSLNYNHLMPTRYTAHDISFEKLSPKDLKDPVKRKTHRFQTRVKFESVYKEGKNKWFFQKLRF
Protein: Gingipain R1 (EC 3.4.22.37) (Arg-gingipain) (Gingipain 1) (RGP-1) (P28784)
Organism: Porphyromonas gingivalis (Bacteroides gingivalis)
Function: Thiol protease. Acts synergistically with RgpB to catalyze the maturation of fimbrial subunits, such as FimA (By similarity). Its proteolytic activity is a major factor in both periodontal tissue destruction and in evasion of host defense mechanisms (Probable).
Subcellular location: Secreted {ECO:0000269|PubMed:1527017, ECO:0000269|PubMed:7864651}.
Interaction partners:
Sequence:
MKNLNKFVSIALCSSLLGGMAFAQQTELGRNPNVRLLESTQQSVTKVQFRMDNLKFTEVQTPKGMAQVPTYTEGVNLSEKGMPTLPILSRSLAVSDTREMKVEVVSSKFIEKKNVLIAPSKGMIMRNEDPKKIPYVYGKSYSQNKFFPGEIATLDDPFILRDVRGQVVNFAPLQYNPVTKTLRIYTEITVAVSETSEQGKNILNKKGTFAGFEDTYKRMFMNYEPGRYTPVEEKQNGRMIVIVAKKYEGDIKDFVDWKNQRGLRTEVKVAEDIASPVTANAIQQFVKQEYEKEGNDLTYVLLVGDHKDIPAKITPGIKSDQVYGQIVGNDHYNEVFIGRFSCESKEDLKTQIDRTIHYERNITTEDKWLGQALCIASAEGGPSADNGESDIQHENVIANLLTQYGYTKIIKCYDPGVTPKNIIDAFNGGISLVNYTGHGSETAWGTSHFGTTHVKQLTNSNQLPFIFDVACVNGDFLFSMPCFAEALMRAQKDGKPTGTVAIIASTINQSWASPMRGQDEMNEILCEKHPNNIKRTFGGVTMNGMFAMVEKYKKDGEKMLDTWTVFGDPSLLVRTLVPTKMQVTAPAQINLTDASVNVSCDYNGAIATISANGKMFGSAVVENGTATINLTGLTNESTLTLTVVGYNKETVIKTINTNGEPNPYQPVSNLTATTQGQKVTLKWDAPSTKTNATTNTARSVDGIRELVLLSVSDAPELLRSGQAEIVLEAHDVWNDGSGYQILLDADHDQYGQVIPSDTHTLWPNCSVPANLFAPFEYTVPENADPSCSPTNMIMDGTASVNIPAGTYDFAIAAPQANAKIWIAGQGPTKEDDYVFEAGKKYHFLMKKMGSGDGTELTISEGGGSDYTYTVYRDGTKIKEGLTETTYRDAGMSAQSHEYCVEVKYAAGVSPKVCVDYIPDGVADVTAQKPYTLTVVGKTITVTCQGEAMIYDMNGRRLAAGRNTVVYTAQGGYYAVMVVVDGKSYVEKLAVK