wanglab/gogpt-training-data huggingface dataset:
Protein: Gamete-specific minus 1 (Gamete-specific protein minus 1) (A0A098)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00108}.
Interaction partners:
- Uncharacterized protein
- Zys1A protein
- Zys1B protein
- RWP-RK domain-containing protein
- Uncharacterized protein
- RWP-RK domain-containing protein
- FHA domain-containing protein
- RWP-RK domain-containing protein
- F-box domain-containing protein
Sequence:
MASMAAELRPSDGGSSLHMLDSLLMMGLSSGGGVGGGGSSQSQILDSAGAAELAALLLPQHSNDPLHLMSTGDAALGLAGPMAAAEHHQHHPHHQHHSVPATAGFPSQTPPPPLFSNATAGAAPATRVRAAGSCGSGGVAGGTTSHSSEDGVFHSADPHHHHQQHLQQPQPQQQQQQQQQPQHQQQQQQQQQQQPQQPQFHHHQPQQHQAQQAVAATAPAAAADHLFLPPAAAGAAGQQQAGWGAATGAHLFHSDAPNRPNGPKTPTNRNGYAMKPPPPAAAAAVMSGHAMAASGVVAGRGGGGGGCDAEEDELTFAAAAAAEVSSDDEVMGGRGGAVMGRAAVGGFRTPAPAPASAGAAVNVAAAAPAAPAGTWVPKGKPAVEVSAWAPAPAAPVAAAAAAAVAVSPTVAAFAAAPVVEAVALVRSQQRQEQEHQLVQVAAAEQQDQQQAKRPVRSSRRRAQESQQAAAEAQQAAQQAAAAQQQQQHTGSGNIVGDKQGKPQGGLQQGRPVATQPSPPPPAVATAAAAAAATAPVATAPVATVATAATADTMPQRLTAVQQHEAYPAVVRGTLDVRKACLPRFPLVAREQAEAELQSVATAALQQAAAAPGASAAVTAAAAAAAAAATAAGEGKAGEGKAATARRGGRGAAEAEAAAALPAVGASGNPGLDEAMGAYVRVAALYGDEAAAAVAECESLMADFDNKLQLGNLATTFAAAASPTAAASGRARGGARSGGVGGGGTKRVASGANASGANSSGMSGGGGGDSAGAEAAAGDEMEWAPGATSVDTATGGADDEDGEEEEGQQPGGAAAAAAVAAAGGEASQLAASIAATYGSQLVQVAASLAQRPKVGKLPPAATQLLKGWWDDNFVWPYPSEEDKKQLGEAAALNNTQINNWFINQRKRHWHKHFPNRRPPSTREEAERLLRAAGAI
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q0VC49)
Organism: Bos taurus (Bovine)
Interaction partners:
- PAS domain-containing protein
- Protein LTV1 homolog
- Cryptochrome-1
- Period circadian protein homolog 2
- Aryl hydrocarbon receptor nuclear translocator like
- Neuronal PAS domain protein 2
- histone acetyltransferase
- Period circadian regulator 1
- Bystin
- Serine/threonine-protein kinase RIO2
Sequence:
MELRVGNKYRLGRKIGSGSFGDIYLGANIASGEEVAIKLECVKTKHPQLHIESKFYKMMQGGVGIPSIKWCGAEGDYNVMVMELLGPSLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKGNLVYIIDFGLAKKYRDARTHQHIPYRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKMSTPIEVLCKGYPSEFSTYLNFCRSLRFDDKPDYSYLRQLFRNLFHRQGFSYDYVFDWNMLKFVSLLKAEAGMGDWTGKANVTLWWAGLPEAGSYELDGTRDPHSSFIRADSLCCRGQQGPGGVPPPSGPERAHLGLPSVLDAWVSGARMALVGPPTVLILACSVLLLVSCTCQLAAFAESPLASLDPFIVASFSLVVAPWVLLGTSLFSLSLKSCGGGVGRSVQPLGLGLRNL
Protein: ThiH protein (Q72AA4)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- Thiazole synthase
- ThiF family protein
- Thiamine-phosphate synthase
- Thiamine biosynthesis protein ThiS
- ThiH protein, putative
- Phosphomethylpyrimidine synthase
- Thiamine-phosphate synthase
- Hydroxyethylthiazole kinase
- Response regulator
- Flagellar basal body rod protein FlgB
Sequence:
MSFYDELARWPHETLDALIASSTADDVLRALAATRPGPADLAALLSPAAMPYLEDMAQRAHELTVRHFGRTIQLFTPLYLANHCTNQCRYCGFNARNHIRRDQLDAERIMAEGRAIASTGLRQLLLLTGDAPRISTVSYIAEAAHRLRPLFPSIGVEVYAMQVEEYAELVAGGVESLTMFQETYNPGLYAWLHPAGPKRDFRFRLDAPERGCLGGMRSVGLGALLGLDDWRRDAFYTAMHGAWLQRYYPATEVSFSVPRMRPHTGSFEPQHPVSDRELVQILTAYRIFMPTAGITVSSREAAAFRDNLIPLGVTRMSAGVSTAVGGHAAGGDGNVASTEGAAAAIAASTAISSGDATGDLSGRSTKVDMTSGMAHAVTEDLQQGADAGPSQFDISDDRSVEEMVSAITARGYQPVFKDWEPPQDNVYACGAAGHADGTVRCEAR
Protein: Protein Vpu (U ORF protein) (Viral protein U) (P19554)
Organism: Human immunodeficiency virus type 1 group M subtype B (isolate SF162) (HIV-1)
Function: Enhances virion budding by targeting host CD4 and Tetherin/BST2 to proteasome degradation. Degradation of CD4 prevents any unwanted premature interactions between viral Env and its host receptor CD4 in the endoplasmic reticulum. Degradation of antiretroviral protein Tetherin/BST2 is important for virion budding, as BST2 tethers new viral particles to the host cell membrane. Mechanistically, Vpu bridges either CD4 or BST2 to BTRC, a substrate recognition subunit of the Skp1/Cullin/F-box protein E3 ubiquitin ligase, induces their ubiquitination and subsequent proteasomal degradation. The alteration of the E3 ligase specificity by Vpu seems to promote the degradation of host IKBKB, leading to NF-kappa-B down-regulation and subsequent apoptosis. Ion channel activity has also been suggested, however, formation of cation-selective channel has been reconstituted ex-vivo in lipid bilayers. It is thus unsure that this activity plays a role in vivo.
Subcellular location: Host membrane {ECO:0000255|HAMAP-Rule:MF_04082}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04082}.
Interaction partners:
Sequence:
MQPLQILAIVALVVAAIIAIVVWTIVYIEYRKILRQRKIDRLIDRITERAEDSGNESEGDQEELSALVERGHLAPWDVDDL
Protein: TATA box-binding protein-like 2 (TBP-like 2) (TATA box-binding protein-related factor 3) (TBP-related factor 3) (Q6SJ95)
Organism: Mus musculus (Mouse)
Function: Transcription factor required in complex with TAF3 for the differentiation of myoblasts into myocytes. The complex replaces TFIID at specific promoters at an early stage in the differentiation process.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q6SJ96, ECO:0000269|PubMed:17704303}. Nucleus {ECO:0000250|UniProtKB:Q6SJ96, ECO:0000269|PubMed:17704303}. Note=Present in the cytoplasm during cytokinesis. {ECO:0000250|UniProtKB:Q6SJ96}.
Interaction partners:
- Transcription initiation factor TFIID subunit 3
- Transcription initiation factor IIB
- Transcription initiation factor TFIID subunit 6
- Transcription initiation factor TFIID subunit 10
- Myoblast determination protein 1
- Transcription initiation factor TFIID subunit 12
- Transcription initiation factor TFIID subunit 1
- TATA box-binding protein-like 1
- B-TFIID TATA-box binding protein associated factor 1
- X-box-binding protein 1
Sequence:
MVGSLIMEEDIYLDLFLDPYTIQDDFPPAMSQLFSPGVPLDMHSLPSNPETVFHPHLGGVKKASTDFSSVDLSFLPDELTQENRDQTVTGNKLASEESCRTRDRQSQLQLPDEHGSELNLNSNSSPDPQSCLCFDDAHSNQPSPETPNSNALPVALIASMMPMNPVPGFSGIVPQLQNVVSTANLACKLDLRKIALNAKNTEYNPKRFAAVIMRIREPRTTALIFSSGKVVCTGAKSEEESRLAARKYARVVQKLGFPVRFFNFKIQNMVGSCDVKFPIRLEILALTHRQFSSSYEPELFPGLIYKMVKPQVVLLIFASGKVVLTGAKERSEIYEAFENMYPILESFKKV
Protein: Mitochondrial fission regulator 1 (Chondrocyte protein with a poly-proline region) (Q9PTD5)
Organism: Gallus gallus (Chicken)
Function: May play a role in mitochondrial aerobic respiration. May also regulate mitochondrial organization and fission.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:15389597}. Note=May be associated with the inner and the outer mitochondrial membrane.
Interaction partners:
Sequence:
MIRWFKCFMRMIFEQVGLNMESVLWSSKPYGSSRSIVRKIGTNLSLIQCPRVQFQLTSQAAEGNHPHQFREDAVASFADVGWVAQEEGEVSTRLRSEVWSKTAQPLPGELHQPGHSLGRQDSVPNLLHEEPAPRSTVIANEEAMQKISALENELATLRAQIAKIVILQEQQNLTAAGLSPVASAAVPCVPPPPPPPPPPPLPPPALQQSMSAIELIRERKNRKTNSGPIPTENGPKKPEIPNMLEILKDMNSVKLRSVKKSSGDTKPKVADPTDPAALIAEALKKKFAYRYRRDSQSESDKVIPKSETNTKTEVVLFGPHMLKSTGKMKTLIEKS
Protein: Translocation protein SEC72 (Sec62/63 complex 23 kDa subunit) (p23) (P39742)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acts as non-essential component of the Sec62/63 complex which is involved in SRP-independent post-translational translocation across the endoplasmic reticulum (ER) and functions together with the Sec61 complex and KAR2 in a channel-forming translocon complex. A cycle of assembly and disassembly of Sec62/63 complex from SEC61 may govern the activity of the translocon. SEC72 may be involved in signal peptide recognition for a defined subset of leader peptides, or may increase the efficiency of unusual or 'difficult' secretory precursors to the translocation pore, it may be that this protein binds charged leader peptides to the membrane until they engage the translocation apparatus.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Protein translocation protein SEC63
- Translocation protein SEC62
- Protein transport protein SSS1
- Translocation protein SEC66
- Protein transport protein SEC61
- Protein transport protein SBH1
- Mediator of RNA polymerase II transcription subunit 15
- Protein transport protein SBH2
- Endoplasmic reticulum chaperone BiP
- Hsp90 co-chaperone AHA1
Sequence:
MVTLEYNANSKLITASDAVVALSTETNIDQINVLTTSLIGETNPNFTPQPNEALSKMIKGLFESGMKNLQQKKLNEALKNVSLAIEMAQRKRAPWEAFAIQLPELHFMLRSKIDLCLILGKHLEALQDLDFLLGTGLIQPDVFVRKADCLLKLRQWEEARATCERGLALAPEDMKLRALLIETARNLAEYNGE
Protein: Large ribosomal subunit protein uL16 (50S ribosomal protein L16) (P9WHD5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs.
Interaction partners:
- Large ribosomal subunit protein uL1
- Small ribosomal subunit protein uS4
- Large ribosomal subunit protein uL23
- Small ribosomal subunit protein uS7
- Small ribosomal subunit protein uS8
- Large ribosomal subunit protein bL34
- Large ribosomal subunit protein bL19
- Small ribosomal subunit protein bS18A
- Large ribosomal subunit protein uL2
- Small ribosomal subunit protein uS19
Sequence:
MLIPRKVKHRKQHHPRQRGIASGGTTVNFGDYGIQALEHAYVTNRQIESARIAINRHIKRGGKVWINIFPDRPLTKKPAETRMGSGKGSPEWWVANVKPGRVLFELSYPNEGVARAALTRAIHKLPIKARIITREEQF
Protein: 1-acylglycerol-3-phosphate O-acyltransferase 5 (Lysophosphatidic acid acyltransferase, epsilon), isoform CRA_a (Testicular tissue protein Li 144) (A0A024R640)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}.
Interaction partners:
Sequence:
MLLSLVLHTYSMRYLLPSVVLLGTAPTYVLAWGVWRLLSAFLPARFYQALDDRLYCVYQSMVLFFFENYTGVQILLYGDLPKNKENIIYLANHQSTVDWIVADILAIRQNALGHVRYVLKEGLKWLPLYGCYFAQHGGIYVKRSAKFNEKEMRNKLQSYVDAGTPMYLVIFPEGTRYNPEQTKVLSASQAFAAQRGLAVLKHVLTPRIKATHVAFDCMKNYLDAIYDVTVVYEGKDDGGQRRESPTMTEFLCKECPKIHIHIDRIDKKDVPEEQEHMRRWLHERFEIKDKMLIEFYESPDPERRKRFPGKSVNSKLSIKKTLPSMLILSGLTAGMLMTDAGRKLYVNTWIYGTLLGCLWVTIKA
Protein: Endoplasmic oxidoreductin-1 (EC 1.8.4.-) (Endoplasmic reticulum oxidoreductase protein 1) (Q03103)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. Acts by oxidizing directly PDI1 isomerase through a direct disulfide exchange. Does not act as a direct oxidant of folding substrate, but relies on PDI1 to transfer oxidizing equivalent. Also able to oxidize directly the PDI related protein MPD2. Does not oxidize all PDI related proteins, suggesting that it can discriminate between PDI1 and related proteins. Reoxidation of ERO1 probably involves electron transfer to molecular oxygen via FAD. Acts independently of glutathione. May be responsible for a significant proportion of reactive oxygen species (ROS) in the cell, thereby being a source of oxidative stress.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11707280, ECO:0000269|PubMed:9659913, ECO:0000269|PubMed:9659914}; Peripheral membrane protein {ECO:0000269|PubMed:11707280, ECO:0000269|PubMed:9659913, ECO:0000269|PubMed:9659914}; Lumenal side {ECO:0000269|PubMed:11707280, ECO:0000269|PubMed:9659913, ECO:0000269|PubMed:9659914}.
Interaction partners:
- Protein disulfide-isomerase
- Protein disulfide-isomerase EUG1
- ER-retained PMA1-suppressing protein 1
- Endoplasmic reticulum chaperone BiP
- Protein disulfide-isomerase MPD1
- FAD-linked sulfhydryl oxidase ERV2
- Transcriptional activator HAC1
- Heat shock protein 70 homolog LHS1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
- Calnexin homolog
Sequence:
MRLRTAIATLCLTAFTSATSNNSYIATDQTQNAFNDTHFCKVDRNDHVSPSCNVTFNELNAINENIRDDLSALLKSDFFKYFRLDLYKQCSFWDANDGLCLNRACSVDVVEDWDTLPEYWQPEILGSFNNDTMKEADDSDDECKFLDQLCQTSKKPVDIEDTINYCDVNDFNGKNAVLIDLTANPERFTGYGGKQAGQIWSTIYQDNCFTIGETGESLAKDAFYRLVSGFHASIGTHLSKEYLNTKTGKWEPNLDLFMARIGNFPDRVTNMYFNYAVVAKALWKIQPYLPEFSFCDLVNKEIKNKMDNVISQLDTKIFNEDLVFANDLSLTLKDEFRSRFKNVTKIMDCVQCDRCRLWGKIQTTGYATALKILFEINDADEFTKQHIVGKLTKYELIALLQTFGRLSESIESVNMFEKMYGKRLNGSENRLSSFFQNNFFNILKEAGKSIRYTIENINSTKEGKKKTNNSQSHVFDDLKMPKAEIVPRPSNGTVNKWKKAWNTEVNNVLEAFRFIYRSYLDLPRNIWELSLMKVYKFWNKFIGVADYVSEETREPISYKLDIQ
Protein: Cyclin-dependent kinases regulatory subunit (Cell division control protein CKS1) (P20486)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Binds to the catalytic subunit of the cyclin dependent kinase (CDC28) and is essential for its biological function.
Interaction partners:
- G2/mitotic-specific cyclin-2
- G2/mitotic-specific cyclin-3
- Cyclin-dependent kinase 1
- S-phase entry cyclin-5
- G1/S-specific cyclin CLN2
- G1/S-specific cyclin CLN1
- Protein SIC1
- Cyclin-dependent protein kinase PHO85
- Suppressor of kinetochore protein 1
- Serine/threonine-protein kinase CAK1
Sequence:
MYHHYHAFQGRKLTDQERARVLEFQDSIHYSPRYSDDNYEYRHVMLPKAMLKVIPSDYFNSEVGTLRILTEDEWRGLGITQSLGWEHYECHAPEPHILLFKRPLNYEAELRAATAAAQQQQQQQQQQQQQQQQHQTQSISNDMQVPPQIS
Protein: Protein IBD2 (Inhibition of bud division protein 2) (P53892)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Part of a checkpoint which monitors spindle integrity and prevents premature exit from mitosis. This cell-cycle arrest depends upon inhibition of the G-protein TEM1 by the BFA1/BUB2 complex.
Subcellular location: Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:12072457}.
Interaction partners:
Sequence:
MTPTNQSSGTTNASVEVLSEDGPMPINVMMQEGVKALTKILSNQLQDRQAFQNAPHAMQFVIRNGGKALSNARLEELKDALPKMDSLSLEDELAKIDGQSAYHIDSAEEKETFESKIGQIASRNSADFIIEEDLQNILDDDLKDSELNLDGEEAEIIFDYESQELDTPDGIGEKISQMIESVLPGGFGSEEQGGLRTVTNVEDLDVAEEVTDIDHDTVDAARLHGDGQHSISSRKHSRSKNSKKNGHVRRHDFYDESRDHKSCCPHHHYENLSKLRNYYYHDFEYISRTENRVPDFSVLVNESSPMCLFCEYYMVFGEPPRNMIKWYNRTFGYNRMPNPPRDEQDSRKRNR
Protein: Uncharacterized protein (Q9VIQ7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Uncharacterized protein, isoform B
- Accessory gland protein Acp32CD
- Extracellular serine/threonine protein CG31145
- GILT-like protein 3
Sequence:
MAKLELKLIGIAIFLVAALEAQETPAAESSPASPTDGETSPVTEASSIGELTQTTEAGSEVTESPTNSTDMVNSTDNPDPNGSPDPENGGDPFVKPGSHIKGPRHVRAHDGFHSLKTEKHWASWNDAFTTPRP
Protein: Constitutive ornithine decarboxylase (EC 4.1.1.17) (P21169)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Agmatinase
- Polyamine aminopropyltransferase
- Spermidine N
- Putrescine aminotransferase
- Gamma-glutamylputrescine synthetase PuuA
- Putrescine transporter PotE
- Inducible ornithine decarboxylase
- S-adenosylmethionine decarboxylase proenzyme
- Ornithine carbamoyltransferase subunit I
Sequence:
MKSMNIAASSELVSRLSSHRRVVALGDTDFTDVAAVVITAADSRSGILALLKRTGFHLPVFLYSEHAVELPAGVTAVINGNEQQWLELESAACQYEENLLPPFYDTLTQYVEMGNSTFACPGHQHGAFFKKHPAGRHFYDFFGENVFRADMCNADVKLGDLLIHEGSAKDAQKFAAKVFHADKTYFVLNGTSAANKVVTNALLTRGDLVLFDRNNHKSNHHGALIQAGATPVYLEASRNPFGFIGGIDAHCFNEEYLRQQIRDVAPEKADLPRPYRLAIIQLGTYDGTVYNARQVIDTVGHLCDYILFDSAWVGYEQFIPMMADSSPLLLELNENDPGIFVTQSVHKQQAGFSQTSQIHKKDNHIRGQARFCPHKRLNNAFMLHASTSPFYPLFAALDVNAKIHEGESGRRLWAECVEIGIEARKAILARCKLFRPFIPPVVDGKLWQDYPTSVLASDRRFFSFEPGAKWHGFEGYAADQYFVDPCKLLLTTPGIDAETGEYSDFGVPATILAHYLRENGIVPEKCDLNSILFLLTPAESHEKLAQLVAMLAQFEQHIEDDSPLVEVLPSVYNKYPVRYRDYTLRQLCQEMHDLYVSFDVKDLQKAMFRQQSFPSVVMNPQDAHSAYIRGDVELVRIRDAEGRIAAEGALPYPPGVLCVVPGEVWGGAVQRYFLALEEGVNLLPGFSPELQGVYSETDADGVKRLYGYVLK
Protein: Stathmin (Leukemia-associated gene protein) (Leukemia-associated phosphoprotein p18) (Metablastin) (Oncoprotein 18) (Op18) (Phosphoprotein p19) (pp19) (Prosolin) (Protein Pr22) (pp17) (P54227)
Organism: Mus musculus (Mouse)
Function: Involved in the regulation of the microtubule (MT) filament system by destabilizing microtubules. Prevents assembly and promotes disassembly of microtubules. Phosphorylation at Ser-16 may be required for axon formation during neurogenesis (By similarity). Involved in the control of the learned and innate fear.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Mitogen-activated protein kinase 3
- Mitogen-activated protein kinase 1
- Cyclin-dependent kinase inhibitor 1B
- Signal transducer and activator of transcription 3
- Serine/threonine-protein kinase Kist
Sequence:
MASSDIQVKELEKRASGQAFELILSPRSKESVPDFPLSPPKKKDLSLEEIQKKLEAAEERRKSHEAEVLKQLAEKREHEKEVLQKAIEENNNFSKMAEEKLTHKMEANKENREAQMAAKLERLREKDKHVEEVRKNKESKDPADETEAD
Protein: Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial (DLST) (EC 2.3.1.61) (2-oxoglutarate dehydrogenase complex component E2) (OGDC-E2) (OGDHC subunit E2) (Alpha-ketoglutarate dehydrogenase subunit E2) (alpha-KGDHC subunit E2) (Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex) (P19262)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:25165143}.
Interaction partners:
- 2-oxoglutarate dehydrogenase, mitochondrial
- Dihydrolipoyl dehydrogenase, mitochondrial
- Succinate--CoA ligase subunit alpha, mitochondrial
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- Succinate--CoA ligase subunit beta, mitochondrial
- Isocitrate dehydrogenase subunit 2, mitochondrial
- Alpha-ketoglutarate dehydrogenase subunit 4, mitochondrial
- Increased recombination centers protein 15
- Isocitrate dehydrogenase subunit 1, mitochondrial
- Aconitate hydratase, mitochondrial
Sequence:
MLSRATRTAAAKSLVKSKVARNVMAASFVKRHASTSLFKQANKVESLGSIYLSGKKISVAANPFSITSNRFKSTSIEVPPMAESLTEGSLKEYTKNVGDFIKEDELLATIETDKIDIEVNSPVSGTVTKLNFKPEDTVTVGEELAQVEPGEAPAEGSGESKPEPTEQAEPSQGVAARENSSEETASKKEAAPKKEAAPKKEVTEPKKADQPKKTVSKAQEPPVASNSFTPFPRTETRVKMNRMRLRIAERLKESQNTAASLTTFNEVDMSALMEMRKLYKDEIIKKTGTKFGFMGLFSKACTLAAKDIPAVNGAIEGDQIVYRDYTDISVAVATPKGLVTPVVRNAESLSVLDIENEIVRLSHKARDGKLTLEDMTGGTFTISNGGVFGSLYGTPIINSPQTAVLGLHGVKERPVTVNGQIVSRPMMYLALTYDHRLLDGREAVTFLKTVKELIEDPRKMLLW
Protein: Glycogenin-1 (GN-1) (GN1) (EC 2.4.1.186) (O08730)
Organism: Rattus norvegicus (Rat)
Function: Self-glucosylates, via an inter-subunit mechanism, to form an oligosaccharide primer that serves as substrate for glycogen synthase.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P13280}. Nucleus {ECO:0000250|UniProtKB:P13280}. Note=Localizes to glycogen granules (glycosomes) in the cytoplasm (By similarity). Cytosolic localization is dependent on the actin cytoskeleton (By similarity). {ECO:0000250|UniProtKB:C4R941, ECO:0000250|UniProtKB:P13280}.
Interaction partners:
- Glycogen [starch] synthase, muscle
- RING-type E3 ubiquitin transferase
- 1,4-alpha-glucan branching enzyme
- Glycogen debranching enzyme
- Glycogen [starch] synthase, liver
- Protein phosphatase 1 regulatory subunit 3C
- Lysosomal alpha-glucosidase
- DNA polymerase delta subunit 2
- DNA polymerase delta catalytic subunit
Sequence:
MTDQAFVTLTTNDAYAKGALVLGSSLKQHRTTRRTVVLASPQVSDSMRKVLETVFDEVIMVDVLDSGDSAHLTLMKRPELGITLTKLHCWSLTQYSKCVFMDADTLVLSNIDDLFEREELSAAPDPGWPDCFNSGVFVYQPSIETYNQLLHLASEQGSFDGGDQGLLNTYFSGWATTDITKHLPFVYNLSSLSIYSYLPAFKAFGKNAKVVHFLGRTKPWNYTYNPQTKSVKCESQDPIVSHPEFLNLWWDTFTTNVLPLLQHHGLVKDAGSYLMMEHVTGALSDLSFGEAPPASQPSLSSEERKERWEQGQADYMGADSFDNIKRKLDTYLQ
Protein: Cytochrome b mRNA maturase bI3 (Q9ZZW7)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Mitochondrial mRNA maturase required for splicing of intron 3 of the cytochrome b (COB) gene, containing its own coding sequence. In vivo splicing requires the formation of a ribonucleoprotein complex together with the imported mitochondrial RNA-splicing protein MRS1. The complex seems to stimulate the intrinsic ribozyme activity of intron bI3 through binding to and stabilizing specific secondary and tertiary structure elements in the RNA.
Subcellular location: Mitochondrion inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Intron-encoded DNA endonuclease aI5 beta
- Cytochrome c oxidase subunit 2
- Intron-encoded DNA endonuclease aI5 alpha
- Cytochrome c oxidase subunit 3
- Cytochrome b mRNA maturase bI2
- Cytochrome c oxidase subunit 1
- Intron-encoded RNA maturase bI4
- Cytochrome b
Sequence:
MAFRKSNVYLSLVNSYIIDSPQPSSINYWWNMGSLLGLCLVIQIVTGIFMAMHYSSNIELAFSSVEHIMRDVHNGYILRYLHANGASFFFMVMFMHMAKGLYYGSYRSPRVTLWNVGVIIFILTIATAFLGYCCVYGQMSHWGATVITNLFSAIPFVGNDIVSWLWGGFNMEDPYYSNMMLNKSVLCWNIFIWMMNYYIIQLIIYNNMIWNKNNMVKMFIMRRKLAVINMYMYMKLIIQRTYSYYMNNTIIYDKNHKLNTDNPIYAYIGGLFEGDGWITISKKGKYLLYELGIEMHIRDIQLLYKIKNILGIGKVTIKKLKMKDGTIKEMCKFNVRNKNHLKNIIIPIFDKYPMLTNKHYDYLYFKDNLLKDIKYYNDLSYYLRPIKPFNTTEDILNKNYFSSWLIGFFEAESCFSIYKPMNKKMKTASFEVSQNNSMEVMLAIKSYLKITQNIYTDKFNNSRMTTKSINGIKNVVMFINNNPIKLLGYKKLQYLLFLKDLRTITKYNNYFKIPPKY
Protein: Holin-like protein 24.1 (Gene product 24.1) (gp24.1) (O48470)
Organism: Bacillus phage SPP1 (Bacteriophage SPP1)
Function: Probably functions as a holin together with holin-like protein 26. Accumulates harmlessly in the cytoplasmic membrane until it reaches a critical concentration that triggers the formation of micron-scale pores (holes) causing host cell membrane disruption and endolysin escape into the periplasmic space. Determines the precise timing of host cell lysis.
Subcellular location: Host cell inner membrane {ECO:0000269|PubMed:27825035}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MEQMRQDIIELKQNDKSQEQRISLLERTSDRHDQQIQAVTESLSKIHENTTWIKRTITGAIISTLSTVVVGGILTIVWNLVKN