wanglab/gogpt-training-data huggingface dataset:
Protein: Retinoic acid receptor alpha-A (RAR-alpha-A) (Nuclear receptor subfamily 1 group B member 1-A) (Retinoic acid receptor alpha) (zRAR alpha) (Retinoic acid receptor alpha-2.A) (RAR-alpha-2.A) (Q90271)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The rar/rxr heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5 (By similarity). Required for hindbrain patterning.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
Interaction partners:
- Retinoic acid receptor RXR-alpha-A
- Retinoic acid receptor RXR-beta-A
- Arginyl-tRNA synthetase
- Cellular retinoic acid binding protein type II
- Nuclear receptor corepressor 2
- Retinoic acid receptor RXR-alpha-B
- Cytochrome P450 26A1
Sequence:
MYESVDVNPFLMMDYYNQSRGCLIPDKMPHPFSSSIRHQHWSGSNHSIETQSTSSEEIVPSPPSPPPPPRIYKPCFVCQDKSSGYHYGVSACEGCKGFFRRSIQKNMVYTCHREKNCIINKVTRNRCQYCRLQKCLEVGMSKESVRNDRNKKKKEEKKPECTENYTLSPDTEQMIDRVRKAHQETFPSLCQLGKYTTSNSSERRVALDVDLWDKFSELSTKCIIKTVEFAKQLPGFTTLTIADQITLLKAACLDILILRICTRYTPEQDTMTFSDGLTLNRTQMHNAGFGPLTDLVFAFANQLLPLEMDDAETGLLSAICLLCGDRQDLEQADKVDVLQEPLLEALKIYVRNRRPHKPHMFPKMLMKITDLRSISAKGAERVITLKMEIPGSMPPLIQEMLENSEGLESSSGAQGSRASATTPGSCSPSLSPNSAQSSPPTQSP
Protein: Uncharacterized protein, isoform D (A1Z7L6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Little elongation complex subunit 2
- Little elongation complex subunit 1
- RNA polymerase II elongation factor Ell
- Ell-associated factor Eaf
- Cyclin-T
- ENL/AF9-related, isoform B
- Cyclin-dependent kinase 9
- Transcription elongation factor SPT5
- Elongin-C
- Transcription elongation factor SPT4
Sequence:
MQRLQPGDECLECQSEGRNHKLRYFYINLEEQLLKCESRSCLWPHNDEVSSDEDLNSEAALPITAPQSELFESPAATLPSHPAALTSKPPPNDDEFILELLQQLTSATETPLKTNVSSSSMPNLHSPSEEKPCPQLELPDLSFLEENSTVCKEPPQALKSELGVPSTVVLPDRLISPPKAKAVQTEDTKAKEHVAHLKGATSQSWQGKAEIPLLPACVKASVRMSPSIKSKGSPFSSPPKKATTQPQGQSPPSTPPAVNIIISVPELNTGMNGLFLDAIKRHSTEAKPALRGVGRRPKRLAKGTTSRGGIRTQDVMHLIEHLETTTEAKLTTPRT
Protein: Outer capsid protein lambda-2 (Lambda2) (Lambda2(Cap)) [Includes: mRNA guanylyltransferase (EC 2.7.7.50); mRNA (guanine-N(7))-methyltransferase (EC 2.1.1.56)] (P11079)
Organism: Reovirus type 3 (strain Dearing) (T3D) (Mammalian orthoreovirus 3)
Function: Outer capsid protein involved in mRNA capping. Catalyzes the last 3 enzymatic activities for formation of the 5' cap structure on the viral plus-strand transcripts, namely the RNA guanylyltransferase, RNA-7N- and RNA-2'O-methyltransferase activities.
Subcellular location: Virion {ECO:0000305}.
Interaction partners:
Sequence:
MANVWGVRLADSLSSPTIETRTRQYTLHDLCSDLDANPGREPWKPLRNQRTNNIVAVQLFRPLQGLVLDTQLYGFPGAFDDWERFMREKLRVLKYEVLRIYPISNYSNEHVNVFVANALVGAFLSNQAFYDLLPLLIINDTMIGDLLGTGASLSQFFQSHGDVLEVAAGRKYLQMENYSNDDDDPPLFAKDLSDYAKAFYSDTYEVLDRFFWTHDSSAGVLVHYDKPTNGHHYLLGTLTQMVSAPPYIINATDAMLLESCLEQFSANVRARPAQPVTRLDQCYHLRWGAQYVGEDSLTYRLGVLSLLATNGYQLARPIPRQLTNRWLSSFVSQIMSDGVNETPLWPQERYVQIAYDSPSVVDGATQYGYVRKNQLRLGMRISALQSLSDTPSPVQWLPQYTIDQAAMDEGDLMVSRLTQLPLRPDYGNIWVGDALSYYVDYNRSHRVVLSSELPQLPDTYFDGDEQYGRSLFSLARKIGDRSLVKDTAVLKHAYQAIDPNTGKEYLRSRQSVAYFGASAGHSGADQPLVIEPWIQGKISGVPPPSSVRQFGYDVARGAIVDLARPFPSGDYQFVYSDVDQVVDGHDDLSISSGLVESLLSSCMHATAPGGSFVVKINFPTRPVWHYIEQKILPNITSYMLIKPFVTNNVELFFVAFGVHQHSSLTWTSGVYFFLVDHFYRYETLSTISRQLPSFGYVDDGSSVTGIETISIENPGFSNMTQAARIGISGLCANVGNARKSIAIYESHGARVLTITSRRSPASARRKSRLRYLPLIDPRSLEVQARTILPADPVLFENVSGASPHVCLTMMYNFEVSSAVYDGDVVLDLGTGPEAKILELIPATSPVTCVDIRPTAQPSGCWNVRTTFLELDYLSDGWITGVRGDIVTCMLSLGAAAAGKSMTFDAAFQQLIKVLSKSTANVVLVQVNCPTDVVRSIKGYLEIDSTNKRYRFPKFGRDEPYSDMDALEKICRTAWPNCSITWVPLSYDLRWTRLALLESTTLSSASIRIAELMYKYMPIMRIDIHGLPMEKRGNFIVGQNCSLVIPGFNAQDVFNCYFNSALAFSTEDVNAAMIPQVSAQFDATKGEWTLDMVFSDAGIYTMQALVGSNANPVSLGSFVVDSPDVDITDAWPAQLDFTIAGTDVDITVNPYYRLMTFVRIDGQWQIANPDKFQFFSSASGTLVMNVKLDIADKYLLYYIRDVQSRDVGFYIQHPLQLLNTITLPTNEDLFLSAPDMREWAVKESGNTICILNSQGFVLPQDWDVLTDTISWSPSIPTYIVPPGDYTLTPL
Protein: 4-aminobutyrate aminotransferase (EC 2.6.1.19) ((S)-3-amino-2-methylpropionate transaminase) (EC 2.6.1.22) (GABA aminotransferase) (GABA-AT) (Gamma-amino-N-butyrate transaminase) (GABA transaminase) (Glutamate:succinic semialdehyde transaminase) (L-AIBAT) (P9WQ79)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Sec translocon accessory complex subunit YajC
- Glutamate decarboxylase
- methylmalonate-semialdehyde dehydrogenase
- Probable aldehyde dehydrogenase
- aldehyde dehydrogenase
- Aldehyde dehydrogenase
- Putative succinate-semialdehyde dehydrogenase [NADP
- Succinate-semialdehyde dehydrogenase [NADP
- Probable aldehyde dehydrogenase NAD dependent AldA
- Probable fatty oxidation protein FadB
Sequence:
MASLQQSRRLVTEIPGPASQALTHRRAAAVSSGVGVTLPVFVARAGGGIVEDVDGNRLIDLGSGIAVTTIGNSSPRVVDAVRTQVAEFTHTCFMVTPYEGYVAVAEQLNRITPGSGPKRSVLFNSGAEAVENAVKIARSYTGKPAVVAFDHAYHGRTNLTMALTAKSMPYKSGFGPFAPEIYRAPLSYPYRDGLLDKQLATNGELAAARAIGVIDKQVGANNLAALVIEPIQGEGGFIVPAEGFLPALLDWCRKNHVVFIADEVQTGFARTGAMFACEHEGPDGLEPDLICTAKGIADGLPLSAVTGRAEIMNAPHVGGLGGTFGGNPVACAAALATIATIESDGLIERARQIERLVTDRLTTLQAVDDRIGDVRGRGAMIAVELVKSGTTEPDAGLTERLATAAHAAGVIILTCGMFGNIIRLLPPLTIGDELLSEGLDIVCAILADL
Protein: VGF protein (Q05BJ3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKALRLSASALFCLLLINGLGAAPPGRPEAQPPPLSSEHKEPVAGDAVPGPKDGSAPEVRGARNSEPQDEGELFQGVDPRALAAVLLQALDRPASPPAPSGSQQGPEEEAAEALLTETVRSQTHSLPAPESPEPAAPPRPQTPENGPEASDPSEELEALASLLQELRDFSPSSAKRQQETAAAETETRTHTLTRVNLESPGPERVWRASWGEFQARVPERAPLPPPAPSQFQARMPDSGPLPETHKFGEGVSSPKTHLGEALAPLSKAYQGVAAPFPKARRPESALLGGSEAGERLLQQGLAQVEAGRRQAEATRQAAAQEERLADLASDLLLQFAAGRGPAARPCPLALPLSPGCVGTCQTPLPGPEPELPELTRG
Protein: Mitochondrial import receptor subunit TOM70 (70 kDa mitochondrial outer membrane protein) (Translocase of outer membrane 70 kDa subunit) (P07213)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the TOM (translocase of outer membrane) receptor complex responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. Together with TOM20 and TOM22 functions as the transit peptide receptor at the surface of the mitochondrion outer membrane and facilitates the movement of preproteins into the TOM40 translocation pore.
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:11502169}; Single-pass membrane protein {ECO:0000269|PubMed:11502169}.
Interaction partners:
- Mitochondrial import receptor subunit TOM7
- Mitochondrial import receptor subunit TOM22
- Mitochondrial import receptor subunit TOM20
- Mitochondrial import receptor subunit TOM40
- Sorting assembly machinery 37 kDa subunit
- Sorting assembly machinery 50 kDa subunit
- Mitochondrial import receptor subunit TOM5
- Mitochondrial import receptor subunit TOM6
- Sorting assembly machinery 35 kDa subunit
- Mitochondrial distribution and morphology protein 10
Sequence:
MKSFITRNKTAILATVAATGTAIGAYYYYNQLQQQQQRGKKNTINKDEKKDTKDSQKETEGAKKSTAPSNPPIYPVSSNGEPDFSNKANFTAEEKDKYALALKDKGNQFFRNKKYDDAIKYYNWALELKEDPVFYSNLSACYVSVGDLKKVVEMSTKALELKPDYSKVLLRRASANEGLGKFADAMFDLSVLSLNGDFNDASIEPMLERNLNKQAMSKLKEKFGDIDTATATPTELSTQPAKERKDKQENLPSVTSMASFFGIFKPELTFANYDESNEADKELMNGLSNLYKRSPESYDKADESFTKAARLFEEQLDKNNEDEKLKEKLAISLEHTGIFKFLKNDPLGAHEDIKKAIELFPRVNSYIYMALIMADRNDSTEYYNYFDKALKLDSNNSSVYYHRGQMNFILQNYDQAGKDFDKAKELDPENIFPYIQLACLAYRENKFDDCETLFSEAKRKFPEAPEVPNFFAEILTDKNDFDKALKQYDLAIELENKLDGIYVGIAPLVGKATLLTRNPTVENFIEATNLLEKASKLDPRSEQAKIGLAQMKLQQEDIDEAITLFEESADLARTMEEKLQAITFAEAAKVQQRIRSDPVLAKKIQETLAKLREQGLM
Protein: Eukaryotic translation elongation factor 1 delta (E9PN56)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRSGKASCTLETVWEDKHKYEEAERRFYEHEATQAAASAQQLPAEGPAMNGPGQDDPEDADEAEAPDGGSRRDPRKSQDSRKPLQKKRKRSPKSGLGPADLALLGLSAERVWLDKSLFDQAESSYRQKLADVAAQAAWPPALAPWGLCTHGNQVACHHVTWGIWVNKSSFDQAERAFVEW
Protein: Actin-related protein 2/3 complex subunit 3-A (A1DPK7)
Organism: Xenopus laevis (African clawed frog)
Function: Component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility. In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA (Probable). The Arp2/3 complex promotes homologous recombination (HR) repair in response to DNA damage by promoting nuclear actin polymerization, leading to drive motility of double-strand breaks (DSBs) (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17178911}. Cell projection {ECO:0000269|PubMed:17178911}. Nucleus {ECO:0000269|PubMed:29925947}.
Interaction partners:
- Actin-related protein 2/3 complex subunit 4
- Actin-related protein 3-A
- Actin-related protein 2/3 complex subunit 2-B
- Actin-related protein 3-B
- Actin-related protein 2/3 complex subunit 2-A
- Actin-related protein 2/3 complex subunit 5-B
- Actin-related protein 2/3 complex subunit 1A-A
- Actin-related protein 2/3 complex subunit 5-C
- Actin-related protein 2
- Actin-related protein 2
Sequence:
MPAYHSMLMEPDTKLIGNMAMLPIRSQFKGPAPRETKDTDIIDEAIYYFKANVFFKNYEIKNEADRTLIYITLYISECLKKLQKCNSKGQGEKEMYTLGITNFPIPGEPGFPLNAMYVKPSNKQEDEVMRAYLQQLRQETGLRLCDKVFDPQTDKPSKWWTCFVKRQFMNKSLSAPGQ
Protein: Rab GTPase SrgA, putative (Q4W9I4)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004342}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004342}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004342}.
Interaction partners:
- Rab guanine nucleotide exchange factor sec2
- Rab GDP dissociation inhibitor
- Exocyst complex protein exo70
- Exocyst complex component exo84
- Exocyst complex component SEC15
- GTP-binding protein ypt1
- GDP/GTP exchange factor Sec2 N-terminal domain-containing protein
- Exocyst complex component Sec8
- Rab proteins geranylgeranyltransferase
- Vacuolar fusion protein mon1
Sequence:
MAGTRNYDFLIKLLLIGDSGVGKSCCLLRFSEDSFTPSFITTIGIDFKIRTIELDGKRVKLQIWDTAGQERFRTITTAYYRGAMGILLVYDVTDERSFQNIRTWFSNVEQHASEGVHKILIGNKCDWEEKRAVSTEQGQQLADELGIPFLEVSAKNNINIEKAFYSLASAIKKGMDTSKSEQVGSQGVNIDHHGSGTSGSTGGKCC
Protein: ShlB/FhaC/HecB family hemolysin secretion/activation protein (Q9I5N4)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Transport protein ExbB2
- Filamentous haemagglutinin FhaB/tRNA nuclease CdiA-like TPS domain-containing protein
- Energy transducer TonB
- Porin
- DNA repair protein
- Probable peptidyl-prolyl cis-trans isomerase, PpiC-type
- YbjN domain-containing protein
- Transport protein ExbD
- Transposase InsH N-terminal domain-containing protein
- VreA
Sequence:
MKRSLFNCAHPFRQRWSIGCLAVALSCASLADEAPPAAAGAEPQRLVDINEYVVRGNTVLDNRAIEAAVYPFLGPQRSLGDIEGARDALQAAYQEKGYQSVYVELPEQQVSGGVVYLQVTETTIGRVRVVGAKHYSPVELREEVPALEEGKVPDFAQVQRELAQVNRTPGRQVLPMVREGQRPGTMDVDLQVEDKNPWHASIGLNNDYSADTRHLRSVVSLGYDNLWQLGHAISLTYFTAPQDQDNAKVWSGSYTAPLSQRWSVQLSGYQSDSDVATVGSMNVVGQGHSYGVAAIYSLPVTGLWSHSFSFGVDFKDFEEQTRIGGNNDRVPIKYAPLTLGYNGFRYTERSQLALGLSLVAGTGSLLGYGDDDEEFDRKRYRAKSGFGVLKGDLNHTLTFGGDWQVATKAAFQLASGPLISNEQFAAGGATSVRGYLAAENTADDGYLLSQEWRTPSLGRFLGKRAGGYVNDWRFYVFAEGAQLRLQDALPEQDDDFSLASVGIGTRAQLADWLSGSLDWAFPLLEGTNTDKHDSRLHFSVQASF
Protein: E3 ubiquitin-protein ligase CCNB1IP1 (EC 2.3.2.27) (Cyclin-B1-interacting protein 1) (Human enhancer of invasion 10) (RING-type E3 ubiquitin transferase CCNB1IP1) (Q9NPC3)
Organism: Homo sapiens (Human)
Function: Ubiquitin E3 ligase that acts as a limiting factor for crossing-over during meiosis: required during zygonema to limit the colocalization of RNF212 with MutS-gamma-associated recombination sites and thereby establish early differentiation of crossover and non-crossover sites. Later, it is directed by MutL-gamma to stably accumulate at designated crossover sites. Probably promotes the dissociation of RNF212 and MutS-gamma to allow the progression of recombination and the implementation of the final steps of crossing over (By similarity). Modulates cyclin-B levels and participates in the regulation of cell cycle progression through the G2 phase. Overexpression causes delayed entry into mitosis.
Subcellular location: Nucleus. Chromosome. Note=Associates to the synaptonemal complex.
Interaction partners:
- Probable E3 SUMO-protein ligase RNF212
- Cytochrome c oxidase subunit 6C
- G2/mitotic-specific cyclin-B1
- High mobility group AT-hook 2
- MutS protein homolog 4
- Dermatopontin
- EPM2A-interacting protein 1
- DNA repair protein RAD51 homolog 2
Sequence:
MSLCEDMLLCNYRKCRIKLSGYAWVTACSHIFCDQHGSGEFSRSPAICPACNSTLSGKLDIVRTELSPSEEYKAMVLAGLRPEIVLDISSRALAFWTYQVHQERLYQEYNFSKAEGHLKQMEKIYTQQIQSKDVELTSMKGEVTSMKKVLEEYKKKFSDISEKLMERNRQYQKLQGLYDSLRLRNITIANHEGTLEPSMIAQSGVLGFPLGNNSKFPLDNTPVRNRGDGDGDFQFRPFFAGSPTAPEPSNSFFSFVSPSRELEQQQVSSRAFKVKRI
Protein: Protein disulfide-isomerase A6 homolog (EC 5.3.4.1) (Q11067)
Organism: Caenorhabditis elegans
Function: May function as a chaperone that inhibits aggregation of misfolded proteins (By similarity). May negatively regulate the unfolded protein response (UPR) through binding to UPR sensors.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:Q15084}.
Interaction partners:
- Endoplasmin homolog
- Endoplasmic reticulum oxidoreductin-1
- J domain-containing protein
- Protein disulfide-isomerase 2
- Heat shock 70 kDa protein C
- Calreticulin
- Endoplasmic reticulum chaperone BiP homolog
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
- DnaJ homolog dnj-20
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
Sequence:
MALIKLLLASLAITSVCGMYSKKDDVVELTEANFQSKVINSDDIWIVEFYAPWCGHCKSLVPEYKKAASALKGVAKVGAVDMTQHQSVGGPYNVQGFPTLKIFGADKKKPTDYNGQRTAQAIADSVLAEAKKAVSARLGGKSSGSSSSGSGSGSGKRGGGGSGNEVVELTDANFEDLVLNSKDIWLVEFFAPWCGHCKSLEPQWKAAASELKGKVRLGALDATVHTVVANKFAIRGFPTIKYFAPGSDVSDAQDYDGGRQSSDIVAWASARAQENMPAPEVFEGINQQVVEDACKEKQLCIFAFLPHILDCQSECRNNYLAMLKEQSEKFKKNLWGWIWVEGAAQPALEESFEVGGFGYPAMTALNFRKNKYAVLKGSFGKDGIHEFLRDLSYGKGRTSSLRGDGFPKIQKTEKWDGKDGALPAEDDIDLSDIDLDKTEL
Protein: Protein sel-1 homolog 1 (Suppressor of lin-12-like protein 1) (Sel-1L) (Q9Z2G6)
Organism: Mus musculus (Mouse)
Function: Plays a role in the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. Enhances SYVN1 stability. Plays a role in LPL maturation and secretion. Required for normal differentiation of the pancreas epithelium, and for normal exocrine function and survival of pancreatic cells. May play a role in Notch signaling.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9UBV2}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9UBV2}.
Interaction partners:
- E3 ubiquitin-protein ligase synoviolin
- Protein OS-9
- Derlin-1
- Derlin-2
- Transitional endoplasmic reticulum ATPase
- E3 ubiquitin-protein ligase AMFR
- Derlin-3
- Family with sequence similarity 8, member A1
- Endoplasmic reticulum lectin 1
- Lipid droplet-regulating VLDL assembly factor AUP1
Sequence:
MQVRVRLSLLLLCAVLLGSAAATSDDKTNQDDSLDSKSSLPTDESVKDHTTTGKVVAGQIFVDSEEAEVESLLQDEEDSSKTQEEEISFLESPNPSSKTYEELKRVRKPVLTAIEGTAHGEPCHFPFLFLDKEYDECTSDGREDGRLWCATTYDYKTDEKWGFCETEEDAAKRRQMQEAEMIYQAGMKILNGSNRKSQKREAYRYLQKAAGMNHTKALERVSYALLFGDYLTQNIQAAKEMFEKLTEEGSPKGQTGLGFLYASGLGVNSSQAKALVYYTFGALGGNLIAHMILGYRYWAGIGVLQSCESALTHYRLVANHVASDISLTGGSVVQRIRLPDEVENPGMNSGMLEEDLIQYYQFLAEKGDVQAQVGLGQLHLHGGRGVEQNHQRAFDYFNLAANAGNSHAMAFLGKMYSEGSDIVPQSNETALHYFKKAADMGNPVGQSGLGMAYLYGRGVQVNYDLALKYFQKAAEQGWVDGQLQLGSMYYNGIGVKRDYKQALKYFNLASQGGHILAFYNLAQMHASGTGVMRSCHTAVELFKNVCERGRWSERLMTAYNSYKDEDYNAAVVQYLLLAEQGYEVAQSNAAFILDQREATIVGENETYPRALLHWNRAASQGYTVARIKLGDYHFYGFGTDVDYETAFIHYRLASEQQHSAQAMFNLGYMHEKGLGIKQDIHLAKRFYDMAAEASPDAQVPVFLALCKLGVVYFLQYIREANIRDLFTQLDMDQLLGPEWDLYLMTIIALLLGTVIAYRQRQHQDIPVPRPPGPRPAPPQQEGPPEQQPPQ
Protein: ER-bound oxygenase mpaB/mpaB'/Rubber oxygenase catalytic domain-containing protein (O53682)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Possible transcriptional regulatory protein
- Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 2
- Putative aminoglycoside phosphotransferase
- Transcriptional regulatory protein
Sequence:
MAISLVAHQPIPHVERPMADPPRLQLARRRRSAAGPGGNEDSLMGVALLAGPANVIMELAMPGVGYGVLESRVESGRLDRHPIKRARTTFTYVAVAVAGSDDQKAAFRRAVNKVHAQVYSTPESPVSYHAFDPELQLWVAACLYKGGVDVYRTFVGEMDDEEADHHYRAGMAMGTTLQVPPQMWPPDRAAFDRYWRQSLDRVHIDDVVRDYLYPIVALRIRGIALPGPLRRLSEGIALLITTGFLPQRFRDEMRLPWDATKQRRFDALMAVLRTVNRLMPRFVREFPFNLMLWDLDRRMRRGRPLV
Protein: PR domain zinc finger protein 5 (EC 2.1.1.-) (PR domain-containing protein 5) (Q9NQX1)
Organism: Homo sapiens (Human)
Function: Sequence-specific DNA-binding transcription factor. Represses transcription at least in part by recruitment of the histone methyltransferase EHMT2/G9A and histone deacetylases such as HDAC1. Regulates hematopoiesis-associated protein-coding and microRNA (miRNA) genes. May regulate the expression of proteins involved in extracellular matrix development and maintenance, including fibrillar collagens, such as COL4A1 and COL11A1, connective tissue components, such as HAPLN1, and molecules regulating cell migration and adhesion, including EDIL3 and TGFB2. May cause G2/M arrest and apoptosis in cancer cells.
Subcellular location: Nucleus {ECO:0000269|PubMed:15077163, ECO:0000269|PubMed:17636019}.
Interaction partners:
Sequence:
MLGMYVPDRFSLKSSRVQDGMGLYTARRVRKGEKFGPFAGEKRMPEDLDENMDYRLMWEVRGSKGEVLYILDATNPRHSNWLRFVHEAPSQEQKNLAAIQEGENIFYLAVEDIETDTELLIGYLDSDMEAEEEEQQIMTVIKEGEVENSRRQSTAGRKDRLGCKEDYACPQCESSFTSEDILAEHLQTLHQKPTEEKEFKCKNCGKKFPVKQALQRHVLQCTAKSSLKESSRSFQCSVCNSSFSSASSFEQHQETCRGDARFVCKADSCGKRLKSKDALKRHQENVHTGDPKKKLICSVCNKKCSSASSLQEHRKIHEIFDCQECMKKFISANQLKRHMITHSEKRPYNCEICNKSFKRLDQVGAHKVIHSEDKPYKCKLCGKGFAHRNVYKNHKKTHSEERPFQCEECKALFRTPFSLQRHLLIHNSERTFKCHHCDATFKRKDTLNVHVQVVHERHKKYRCELCNKAFVTPSVLRSHKKTHTGEKEKICPYCGQKFASSGTLRVHIRSHTGERPYQCPYCEKGFSKNDGLKMHIRTHTREKPYKCSECSKAFSQKRGLDEHKRTHTGEKPFQCDVCDLAFSLKKMLIRHKMTHNPNRPLAECQFCHKKFTRNDYLKVHMDNIHGVADS
Protein: Probable methyltransferase PMT5 (EC 2.1.1.-) (Q3EC77)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- DUF241 domain protein, putative
- Cation/H
- AT4G23670 protein
- Uncharacterized protein AT4g35200
- Defensin-like protein 99
- Probable E3 ubiquitin-protein ligase EDA40
- Zinc finger A20 and AN1 domain-containing stress-associated protein 4
- Receptor-like protein 9b
- Receptor-like protein 9a
- Pollen Ole e 1 allergen and extensin family protein
Sequence:
MRGSWYKSVSSVFGLRPRIRGLLFFIVGVVALVTILAPLTSNSYDSSSSSTLVPNIYSNYRRIKEQAAVDYLDLRSLSLGASLKEFPFCGKERESYVPCYNITGNLLAGLQEGEELDRHCEFEREKERCVVRPPRDYKIPLRWPLGRDIIWSGNVKITKDQFLSSGTVTTRLMLLEENQITFHSEDGLVFDGVKDYARQIAEMIGLGSDTEFAQAGVRTVLDIGCGFGSFGAHLVSLKLMPICIAEYEATGSQVQLALERGLPAMIGNFFSKQLPYPALSFDMVHCAQCGTTWDIKDAMLLLEVDRVLKPGGYFVLTSPTNKAQGNLPDTKKTSISTRVNELSKKICWSLTAQQDETFLWQKTSDSSCYSSRSQASIPLCKDGDSVPYYHPLVPCISGTTSKRWISIQNRSAVAGTTSAGLEIHGKSALKNYWSLLTPLIFSDHPKRPGDEDPLPPFNMIRNVMDMHARFGNLNAALLDEGKSAWVMNVVPVNARNTLPIILDRGFAGVLHDWCEPFPTYPRTYDMLHANELLTHLSSERCSLMDLFLEMDRILRPEGWVVLSDKVGVIEMARALAARVRWEARVIDLQDGSDQRLLVCQKPFIKK
Protein: Vacuolar amino acid transporter 1 (P47082)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for the vacuolar uptake of large neutral amino acids including tyrosine, glutamine, asparagine, isoleucine and leucine. Requires ATP for function.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:11274162, ECO:0000269|PubMed:25747199}; Multi-pass membrane protein {ECO:0000269|PubMed:11274162}.
Interaction partners:
- Vacuolar amino acid transporter 6
- Vacuolar basic amino acid transporter 1
- Vacuolar amino acid transporter 5
- Vacuolar amino acid transporter 7
- Vacuolar arginine/histidine antiporter YPQ2
Sequence:
MPEQEPLSPNGRKRSEVHYISIPLNRGSAFSPDDSVSQFQSDGFMTRRQSILDHPVGSFKGVNSLSRFATSLRRANSFRNIELNADNERSFFKESNDETYDPDTLAPALDGRRLSVTLNNAGRPRITNLANNDRVSTASMAIHDDDYGSIQNSTIGDSGSILRPTASLTEMMSGGAGRRFTNNDMDSIVVKRVEGVDGKVVTLLAGQSTAPQTIFNSINVLIGIGLLALPLGLKYAGWVIGLTMLAIFALATFCTAELLSRCLDTDPTLISYADLGYAAFGTKGRALISALFTLDLLGSGVSLVILFGDSLNALFPQYSTTFFKIVSFFIVTPPVFIPLSVLSNISLLGILSTTGTVLVICCCGLYKSSSPGSLVNPMETSMWPIDLKHLCLSIGLLSACWGGHAVFPNLKTDMRHPDKFKDCLKTTYKITSVTDIGTAVIGFLMFGNLVKDEITKNVLLTEGYPKFVYGLISALMTIIPIAKTPLNARPIVSVLDVLMNVQHIDEAASAIKRRAAKGLQVFNRIFINVVFVLIAINFPEFDKIIAFLGAGLCFTICLILPCWFYLRLCKTTIKPWERVACHVTICISVVLSTLGVGAAIIS
Protein: 2-oxoacid:ferredoxin oxidoreductase 2, subunit alpha (OFOR2) (EC 1.2.7.11) (Q9YBX7)
Organism: Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Function: Catalyzes the coenzyme A-dependent oxidative decarboxylation of different 2-oxoacids such as pyruvate, 2-oxobutyrate, glyoxylate and 2-oxoglutarate to form their CoA derivatives.
Interaction partners:
- 2-oxoacid:ferredoxin oxidoreductase 2, subunit beta
- 2-oxoacid:ferredoxin oxidoreductase 1, subunit beta
- Succinate--CoA ligase subunit beta
- Succinate--CoA ligase subunit alpha
- 2-oxoacid oxidoreductase
- isocitrate dehydrogenase
- Citrate synthase
- Pyruvate dehydrogenase complex, E2 component
- Pyruvate kinase
- 2-oxoacid oxidoreductase
Sequence:
MVDISLIIGGPQGGGIESAGQIAIKSMVLLGYEVLGSREYHSNIMGAHSYYHLRVQQHRPRSLKLPVDGVLALDAESVFTHFRDVRPGGILVYDPGTKSTRVDAIQPMAGPLKKRLKSLFDSRGMQPVVESAVKLAEEAGARIVGLPLKEMLKTLSERTGAPVARVSRALNTLGLASMLYMLGVPVEYIEKAISLQFAGKEKVINMNVEAVRIAVDYVREAFGEPESRLPPGPRRGQTMMVATGNDLVAMGKIVGGLGVITYYPITPSSDEALYVEKHSYISIDGPLAEKLGYDKIAVAIVQMEDELASINAVLGAAAAGARASTTTSGPGFSLMNEAVSLAVEAEIPVVVTLWMRAGPSTGMPTRTGQQDLLHSIFSGHGDAPKIVLASGDHVEAFYDAIKAFNWAEEFQTPVIHLLDKYLASSMVSLAREDLDPSKVPITRGKLLDNPPADYRRYEVVEDGISPRARLGSATMVITGLEHDEYGYATEDPVMREIMMFKRERKFKVIEERIPDEEKAVLHGDSEASVALVSFGSTKQPILEALEMLRDEGVRARFAQVRLLYPFPGRLVEEMLEGVEKVIMVEQNLLGQLAMLLRAHTSIKPDSSIVKINGRPLYSFEVAGAVKRILETGEERVVVSHGS
Protein: Uncharacterized protein (Q388G7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MWRISPQLLCAAGTSTANLQQFSFAKRFEEMKNDESCPLSGPEYALLLEKVEHYRSLQNTYAVKQSDIERAKRAAHYSGLEFTPKPPTKLTPKSGTA
Protein: Very-long-chain 3-oxoacyl-CoA reductase (EC 1.1.1.330) (3-ketoacyl-CoA reductase) (3-ketoreductase) (KAR) (Microsomal beta-keto-reductase) (P38286)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the microsomal membrane bound fatty acid elongation system, which produces the 26-carbon very long-chain fatty acids (VLCFA) from palmitate. Catalyzes the reduction of the 3-ketoacyl-CoA intermediate that is formed in each cycle of fatty acid elongation. VLCFAs serve as precursors for ceramide and sphingolipids.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03107, ECO:0000269|PubMed:23263984}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03107}.
Interaction partners:
- Very-long-chain enoyl-CoA reductase
- Very-long-chain
- Fatty acid elongase 2
- Fatty acid elongase 1
- Fatty acid elongase 3
- Acyl-CoA desaturase 1
- 3-oxoacyl-[acyl-carrier-protein] reductase
- 3-keto-steroid reductase ERG27
- Lanosterol synthase ERG7
- Sterol-4-alpha-carboxylate 3-dehydrogenase ERG26, decarboxylating
Sequence:
MTFMQQLQEAGERFRCINGLLWVVFGLGVLKCTTLSLRFLALIFDLFLLPAVNFDKYGAKTGKYCAITGASDGIGKEFARQMAKRGFNLVLISRTQSKLEALQKELEDQHHVVVKILAIDIAEDKESNYESIKELCAQLPITVLVNNVGQSHSIPVPFLETEEKELRNIITINNTATLLITQIIAPKIVETVKAENKKSGTRGLILTMGSFGGLIPTPLLATYSGSKSFLQGWSNSLAGELSKDAIDVELIISYLVTSSMSKIRRSSLMIPNPQQFVKSTLRSVGRRCGSQERYATMTPYWAHAVYQFVITETFGVYSKIVNSINYSFHKSIRIRALKKAARQVKKE