wanglab/gogpt-training-data huggingface dataset:
Protein: Adducin 3 (Gamma), isoform CRA_a (cDNA FLJ77558, highly similar to Homo sapiens adducin 3 (gamma) (ADD3), transcript variant 1, mRNA) (Q5VU08)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004413}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MSSDASQGVITTPPPPSMPHKERYFDRINENDPEYIRERNMSPDLRQDFNMMEQRKRVTQILQSPAFREDLECLIQEQMKKGHNPTGLLALQQIADYIMANSFSGFSSPPLSLGMVTPINDLPGADTSSYVKGEKLTRCKLASLYRLVDLFGWAHLANTYISVRISKEQDHIIIIPRGLSFSEATASNLVKVNIIGEVVDQGSTNLKIDHTGFSPHAAIYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQESLLLGDVAYYDYQGSLEEQEERIQLQKVLGPSCKVLVLRNHGVVALGETLEEAFHYIFNVQLACEIQVQALAGAGGVDNLHVLDFQKYKAFTYTVAASGGGGVNMGSHQKWKVGEIEFEGLMRTLDNLGYRTGYAYRHPLIREKPRHKSDVEIPATVTAFSFEDDTVPLSPLKYMAQRQQREKTRWLNSPNTYMKVNVPEESRNGETSPRTKITWMKAEDSSKVSGGTPIKIEDPNQFVPLNTNPNEVLEKRNKIREQNRYDLKTAGPQSQLLAGIVVDKPPSTMQFEDDDHGPPAPPNPFSHLTEGELEEYKRTIERKQQGLEDAEQELLSDDASSVSQIQSQTQSPQNVPEKLEENHELFSKSFISMEVPVMVVNGKDDMHDVEDELAKRVSRLSTSTTIENIEITIKSPEKIEEVLSPEGSPSKSPSKKKKKFRTPSFLKKNKKKEKVEA
Protein: ELAV-like protein 1-A (36 kDa embryonic-type cytoplasmic polyadenylation element-binding protein) (36 kDa eCPE-binding protein) (36 kDa eCPEB) (p36) (Protein ElrA-A) (ElrA) (Q1JQ73)
Organism: Xenopus laevis (African clawed frog)
Function: RNA-binding protein that binds to the 3'-UTR region of mRNAs and increases their stability. Involved in embryonic stem cells (ESCs) differentiation: preferentially binds mRNAs that are not methylated by N6-methyladenosine (m6A), stabilizing them, promoting ESCs differentiation (By similarity). Binds to poly-U elements and AU-rich elements (AREs) in the 3'-UTR of target mRNAs. May be involved in cytoplasmic mRNA polyadenylation. Acts cooperatively with cribp to stabilize AU-rich sequence (ARE)-containing mRNAs. May play a role during gastrulation. Required for the vegetal localization of vg1 mRNA.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16199879, ECO:0000269|PubMed:19458392, ECO:0000269|PubMed:8873767, ECO:0000269|PubMed:9343402}. Cytoplasm, cell cortex {ECO:0000269|PubMed:16199879, ECO:0000269|PubMed:19458392, ECO:0000269|PubMed:8873767, ECO:0000269|PubMed:9343402}. Note=Enriched at the vegetal cortex in stage III and IV oocytes. Shows very weak nuclear localization. {ECO:0000269|PubMed:16199879, ECO:0000269|PubMed:19458392, ECO:0000269|PubMed:8873767, ECO:0000269|PubMed:9343402}.
Interaction partners:
Sequence:
MSNGYEDHMDDVCRDDIGRTNLIVNYLPQNMTQDELRSLFSSIGEVESAKLIRDKVAGFEMRSSSLSKGHSLGYGFVNYLNAKDAERAINTLNGLRLQSKTIKVSFARPSSESIKDANLYISGLPRTMTQKDVEDMFLPFGHIINSRVLVDQATGLSRGVAFIRFDKRSEAEEAIASFNGHKPPGSSEPITVKFAANPNQNKNVALLSQICHSPARRFGGPVHHQAQRFRFSPMGVDHMSSISSVNVASSATSGWCIFVYNLGQDADEGILWQMFGPFGAVTNVKVIRDFNTNKCKGFGFVTMTNYEEAAMAIASLNGYRLGDKTLQVSFKTSKSHK
Protein: Replication protein A subunit (Q54HE3)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- DNA helicase
- DNA 3'-5' helicase
- DNA replication ATP-dependent helicase/nuclease DNA2
- Probable serine/threonine-protein kinase atr1
- Proliferating cell nuclear antigen
- Single-stranded DNA binding protein Ssb-like OB fold domain-containing protein
- Component of 9-1-1 complex
- DNA topoisomerase 3
- Uncharacterized protein
- Uncharacterized protein
Sequence:
MSINRGCLTNIINVDQTKRFQNIDCRVQVIKTKQSSSNNLEIHLSDQDHIFVGISKTDPSNIPINSIVNLSDFSINFPKRFLNIVQFNVISQEKEIKTAQGKALTYHSVYKKTDGNSQNSNQPQPQQQQQHQQQQQPRANTTMGSNSGIASRGNPLANQRNQAGAIRSNNNFGGNSNNNNNNNYNNNNNNNNNNSGGGSNNFYADLSTQPITDIESIAPGMNVQFTIRAMVRNKQPLKSWNKGANGEGKLFSMELVDSTGEIKCACFSDSSNPNNFINALYDCFENGKVYFIQRFFVKSANKLYNTLSHQSELSINSESRVMISPDQTQFTPHYNFKKIADIENLEKNDTVDVIGAITNIDPIANLTSKQGKEFTKFGITIADDTNASINVVFWNEKATEVAPQVKVGDIIAMKGVKVSDFSGRTLSYSFGSSFGLNDEQLQETSNLRAHLQNFDVNSLQSLTIASSYTQSSYEQVNLPIFLIRTISEGSPLFISDPKTNKKLYRTIGQFQRVVPLSQAGEMDKGDEISSKMEWKYKACKKCKKSCPEGSCPQCGSDDWEYAYRMSLKLSDGDDAISVEVMGKTGDRLFGKSAAELYQMNQEQINEIFNTVLSNNYVVSLAPSSYMGSNGQTYNRFNVYDFANLYDTPNKLVSGPNPNAPNQFQNYIESSFNDCRLFNE
Protein: Thyroid hormone receptor beta (C9JJM3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTPNSMTENGLTAWDKPKHCPDREHDWKLVGMSEACLHRKSHSERRSTLKNEQSSPHLIQTTWTSSIFHLDHDDVNDQSVSSAQTFQTEEKKCKGYIPSYLDKDELCVVCGDKA
Protein: LIM domain-containing protein PLIM2b (Pollen-expressed LIM protein 2b) (OsPLIM2b) (Q7F9R9)
Organism: Oryza sativa subsp. japonica (Rice)
Interaction partners:
Sequence:
MSFTGTQDKCTACDKTVHFIDLLTADGVPYHKTCFKCSHCKGILSMCSYSSMDGVLYCKTHFEQLFKETGSFSKKFAPGCRSTDKELARAPSKICSAFSGTQDKCAACQKTVYPLEKLTLEGESYHKSCFKCSHGGCILTTSSYAALNGVLYCKIHFGQLFMEKGSYNHMKKKSESQEVLPEVVPEEQPAPPPPDENREDN
Protein: Urocortin (P81615)
Organism: Mus musculus (Mouse)
Function: Acts in vitro to stimulate the secretion of adrenocorticotropic hormone (ACTH) (By similarity). Binds with high affinity to CRF receptor types 1, 2-alpha, and 2-beta (By similarity). Plays a role in the establishment of normal hearing thresholds. Reduces food intake and regulates ghrelin levels in gastric body and plasma (By similarity).
Subcellular location: Secreted.
Interaction partners:
- Corticotropin-releasing factor receptor 1
- Corticotropin-releasing factor receptor 2
- Corticotropin-releasing factor-binding protein
- Urocortin-2
- Urocortin-3
- Corticoliberin
- Pro-opiomelanocortin
- Pituitary adenylate cyclase-activating polypeptide
Sequence:
MIQRGRATLLVALLLLAQLRPESSQWSPAAAAATGVQDPNLRWSPGVRNQGGGVRALLLLLAERFPRRAGSEPAGERQRRDDPPLSIDLTFHLLRTLLELARTQSQRERAEQNRIIFDSVGK
Protein: Uncharacterized protein (Q38D73)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRRLATACCLSCHFGRSQLTSERFIHITPLALLASQSDKPGYSNDDALGAEDPFRAVGDAMKDQQRQLEKNEGGKGALPDDIDPTASALNRRRNRRKRTVDTILGDVLHDALRLRDMGHKPTADFVYKRTQERMYEEEYGHKPPSKSENAAKYVPFPPDFGLRRLVPLEMDDPWPQRAITQENPVWTRRQVEEDRAATGGAGLREWEAKTFGPREGFDSTGELTDAMDELAYWEECFLRFIRGAPLPQRRTLPLLHEHYRYLTHRLIRAERHYIATRDVVLLKCHASPSVYKMSEDVVNRVRALYSETHRSLSSPNYDPVRMKKSVTGPLLQMSEAEFEEWKNVQKHRRNRFLSEIL
Protein: Putative acetolactate synthase small subunit (EC 2.2.1.6) (Acetohydroxy-acid synthase small subunit) (AHAS) (ALS) (P9WKJ3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the conversion of 2 pyruvate molecules into acetolactate in the first common step of the biosynthetic pathway of the branched-amino acids such as leucine, isoleucine, and valine.
Interaction partners:
- Acetolactate synthase large subunit IlvB1
- Ketol-acid reductoisomerase
- Acetolactate synthase large subunit IlvG
- Putative acetolactate synthase large subunit IlvB2
- 3-isopropylmalate dehydrogenase
- Putative acetolactate synthase large subunit IlvX
- L-threonine dehydratase biosynthetic IlvA
- 2-isopropylmalate synthase
- Dihydroxy-acid dehydratase
- Probable oxalyl-CoA decarboxylase OxcA
Sequence:
MSPKTHTLSVLVEDKPGVLARVAALFSRRGFNIESLAVGATECKDRSRMTIVVSAEDTPLEQITKQLNKLINVIKIVEQDDEHSVSRELALIKVQADAGSRSQVIEAVNLFRANVIDVSPESLTVEATGNRGKLEALLRVLEPFGIREIAQSGMVSLSRGPRGIGTAK
Protein: Ankyrin 2 (A0A5F9ZHJ4)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MTTMLQKSDSNASFLRAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILLENDTKGKVRLPALHIAARKDDTKSAALLLQNDHNADVQSKMMVNRTTESGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTALAIAKRLGYISVVDTLKVVTEEVTTTTTTITEKHKLNVPETMTEVLDVSDEEGDDTMTGDGGEYLRPEDLKELGDDSLPSSQFLDGMNYLRYSLEGGRSDSLRSFSSDRSHTLSHASYLRDSAVMDDSVVIPSHQVSTLAKEAERNSYRLSWGTENLDNVALSSSPIHSGFLVSFMVDARGGAMRGCRHNGLRIIIPPRKCTAPTRVTCRLVKRHRLATMPPMVEGEGLASRLIEVGPSGAQFLGPVIVEIPHFAALRGKERELVVLRSENGDSWKEHFCDYTEDELNEILNGMDEVLDSPEDLEKKRICRIITRDFPQYFAVVSRIKQDSNLIGPEGGVLSSTVVPQVQAVFPEGALTKRIRVGLQAQPMHSELVKKILGNKATFSPIVTLEPRRRKFHKPITMTIPVPKASSDVMLNGFGGDAPTLRLLCSITGGTTPAQWEDITGTTPLTFVNECVSFTTNVSARFWLIDCRQIQESVTFASQVYREIICVPYMAKFVVFAKSHDPIEARLRCFCMTDDKVDKTLEQQENFAEVARSRDVEVLEGKPIYVDCFGNLVPLTKSGQHHIFSFFAFKENRLPLFVKVRDTTQEPCGRLSFMKEPKSTRGLVHQAICNLNITLPIYTKESESDQEQEEEIDMTSEKNPQDEQERIEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIVHLMETNTEPLQERISHSYAEIEQTITLDHSEGFSVLQEELCTAQHKQKEEQAVSKESETCDHPPIVSEEDISVGYSTFQDGVPKTEGDSSATALFPQTHKEQVQQDFSGKMQDLPEESSLEYQQEYFVTTPGTETSETQKAMIVPSSPSKTPEEVSTPAEEEKLYLQTPTSSERGGSPIIQEPEEPSEHREESSPRKTSLVIVESADNQPETCERLDEDAAFEKGDDMPEIPPETVTEEEYIDEHGHTVVKKVTRKIIRRYVSSEGTEKEEIMVQGMPQEPVNIEEGDGYSKVIKRVVLKSDTEQSEDNNE
Protein: Zgc:154007 (A0JMM4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell projection, podosome {ECO:0000256|ARBA:ARBA00004188}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Recycling endosome {ECO:0000256|ARBA:ARBA00004172}.
Interaction partners:
Sequence:
MRGEEASGTVLHRLIQEQLRYGNPTDAHTLLAIQQQALRRGGGAASSSQSSSESLSQDEPHSPQLSTRQEPQGQEHQVDYQHSENYTTYPHHQEELPTYEQAKAHSQYLASQWCLPHRVCSLQDSVAIQKPCEEQDSWDMKQGHVRSISDRLLHFSMESGKMPCSASYPQINGYHANQHLQYNQQGLEYNKLAPYTEYPFSVEYENGYKAPPPFHSQHNRLPTPEVCHRLSTSPPAGREVNACSRSQLEMLMNENKRLRQELEGQTEKALKIQKLEQEIQRISEAYDTLMKGCAKREALEQALRNKLMAEIKRLQHSSVQAAKQAEAADQNQHAIEKLHLQNEEQKLRCACLEQEVQHLRNEAEKHQRRSEALESTLRSTQTRSQQLWTELQRKRAYVEKVERLQGALTQLQATCEKREGLEMRLRTRLEQELRSLRNQQRQPQPVGGTSHVSVYTLQENLREKEERILSLEADKIRWEQKYLEEKTMREFAMDAAATAAAQRDTTIINHSPCHSFIEELPSTEYRNQEVENRIRSLYAQILEKDTVISILKQKLQHEQKGQLGALQPATADSSIISSHSTPAHTAQGKERSHFNDQAAGTLHSSHAPVEALAHTTDQTPHTEAKPKNIQKAPSAVDLFKGVDDVSAEAVEIFI
Protein: Integrin subunit alpha 6 (A0A8I6A5C8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}.
Interaction partners:
Sequence:
MAVAGQLCLLYLSAGLLARLSTAFNLDTREDNVIRKSGDPGSLFGFSLAMHWQLQPEDKRLLLVGAPRAEALPLQKANRTGGLYSCDITSRGPCTRIVFDNDADPMSESKEDQWMGVTVQSQGPGGKVVTCAHRYEKRQHVNTKQESRDIFGRCYVLSQNLRIEDDMDGGDWSFCDGRLRGHEKFGSCQQGVAATFTKDFHYIVFGAPGTYNWKGIVRVEQKNNTFFDMNIFEDGPYEVGGETDHDESLVPVPANSYLGFSLDSGKGIVSKDDITFVSGAPRANHSGAVVLLKRDMKSAHLLLEYIFDGEGLASSFGYDVAVVDLNADGWQDIVIGAPQYFDRDGEVGGAVYVYINQQGRWSNVKPVRLNGTKDSMFGIAVKNIGDINQDGYPDIAVGAPYDDLGKVFIYHGSPTGIITKPTQVLEGTTPFFGYSIAGNMDLDRNSYPDVAVGSLSDSVTIFRSRPVINILKTITVTPSRIDLRQKSMCGSPSGICLKVKACFEYTAKPSGYNPPISILGILEAEKERRKSGLSSRVQFRNQGSEPKYTQELTLNRQKQRACMEETLWLQENIRDKLRPIPITASVEIQEPSSRRRVNSLPEVLPILNSNEAKTVQTDVHFLKEGCGDDNVCNSNLKLEYKFGTREGNQDKFSYLPIQKGIPELVLKDQKDIALEITVTNGPSDPRNPRKDGDDAHEAKLIATFPDTLTYSAYRELRAFPEKQLSCVANQNGSQADCELGNPFKRNSSVTFYLILSTTEVTFDTTDLDINLKLETTSNQDNLAPITAKAKVVIELLLSVSGVAKPSQVYFGGTVVGEQAMKSEDEVGSLIEYEFRVINLGKPLKNLGTATLNIQWPKEISNGKWLLYLMKVESKGLEQVVCEPHNEINFLKLKESHNSRKKRELPEKQIDDSRKFSLFSERKYQTLNCSVNVRCVNIRCPLRGLDSKASLVLRSRLWNSTFLEVWLYLLEEFATANGRTFVGFLTPLSSPVGIFQTELLGHPREGVHRCDRRRSEYQAPSCGHSGSSDGVSLKDGSSVFRDSVVDHPPGCACRDFDAGSISVFTVEVWFLQEK
Protein: Homeobox containing 1 (E5RGZ2)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MLSSFPVVLLETMSHYTDEPRFTIEQIDLLQRLRRTGMTKHEILHALETLDRLDQEHSDKFGRRSSYGGSSYGNSTNNVPASSSTATASTQTQHSGMSPSPSNSYDTSPQPCTTNQNGRENNERLSTSNGKMSPTRYHANSMGQRSYSFEASEEDLDVDDKVEELMRRDSSVIKEEIKAFLANRRISQAVVAQVTGISQSRISHWLLQQGSDLSEQKKRAFYRWYQLEKTNPGATLSMRPAPIPIEDPEWRQTPPPVSATSGTFRLRRGSRFTWRKECLAVMESYFNENQYPDEAKREEIANACNAVIQKPGKKLSDLERVTSLKVYNWFANRRKEIKRRANIAAILESHGIDVQSPGGHSNSDDVDGNDYSEQTDRMQAEVVAQE
Protein: Temperature-induced lipocalin-1 (AtTIL1) (Q9FGT8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in basal (BT) and acquired thermotolerance (AT), probably by preventing plasma membrane lipids peroxidation induced by severe heat-shock (HS). Lipocalin that confers protection against oxidative stress caused by heat, freezing, paraquat and light. Confers resistance to high salt (NaCl) levels, probably by protecting chloroplasts from ion toxicity via ion homeostasis maintenance. Required for seed longevity by insuring polyunsaturated lipids integrity.
Subcellular location: Cell membrane {ECO:0000269|PubMed:19302169, ECO:0000269|PubMed:23837879, ECO:0000269|PubMed:24028869, ECO:0000269|PubMed:25957952}; Peripheral membrane protein {ECO:0000269|PubMed:19302169, ECO:0000269|PubMed:24028869, ECO:0000269|PubMed:25957952}; Cytoplasmic side {ECO:0000269|PubMed:19302169, ECO:0000269|PubMed:24028869}. Cytoplasm {ECO:0000269|PubMed:24028869}. Plastid, chloroplast membrane {ECO:0000269|PubMed:24028869}; Peripheral membrane protein {ECO:0000269|PubMed:24028869}; Cytoplasmic side {ECO:0000269|PubMed:24028869}. Note=Translocates from cell membrane to cytoplasm upon salinity stress. A small fraction is associated with the chloroplast envelope. {ECO:0000269|PubMed:24028869}.
Interaction partners:
- Chloroplastic lipocalin
- DNA polymerase epsilon catalytic subunit A
- Heavy metal-associated isoprenylated plant protein 43
- Heavy metal-associated isoprenylated plant protein 33
Sequence:
MTEKKEMEVVKGLNVERYMGRWYEIASFPSRFQPKNGVDTRATYTLNPDGTIHVLNETWSNGKRGFIEGSAYKADPKSDEAKLKVKFYVPPFLPIIPVTGDYWVLYIDPDYQHALIGQPSRSYLWILSRTAQMEEETYKQLVEKAVEEGYDISKLHKTPQSDTPPESNTAPEDSKGVWWFKSLFGK
Protein: Tryptophan synthase beta chain 2, chloroplastic (EC 4.2.1.20) (P25269)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Tryptophan synthase alpha chain, chloroplastic
- Tryptophan synthase alpha chain
- Indole-3-glycerol phosphate synthase, chloroplastic
- indole-3-glycerol-phosphate synthase
- Anthranilate phosphoribosyltransferase, chloroplastic
- Threonine dehydratase biosynthetic, chloroplastic
- Anthranilate synthase beta subunit 1, chloroplastic
- N-
- N-
- Anthranilate phosphoribosyltransferase
Sequence:
MATASTAATFRPSSVSASSELTHLRSPSKLPKFTPLPSARSRSSSSFSVSCTIAKDPAVVMADSEKIKAAGSDPTMWQRPDSFGRFGKFGGKYVPETLMHALSELETAFYSLATDEDFQRELAEILKDYVGRESPLYFAERLTEHYRRENGEGPLIYLKREDLNHTGAHKINNAVAQALLAKRLGKKRIIAETGAGQHGVATATVCARFGLQCIIYMGAQDMERQALNVFRMRLLGAEVRGVHSGTATLKDATSEAIRDWVTNVETTHYILGSVAGPHPYPMMVRDFHAVIGKETRKQAMEKWGGKPDVLVACVGGGSNAMGLFHEFVDDTEVRMIGVEAAGFGLDSGKHAATLTKGDVGVLHGAMSYLLQDDDGQIIEPHSISAGLDYPGVGPEHSFLKDVGRAEYFSVTDEEALEAFKRVSRLEGIIPALETSHALAHLEKLCPTLPDGARVVLNFSGRGDKDVQTAIKYLEV
Protein: Very-long-chain aldehyde decarbonylase GL1-3 (EC 4.1.99.5) (Protein GLOSSY 1-3) (Protein GLOSSY l) (Q67WQ7)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Aldehyde decarbonylase involved in the conversion of aldehydes to alkanes. Core component of a very-long-chain alkane synthesis complex.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:F4HVY0}; Multi-pass membrane protein {ECO:0000250|UniProtKB:F4HVY0}.
Interaction partners:
- Very-long-chain aldehyde decarbonylase GL1-4
- Very-long-chain aldehyde decarbonylase GL1-5
Sequence:
MAISMASPLSSWPWAFLGSYKYLLYGPVVGKVVQEWREQGRLPLGTSWCLHLILLLALRSLTMLFFTRRRRVVDDGVDFRQIDTEWDWDNMVIMQTLIAAVLVTSRVFPATSDLSAWDLRGWAIAVVLHVAVSEPAFYWAHRALHLGPLFSRYHSLHHSFQATQALTAGFVTPLESLILTLVAWAPLAGAFMAGHGSVSLVYGHILLFDYLRSMGYSNVEVISHKTFQDFPFLRYLIYTPSYLSLHHREKDSNFCLFMPLFDALGGTLNPKSWQLQKEVDLGKNHRVPDFVFLVHVVDVVSSMHVPFAFRACSSLPFATHLVLLPLWPIAFGFMLLQWFCSKTFTVSFYKLRGFLHQTWSVPRYGFQYFIPSAKKGINEMIELAILRADKMGVKVLSLAALNKNEALNGGGTLFVRKHPDLRVRVVHGNTLTAAVILNEIPGDVAEVFLTGATSKLGRAIALYLCRKKIRVLMLTLSTERFMNIQREAPAEFQQYLVQVTKYQAAQNCKTWIVGKWLSPREQRWAPAGTHFHQFVVPPIIGFRRDCTYGKLAAMRLPEDVEGLGTCEYTMGRGVVHACHAGGVVHFLEGWDHHEVGAIDVDRIDAVWNAALRHGLTPA
Protein: Septin and tuftelin-interacting protein 1 homolog 2 (Protein SPLICEOSOMAL TIMEKEEPER LOCUS 2) (Q9SLC6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in pre-mRNA splicing, specifically in spliceosome disassembly during late-stage splicing events.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Pre-mRNA-splicing factor SYF2
- Tetratricopeptide repeat
- U2 small nuclear ribonucleoprotein A'
- Probable pre-mRNA-splicing factor ATP-dependent RNA helicase DEAH2
- Probable pre-mRNA-splicing factor ATP-dependent RNA helicase DEAH3
- RNA helicase
- Tetratricopeptide repeat
- Crooked neck protein, putative / cell cycle protein
- Crooked neck protein, putative / cell cycle protein
- Crooked neck protein, putative / cell cycle protein
Sequence:
MGDEGKKEKRRQTKEDAVYGFVFESDSNSDDSGGSRRKKRRKTKPVKFSSAGNIDQVLKQNRGNCKIDENDDTILPIALGKKIADKAHVREKNNKKENFEKFSGGIGMKLLEKMGYKGRGLGKNQQGIVAPIEVQLRPKNMGMGYNDFKEKNAPLFPCLNKVEEKKKSVVVTVSENHGDGRRDLWKKKNVRKEVYITAEEFLGKKQEEGFGCDQLIIDKRGPQDRVVNSLRNLYAEEKATDANVQQPELQHNLRFIVKSLEHGILKTDKDLRNEKGLALSLQQEKEKFKMGVKKQKTLFDNLGYVAEEIDRIEVEIASGNLTLDSLANRFKDLRSSYPDDYKCCNLSCIASSLALPLFIRMFQGWDPLSDAEHGIEAISSWKMLLEVEDNQSISTPYSQLVSEVILPAVRVSGINTWEPRDPEPMLRLLETWEKMLPSLIFETILTTVVLPKLSIAIESWEPRLETVPIHFWVHPWLPVLGQKLESAYQIIRMKFGNLLDAWHPSDVSVHTILSPWKTVFDAASWEQLMRRYIVPKLQVALQEFQINPADQNLDEFNLVMGWVSSVPIHLMTDLMERFFFPKWLDVLYHWLCSEPKFDEIMKWFLGWKGTFPQELSANRRIEIQFKRGLDMAREAVERMEMSQPGARENISYHKAQEQRQSEGRAKVQAQVDDPEELSFKEAVELFAQEKELLLKPKPHRMHNGLQIYRFGNVSVLLDSANSKLLAQEEGRWFPVDLDSLLKMHYSAVTGKQ
Protein: Sulfotransferase 1C4 (ST1C4) (EC 2.8.2.1) (Sulfotransferase 1C2) (SULT1C#2) (O75897)
Organism: Homo sapiens (Human)
Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of phenolic compounds. Can also sulfonate estrogenic compounds, however, the dietary flavonoids (phytoestrogen) and environmental estrogens, like bisphenol A are better substrates than 17beta-estradiol (E2). Mediates the sulfation of doxorubicin and its analog epirubicin, two antitumor anthracyclines.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:28222028}.
Interaction partners:
- Carbohydrate sulfotransferase 6
- Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 1
- Heparan sulfate glucosamine 3-O-sulfotransferase 1
- Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 2
- Heparan sulfate glucosamine 3-O-sulfotransferase 3A1
- Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1
- Heparan sulfate glucosamine 3-O-sulfotransferase 3B1
- Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 2
- Carbohydrate sulfotransferase 3
- Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 3
Sequence:
MALHDMEDFTFDGTKRLSVNYVKGILQPTDTCDIWDKIWNFQAKPDDLLISTYPKAGTTWTQEIVELIQNEGDVEKSKRAPTHQRFPFLEMKIPSLGSGLEQAHAMPSPRILKTHLPFHLLPPSLLEKNCKIIYVARNPKDNMVSYYHFQRMNKALPAPGTWEEYFETFLAGKVCWGSWHEHVKGWWEAKDKHRILYLFYEDMKKNPKHEIQKLAEFIGKKLDDKVLDKIVHYTSFDVMKQNPMANYSSIPAEIMDHSISPFMRKGAVGDWKKHFTVAQNERFDEDYKKKMTDTRLTFHFQF
Protein: Beta-microseminoprotein (P83242)
Organism: Struthio camelus (Common ostrich)
Subcellular location: Secreted.
Interaction partners:
Sequence:
YCFQKINRPGESDEGCILDGKLYPFGEISRTENCYRCSCSRDAMRCCTLFHTPVGYNKEKCKVVFNKESCNYDVVQKDDPSKECFVYSRV
Protein: Insulin-induced gene 2 protein (INSIG-2) (Q91WG1)
Organism: Mus musculus (Mouse)
Function: Oxysterol-binding protein that mediates feedback control of cholesterol synthesis by controlling both endoplasmic reticulum to Golgi transport of SCAP and degradation of HMGCR. Acts as a negative regulator of cholesterol biosynthesis by mediating the retention of the SCAP-SREBP complex in the endoplasmic reticulum, thereby blocking the processing of sterol regulatory element-binding proteins (SREBPs) SREBF1/SREBP1 and SREBF2/SREBP2. Binds oxysterol, including 22-hydroxycholesterol, 24-hydroxycholesterol, 25-hydroxycholesterol and 27-hydroxycholesterol, regulating interaction with SCAP and retention of the SCAP-SREBP complex in the endoplasmic reticulum (By similarity). In presence of oxysterol, interacts with SCAP, retaining the SCAP-SREBP complex in the endoplasmic reticulum, thereby preventing SCAP from escorting SREBF1/SREBP1 and SREBF2/SREBP2 to the Golgi (By similarity). Sterol deprivation or phosphorylation by PCK1 reduce oxysterol-binding, disrupting the interaction between INSIG2 and SCAP, thereby promoting Golgi transport of the SCAP-SREBP complex, followed by processing and nuclear translocation of SREBF1/SREBP1 and SREBF2/SREBP2 (By similarity). Also regulates cholesterol synthesis by regulating degradation of HMGCR: initiates the sterol-mediated ubiquitin-mediated endoplasmic reticulum-associated degradation (ERAD) of HMGCR via recruitment of the reductase to the ubiquitin ligase RNF139 (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9Y5U4}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9Y5U4}.
Interaction partners:
- Sterol regulatory element-binding protein cleavage-activating protein
- 3-hydroxy-3-methylglutaryl-coenzyme A reductase
- Sterol regulatory element-binding protein 2
- E3 ubiquitin-protein ligase AMFR
- Insulin-induced gene 1 protein
- Sterol regulatory element-binding protein 1
- Chromatin assembly factor 1 subunit B
- NPC1-like intracellular cholesterol transporter 1
Sequence:
MAEGETESPRPKKCGPYISSVTSQSVNVVIRGVVLFFIGVFLALVLNLLQIQRNVTLFPPDVITSIFSSAWWVPPCCGTASAVIGLLYPCIDRHLGEPHKFKREWSSVMRCVAVFVGINHASAKVDFDNNFQFSLTLAALSVGLWWTFDRSRSGFGLGVGIAFLATVVTQLLVYNGVYQYTSPDFLYVRSWLPCIFFAGGITMGNIGRQLAMYECKVIAEKSHQE
Protein: Transmembrane protein (Q383X2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MDGLYFTAKAQFHQLATHISLYHEDASPTYRTLGEACLQLAGLRPDRFTFWNVPNMSGYFNKALPLDIHGGYVLVDEAAVKAAAGTYGVLRYAYLAAAVRARAGGRWRYDFTTMNAALCVGVASGFAVLSVGRRRWPLMRRRPVGAIAVGVATCFVAVVATRLLLRAMGAGITHARNSNRRALEKLRCVDCYDDVARYTEQRKEEVEAQRVPQPQPGMPPLPEVSLRQFERLSALQVQLLESNLCEIRLAKRRANSQLCDVHRGLRDDEQYAVSAGLPIQSADVALARERARQLPSGG
Protein: Large ribosomal subunit protein bL34m (54S ribosomal protein L34, mitochondrial) (L34mt) (Q04598)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095}. Note=Mitoribosomes are tethered to the mitochondrial inner membrane and spatially aligned with the membrane insertion machinery through two distinct membrane contact sites, formed by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein MBA1. {ECO:0000269|PubMed:25609543}.
Interaction partners:
- Large ribosomal subunit protein bL19m
- Large ribosomal subunit protein uL30m
- Large ribosomal subunit protein uL3m
- Large ribosomal subunit protein mL41
- Large ribosomal subunit protein uL16m
- Large ribosomal subunit protein bL33m
- Large ribosomal subunit protein mL49
- Large ribosomal subunit protein uL13m
- Large ribosomal subunit protein bL36m
- Small ribosomal subunit protein uS15m
Sequence:
MPLFARLCQPQSRRMFSSISSFSALSVLRPQTGMLLNSSPLKTPSFTPLGFGLIGQRRWKSRGNTYQPSTLKRKRTFGFLARAKSKQGSKILKRRKLKGRWFLSH