wanglab/gogpt-training-data huggingface dataset:
Protein: Threonine synthase (TS) (EC 4.2.3.1) (P16120)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine.
Interaction partners:
- Homoserine dehydrogenase
- Homoserine kinase
- Aspartokinase
- Phosphoserine phosphatase
- Threonine dehydratase, mitochondrial
- Catabolic L-serine/threonine dehydratase
- Phosphoserine aminotransferase
- Pyrroline-5-carboxylate reductase
- Aspartate-semialdehyde dehydrogenase
- Low specificity L-threonine aldolase
Sequence:
MPNASQVYRSTRSSSPKTISFEEAIIQGLATDGGLFIPPTIPQVDQATLFNDWSKLSFQDLAFAIMRLYIAQEEIPDADLKDLIKRSYSTFRSDEVTPLVQNVTGDKENLHILELFHGPTYAFKDVALQFVGNLFEYFLQRTNANLPEGEKKQITVVGATSGDTGSAAIYGLRGKKDVSVFILYPTGRISPIQEEQMTTVPDENVQTLSVTGTFDNCQDIVKAIFGDKEFNSKHNVGAVNSINWARILAQMTYYFYSFFQATNGKDSKKVKFVVPSGNFGDILAGYFAKKMGLPIEKLAIATNENDILDRFLKSGLYERSDKVAATLSPAMDILISSNFERLLWYLAREYLANGDDLKAGEIVNNWFQELKTNGKFQVDKSIIEGASKDFTSERVSNEETSETIKKIYESSVNPKHYILDPHTAVGVCATERLIAKDNDKSIQYISLSTAHPAKFADAVNNALSGFSNYSFEKDVLPEELKKLSTLKKKLKFIERADVELVKNAIEEELAKMKL
Protein: RAB8A, member RAS oncogene family (Rab8a protein) (Ras-related protein Rab-8A (EC 3.6.5.2)) (A4FVK4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004635}.
Interaction partners:
- RAB3A-interacting protein
- WD repeat domain 41
- Guanine nucleotide exchange protein smcr8b
- Guanine nucleotide exchange C9orf72 homolog
- Myosin VB
- Centrosomal protein of 290 kDa
- Intraflagellar transport protein 20 homolog
- MICAL-like protein 2a
- Guanine nucleotide exchange protein smcr8a
- Protein ref
Sequence:
MAKTYDYLFKLLLIGDSGVGKTCVLFRFSEDAFNSTFISTIGIDFKIRTIELDGKKIKLQIWDTAGQERFRTITTAYYRGAMGIMLVYDITNEKSFDNIKNWIRNIEEHASADVEKMILGNKCDINEKRQVSKDRGEKLALEYGIKFMETSAKANINVENAFLTLARDIKAKMDTKLEGNNPQGSNHGVKITTEQPKKSSFFRCVLL
Protein: Atlastin-2 (EC 3.6.5.-) (ADP-ribosylation factor-like protein 6-interacting protein 2) (ARL-6-interacting protein 2) (Aip-2) (Q6PA06)
Organism: Mus musculus (Mouse)
Function: GTPase tethering membranes through formation of trans-homooligomers and mediating homotypic fusion of endoplasmic reticulum membranes. Functions in endoplasmic reticulum tubular network biogenesis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8NHH9}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8NHH9}. Note=Localizes at endoplasmic reticulum (ER) three-way tubular junctions. {ECO:0000250|UniProtKB:Q8NHH9}.
Interaction partners:
- Spastin
- Receptor expression-enhancing protein 1
- Endoplasmic reticulum junction formation protein lunapark
- ADP-ribosylation factor-like protein 6-interacting protein 1
- Reticulon-2
- Spartin
Sequence:
MAEGDEAARRQQPQQGLRRRRQTSDSSVGVNHVSSTTSLGEDYEDDDLVNSDEVMKKPCPVQIVLAHEDDHNFELDEEALEQILLQEHIRDLNIVVVSVAGAFRKGKSFLLDFMLRYMYNKDSQSWIGGNNEPLTGFTWRGGCERETTGIQVWNEVFVIDRPNGTKVAVLLMDTQGAFDSQSTIKDCATVFALSTMTSSVQVYNLSQNIQEDDLQHLQLFTEYGRLAMEEIYQKPFQTLMFLIRDWSYPYEHSYGLEGGKQFLEKRLQVKQNQHEELQNVRKHIHNCFSNLGCFLLPHPGLKVATNPSFDGRLKDIDEDFKRELRNLVPLLLAPENLVEKEISGSKVTCRDLVEYFKAYIKIYQGEELPHPKSMLQATAEANNLAAVAGARDVYCKSMEQVCGGDKPYIAPSDLERKHLDLKEVALKQFRSVKKMGGDEFCRRYQDQLEAEIEETYANFIKHNDGKNIFYAARTPATLFAVMFAMYIISGLTGFIGLNSIAVLCNLVMGLALTSLCTWAYVKYSGEFREIGTMIDQIAETLWEQVLKPLGDNLMEENIRQSVTNSIKAGLTDQVSHHARLKTD
Protein: Peroxisomal 2,4-dienoyl-CoA reductase [(3E)-enoyl-CoA-producing] (EC 1.3.1.124) (2,4-dienoyl-CoA reductase 2) (DCR-AKL) (pVI-AKL) (Q9Z2M4)
Organism: Rattus norvegicus (Rat)
Function: Auxiliary enzyme of beta-oxidation. Participates in the degradation of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions in peroxisome. Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA. Has activity towards short and medium chain 2,4-dienoyl-CoAs, but also towards 2,4,7,10,13,16,19-docosaheptaenoyl-CoA, suggesting that it does not constitute a rate limiting step in the peroxisomal degradation of docosahexaenoic acid.
Subcellular location: Peroxisome {ECO:0000269|PubMed:10333503}.
Interaction partners:
Sequence:
MTQQPPDVEEDDCLSEYHHLFCPDLLQDKVAFITGGGSGIGFRIAEIFMRHGCHTVIVSRSLPRVSEAAKKLVAATGKRCLPLSMDVRVPPAVMAAVDQALKEFGKIDILINCAAGNFLCPASALSFNAFKTVVDIDTLGTFNVSRVLYEKFFRDHGGVIVNITATLSMRGQVLQLHAGAAKAAVDAMTRHLAVEWGPQNIRVNSLAPGAISGTEGLRRLGGPKASSKFKYLSSPIPRLGTKTEIAHSVLYLASPLASYVSGIVLVVDGGSWMTLPNDIGRLLEFESSSAKL
Protein: Kallikrein 1-related peptidase b9 (EC 3.4.21.35) (Epidermal growth factor-binding protein type C) (EGF-BP C) (Glandular kallikrein K9) (mGK-9) (Tissue kallikrein-9) (P15949)
Organism: Mus musculus (Mouse)
Function: Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin.
Interaction partners:
- Plasma protease C1 inhibitor
- Alpha-2-macroglobulin-P
- Pregnancy zone protein
- Kininogen-1
- B2 bradykinin receptor
- B1 bradykinin receptor
- Angiotensin-converting enzyme
- Antithrombin-III
- Renin-1
Sequence:
MRFLILFLALSLGGIDAAPPVHSRIVGGFKCEKNSQPWHVAVYRYNEYICGGVLLDANWVLTAAHCYYEENKVSLGKNNLYEEEPSAQHRLVSKSFLHPGYNRSLHRNHIRHPEYDYSNDLMLLRLSKPADITDVVKPIALPTEEPKLGSTCLASGWGSTTPFKFQNAKDLQCVNLKLLPNEDCGKAHIEKVTDVMLCAGETDGGKDTCKGDSGGPLICDGVLQGITSWGFTPCGEPKKPGVYTKLIKFTSWIKDTMAKNL
Protein: Endoprotease bli-4 (EC 3.4.21.-) (Blisterase) (Blistered cuticle protein 4) (P51559)
Organism: Caenorhabditis elegans
Function: Serine endoprotease which cleaves proproteins at paired basic amino acids (Probable). Involved in cuticle biosynthesis probably by cleaving pro-collagen into its mature form. Acts in ASEL sensory neurons to regulate high salt chemotaxis responses probably by cleaving insulin-like protein ins-6 into its mature and active form. Essential for embryonic and larval development. isoform a, isoform e, isoform f, isoform g and isoform h are involved in cuticle biosynthesis but are dispensable for larval development.
Subcellular location: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Cuticle collagen dpy-5
- Kunitz-type protein bli-5
- C-mannosyltransferase dpy-19
- Protein unc-119
- Cyclin N-terminal domain-containing protein
- Phorbol ester/diacylglycerol-binding protein unc-13
- Cuticle collagen dpy-10
Sequence:
MRISIGRIAWQILAVLIAVAFTIEHDSICDESIGACGEPIHTVIRLAKRDDELARRIAADHDMHVKGDPFLDTHYFLYHSETTRTRRHKRAIVERLDSHPAVEWVEEQRPKKRVKRDYILLDNDVHHSNPFRRSVLNRDGTRRAQRQQPQSPREIPSLPFPDPLYKDQWYLHGGAVGGYDMNVRQAWLQGYAGRNVSVSILDDGIQRDHPDLAANYDPLASTDINDHDDDPTPQNNGDNKHGTRCAGEVAALAGNNQCGVGVAFKAKIGGVRMLDGAVSDSVEAASLSLNQDHIDIYSASWGPEDDGKTFDGPGPLAREAFYRGIKNGRGGKGNIFVWASGNGGSRQDSCSADGYTTSVYTLSISSATYDNHRPWYLEECPSSIATTYSSADFRQPAIVTVDVPGGCTDKHTGTSASAPLAAGIIALALEANPELTWRDMQHLVLRTANWKPLENNPGWSRNGVGRMVSNKFGYGLIDGGALVNMAKTWKTVPEQHICTYEYRLANPNPRPIVGRFQLNFTLDVNGCESGTPVLYLEHVQVHATVRYLKRGDLKLTLFSPSGTRSVLLPPRPQDFNANGFHKWPFLSVQQWGEDPRGTWLLMVESVTTNPAATGTFHDWTLLLYGTADPAQSGDPVYSATPATSQGVLSRVHQLTSQVEESAPISFPDLTSAGNCHDECNGGCTESSSATSCFACKHLTQTLRNKGGSGFKCVQKCDDTYYLDGDKCKMCSSHCHTCTKAEVCETCPGSLLLIDVDNMPHYDHGKCVESCPPGLVADYESNLVQAKCIWRKDLCGDGYYINAVGKCDLCDSSCETCTAPGPMSCEKCSKGYGKGSIGYCRPCCPEGSTKSWQCEDCSKPDPTLLIDSNKSSGFGLMFWIVVSLIAACGICACKKCASETKSSNVEYAPLAQYNATNGAINLGAHTDDEDDDEDEVFVNPQIV
Protein: Chaperonin GroEL 2 (EC 5.6.1.7) (60 kDa chaperonin 2) (65 kDa antigen) (Antigen A) (Cell wall protein A) (Chaperonin-60 2) (Cpn60 2) (Heat shock protein 65) (HSP65) [Cleaved into: Cleaved form] (P9WPE7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding (By similarity). Prevents aggregation of substrate proteins and promotes their refolding. In vitro, activity may be independent of the presence or absence of the GroES co-chaperonin or ATP. Shows weak ATPase activity.
Subcellular location: Secreted, capsule {ECO:0000269|PubMed:19470749, ECO:0000269|PubMed:20633027}. Cell surface {ECO:0000269|PubMed:19470749, ECO:0000269|PubMed:20633027}. Secreted, cell wall {ECO:0000269|PubMed:24830429}. Note=Although thought of as a cytoplasmic chaperone this protein is routinely found extracellularly in the absence of cell lysis. {ECO:0000305|PubMed:19470749}.; SUBCELLULAR LOCATION: [Cleaved form]: Secreted {ECO:0000269|PubMed:24830429}. Host mitochondrion {ECO:0000269|PubMed:28288970}. Note=Exits phagosomal membrane and reaches macrophage mitochondria. {ECO:0000269|PubMed:28288970}.
Interaction partners:
- Co-chaperonin GroES
- Chaperone protein DnaK
- Protein GrpE
- Chaperone protein DnaJ 1
- Chaperonin GroEL 1
- DNA-directed RNA polymerase subunit beta
- Possible formate hydrogenase HycE
- Chaperone protein DnaJ 2
- 6 kDa early secretory antigenic target
- Chaperone protein HtpG
Sequence:
MAKTIAYDEEARRGLERGLNALADAVKVTLGPKGRNVVLEKKWGAPTITNDGVSIAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVREGLRNVAAGANPLGLKRGIEKAVEKVTETLLKGAKEVETKEQIAATAAISAGDQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTEGMRFDKGYISGYFVTDPERQEAVLEDPYILLVSSKVSTVKDLLPLLEKVIGAGKPLLIIAEDVEGEALSTLVVNKIRGTFKSVAVKAPGFGDRRKAMLQDMAILTGGQVISEEVGLTLENADLSLLGKARKVVVTKDETTIVEGAGDTDAIAGRVAQIRQEIENSDSDYDREKLQERLAKLAGGVAVIKAGAATEVELKERKHRIEDAVRNAKAAVEEGIVAGGGVTLLQAAPTLDELKLEGDEATGANIVKVALEAPLKQIAFNSGLEPGVVAEKVRNLPAGHGLNAQTGVYEDLLAAGVADPVKVTRSALQNAASIAGLFLTTEAVVADKPEKEKASVPGGGDMGGMDF
Protein: F-box domain-containing protein (Q2YS44)
Organism: Caenorhabditis elegans
Interaction partners:
- Acyltransferase
Sequence:
MEANQINEKMAKKLTDELKAIEISGPPSLFDMPMCVMHTIVDNLDAIDRLILRYVNRKLRNFVDNKKPIFKNVKVYSVVGGYNLVLGHDKSTIFYDSKGSGCIARCDGRRMRKINKSSLAALFGDLEVWMKNPQLQLDKFSLYAVCDDELTTNLLKKITNVEYMFHAKSIYLSVAKFSNVISILSHFKPGFLEEIVFFCHSGHESIHELFLLEQWKQVKSVFIKWFPFDDFPFEHLVHVSCFELNLPRISVSVAIIIRDVLMKTAQFEYGKIRLYDLNNMDDPPDIEADVVRVFNPNFVDEYVTRPLQFKVEQFLVTIHKRSLRIKKIENPR
Protein: Cytochrome P450 monooxygenase abl2 (EC 1.-.-.-) (Abscisic acid biosynthesis cluster protein 2) (Q5K0D9)
Organism: Botryotinia fuckeliana (Noble rot fungus) (Botrytis cinerea)
Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of abscisic acid (ABA), a phytohormone that acts antagonistically toward salicylic acid (SA), jasmonic acid (JA) and ethylene (ETH) signaling, to impede plant defense responses. The first step of the pathway catalyzes the reaction from farnesyl diphosphate to alpha-ionylideneethane performed by the alpha-ionylideneethane synthase aba3 via a three-step reaction mechanism involving 2 neutral intermediates, beta-farnesene and allofarnesene. The cytochrome P450 monooxygenase aba1 might then be involved in the conversion of alpha-ionylideneethane to alpha-ionylideneacetic acid (Probable). Alpha-ionylideneacetic acid is further converted to abscisic acid in 2 steps involving the cytochrome P450 monooxygenase aba2 and the short-chain dehydrogenase/reductase aba4, via the intermediates 1'-deoxy-ABA or 1',4'-trans-diol-ABA, depending on the order of action of these 2 enzymes (Probable). Aba2 is responsible for the hydroxylation of carbon atom C-1' and aba4 might be involved in the oxidation of the C-4' carbon atom.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MLLSIKDLSEKYIMLLDVKDLSTLKTTVAVLVTVALIAQVLWKIFFHPLSAFPGPWFNRISEIPGSWVIATGKQHSYYRKLHEKYGPVVRVAPNELSFIGDRAWDDIYGVQKKGPNFEKSPIFIGAVSPLDGQTGISLAPNEAHTRQRRALAHVFSNTALLQQEEIMRSHVDKLVGQLKKTIAENRPINFSNWYTYTTFDMMGDLCFAEPFGCLDQGGATEWSTSVINVFKSAAWDQSIRRVAGVNTWLQKLMVKLLIPSKAANWRKVHFQNSREKTLRRLADGNREHKDFIYHILKNKEAKNSLSETEIILNMVLLISAGTETTASLLTGWTYFICTHPEVYKRLTDEIRGRFNSEQDITWETVKDLPYLHATLSEALRLYSPAPANQQRIVPPGGSVIDGHFVPGKTTVAVAPWAAINSSLNFKDPQKFIPERWLGDERFVNDKLNASQPFSLGPRGCIGKNLSFFEMRLITSRLLWNFDVSLVTTGEHGETNKLWDMDGAGKYMKVYQTWNKPDMWVMLKEVPR
Protein: Fat1 protein (Q80VA2)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
SVQSIQVNDGQWHAVSLEVEGNYAKLVLDEVHTASGTAPGALKTLNLDNYVFFGGHLRQQGTKHGRGAQVANGFRGCMDSIYLNGQELPLNNKPRAYAHIEEWVELSHGCLLTATEDCSSSPCQNGGVCNPSPTGGYYCKCSALYVGTFCEVSVNPCSSNPCLYGGTCMVDNGGFVCQCRGLYTGQRCQLSPYCKDDPCKNGGTCFDSLDGAVCQCDSGFRGERCQSDIDECAGNPCRNGALCENTHGSYHCNCSQEYRGKHCEDASPNHYVSTPWNIGLAEGIGIIVFIAGIVLLVMVFVLCRKMISRKKKRQAEPEDKRLGPTTAFLQRPYFDSKLNKNIYSDIPPQVPVRPISYTPSIPSDSRNNLDRNSFEGSAIPEHPEFSTFNPESMHGHRKAVAVCSVAPNLPPPPPSNSPSDSDSIQKPSWDFDYDAKVVDLDPCLSKKPLEEKPSQPYSARESLSEVQSLSSFQSESCDDNGYHWDTSDWMPSVPLPDIQEFPNYEAIDEHTPLYSADPNAIDTDYYPGGYDIESDFPPPPEDFPAPDELPPLPPEFSDQFESIHPPRDMPAAGSLGSSSRSRQRFNLNQYLPNFYPADMSEPQKQGAGENSPCREPYTPYPPGYQRNFEAPTIENMPMSVYASTASCSDVSACCEVESEVMMSDYESGDDGHFEEVTIPPLDSQQHTEV
Protein: Netrin-4 (Beta-netrin) (Hepar-derived netrin-like protein) (Q9HB63)
Organism: Homo sapiens (Human)
Function: May play an important role in neural, kidney and vascular development. Promotes neurite elongation from olfactory bulb explants.
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000269|PubMed:11038171}. Note=Major component.
Interaction partners:
- Neogenin
- Netrin receptor DCC
- Netrin receptor UNC5B
- Netrin receptor UNC5A
- Cell adhesion molecule DSCAM
- Netrin receptor UNC5C
Sequence:
MGSCARLLLLWGCTVVAAGLSGVAGVSSRCEKACNPRMGNLALGRKLWADTTCGQNATELYCFYSENTDLTCRQPKCDKCNAAYPHLAHLPSAMADSSFRFPRTWWQSAEDVHREKIQLDLEAEFYFTHLIVMFKSPRPAAMVLDRSQDFGKTWKPYKYFATNCSATFGLEDDVVKKGAICTSKYSSPFPCTGGEVIFKALSPPYDTENPYSAKVQEQLKITNLRVQLLKRQSCPCQRNDLNEEPQHFTHYAIYDFIVKGSCFCNGHADQCIPVHGFRPVKAPGTFHMVHGKCMCKHNTAGSHCQHCAPLYNDRPWEAADGKTGAPNECRTCKCNGHADTCHFDVNVWEASGNRSGGVCDDCQHNTEGQYCQRCKPGFYRDLRRPFSAPDACKPCSCHPVGSAVLPANSVTFCDPSNGDCPCKPGVAGRRCDRCMVGYWGFGDYGCRPCDCAGSCDPITGDCISSHTDIDWYHEVPDFRPVHNKSEPAWEWEDAQGFSALLHSGKCECKEQTLGNAKAFCGMKYSYVLKIKILSAHDKGTHVEVNVKIKKVLKSTKLKIFRGKRTLYPESWTDRGCTCPILNPGLEYLVAGHEDIRTGKLIVNMKSFVQHWKPSLGRKVMDILKRECK
Protein: DNA repair protein RecN (Recombination protein N) (P9WHI7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: May be involved in recombinational repair of damaged DNA.
Interaction partners:
- Uncharacterized protein
- Tetratrico peptide repeat group 5 domain-containing protein
- D-glycerol 3-phosphate phosphatase
- NAD kinase
- Protein RecA
- 16S/23S rRNA
- UvrABC system protein A
- UvrABC system protein B
- DNA repair protein RecO
- LexA repressor
Sequence:
MLTELRIESLGAISVATAEFDRGFTVLTGETGTGKTMVVTGLHLLGGARADATRVRSGADRAVVEGRFTTTDLDDATVAGLQAVLDSSGAERDEDGSVIALRSISRDGPSRAYLGGRGVPAKSLSGFTNELLTLHGQNDQLRLMRPDEQRGALDRFAAAGEAVQRYRKLRDAWLTARRDLVDRRNRARELAQEADRLKFALNEIDTVDPQPGEDVALVADIARLSELDTLREAATTARATLCGTPDADAFDRGAVDSLGRARAALQSSDDAALRGLAEQVGEALTVVVDAVAELGAYLDELPADASALDAKLARQAQLRTLTRKYAADIDGVLRWADEARARLAQLDVSEEGLAALERRTGELAHELGQAAVDLSTIRRKAAKRLAKEVSAELSALAMADAEFTIGVTTELADHGDPVALALASGELARAGADGVDAVEFGFVAHRGMTVLPLAKSASGGELSRVMLSLEVVLATSRKQAAGTTMVFDEIDAGVGGWAAVQIGRRLARLARTHQVIVVTHLPQVAAYADVHLMVQRTGRDGASGVRRLTSEDRVAELARMLAGLGDSDSGRAHARELLETAQNDELT
Protein: Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial (EC 1.3.5.1) (Flavoprotein subunit of complex II) (Fp) (Malate dehydrogenase [quinone] flavoprotein subunit) (EC 1.1.5.-) (P31039)
Organism: Bos taurus (Bovine)
Function: Flavoprotein (FP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q) (Probable). Can act as a tumor suppressor (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q0QF01}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q0QF01}; Matrix side {ECO:0000250|UniProtKB:Q0QF01}.
Interaction partners:
- NADH dehydrogenase flavoprotein 1, mitochondrial
- Fumarate hydratase, mitochondrial
- Succinate dehydrogenase cytochrome b small subunit, mitochondrial
- Succinate dehydrogenase cytochrome b560 subunit, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- NADH dehydrogenase iron-sulfur protein 2, mitochondrial
- Succinate dehydrogenase cytochrome b560 subunit, mitochondrial
- NADH dehydrogenase iron-sulfur protein 8, mitochondrial
- Succinate--CoA ligase subunit alpha, mitochondrial
- Succinate--CoA ligase subunit beta, mitochondrial
Sequence:
MSGVAAVSRLWRARRLALTCTKWSAAWQTGTRSFHFTVDGNKRSSAKVSDAISAQYPVVDHEFDAVVVGAGGAGLRAAFGLSEAGFNTACVTKLFPTRSHTVAAQGGINAALGNMEEDNWRWHFYDTVKGSDWLGDQDAIHYMTEQAPASVVELENYGMPFSRTEDGKIYQRAFGGQSLKFGKGGQAHRCCCVADRTGHSLLHTLYGRSLRYDTSYFVEYFALDLLMESGECRGVIALCIEDGSIHRIRARNTVIATGGYGRTYFSCTSAHTSTGDGTAMVTRAGLPCQDLEFVQFHPTGIYGAGCLITEGCRGEGGILINSQGERFMERYAPVAKDLASRDVVSRSMTLEIREGRGCGPEKDHVYLQLHHLPPAQLAMRLPGISETAMIFAGVDVTKEPIPVLPTVHYNMGGIPTNYKGQVLRHVNGQDQGVPGLYACGEAACASVHGANRLGANSLLDLVVFGRACALSIAESCRPGDKVPSIKPNAGEESVMNLDKLRFANGSIRTSELRLNMQKSMQSHAAVFRVGSVLQEGCEKISSLYGDLRHLKTFDRGMVWNTDLVETLELQNLMLCALQTIYGAEARKESRGGPRREDFKERVDEYDYSKPIQGQQKKPFEQHWRKHTLSYVDIKTGKVTLEYRPVIDRTLNETDCATVPPAIGSY
Protein: Large ribosomal subunit protein eL6 (60S ribosomal protein L6) (Neoplasm-related protein C140) (Tax-responsive enhancer element-binding protein 107) (TaxREB107) (Q02878)
Organism: Homo sapiens (Human)
Function: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:25957688}. Cytoplasm {ECO:0000305|PubMed:23636399, ECO:0000305|PubMed:25901680}. Rough endoplasmic reticulum {ECO:0000250|UniProtKB:Q2YGT9}. Note=Detected on cytosolic polysomes (PubMed:25957688). Detected in ribosomes that are associated with the rough endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:Q2YGT9, ECO:0000269|PubMed:25957688}.
Interaction partners:
- Small ribosomal subunit protein uS3
- Ubiquitin-ribosomal protein eS31 fusion protein
- Small ribosomal subunit protein eS1
- Small ribosomal subunit protein uS15
- Large ribosomal subunit protein uL10
- Large ribosomal subunit protein eL32
- Ubiquitin-like protein FUBI
- Large ribosomal subunit protein eL42
- Large ribosomal subunit protein eL27
- Large ribosomal subunit protein eL29
Sequence:
MAGEKVEKPDTKEKKPEAKKVDAGGKVKKGNLKAKKPKKGKPHCSRNPVLVRGIGRYSRSAMYSRKAMYKRKYSAAKSKVEKKKKEKVLATVTKPVGGDKNGGTRVVKLRKMPRYYPTEDVPRKLLSHGKKPFSQHVRKLRASITPGTILIILTGRHRGKRVVFLKQLASGLLLVTGPLVLNRVPLRRTHQKFVIATSTKIDISNVKIPKHLTDAYFKKKKLRKPRHQEGEIFDTEKEKYEITEQRKIDQKAVDSQILPKIKAIPQLQGYLRSVFALTNGIYPHKLVF
Protein: Valine--tRNA ligase (EC 6.1.1.9) (Valyl-tRNA synthetase) (Q960E6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPEAEQQNDANAPAGAGGDPPKTAKQLEKERLKAEKLAKLQAKLDKKAAAAPAAGEKREKPEKRTKEVKEAAVYTAQTAPGEKKDLSGALPDAYSPRYVEAQWYSWWEKEGFFTPEYGRASIDAPNPNGKFVMIIPPPNVTGSLHLGHALTNAIEDAITRYHRMKGRTTLWVPGCDHAGIATQVVVEKLLWRDEKLSRHDLGREKFIERIWDWRREKGGRIYEQLKSLGSSYDWTRVAFTMDPKLCRAVTEAFVRLHEEGSIYRSSRLVNWSCTLRSAISDIEVDKVEIPGRTFLSIPGYEDKVEFGVLIKFAYKVEGSDEEIIVATTRIETMLGDTAVAVHPQDDRYKHLHGKFVVHPFSTRRLPIVCDEFVDMAFGTGAVKITPAHDPNDYEVGKRCNLPFYTIFNDDGYIIGDYGEFTGMKRFECRKKILEKLKALNLYRETLNNPMVVPICSRSKDVVEPLIKPQWYVSCSDMAASATEAVRSGELKIIPEHHTKTWYHWMDGIRDWCVSRQLWWGHRIPAYHVSFTDPSLQTGSNDDEQYWIVARSEAEALTKAADRFGVDASKIVLKQDEDVLDTWFSSGIFPFSVFGWPDQTKDLQTFYPTSLLETGHDILFFWVARMVFFGQKLLGKLPFKEVYLHPMVRDAHGRKMSKSLGNVIDPMDVIRGITLEGLHAQLVGSNLDPREIEKAKAGQKQDYPQGIPECGSDALRFALCAYITQARDINLDINRVLGYRFFCNKLWNATKFALLYFTGSEKFDTELSASATINQMDAWILSRLAAAIEACNTGFESYDFAAATSACYAFWLYDLCDVYLECLKPIFQSGSEEQQTAARRTLYVCLDYGLRLLSPFMPFITEELYQRLPRANPAPSICVASYPSNTSWRSTKIESDVEFVQKAARIIRSARSDYNLPNKVKTEVYIVCTDSVPSEILKRYASDLATISYCSNVVFDSPAPQGCAILTVTGQCEVHLLLKGLVEADKEIAKLQKKSDQLVQTVGKLTQAIQAADYATKVPAEVQEANETKLSESRAEIERIAAAIETLKLM
Protein: Single-stranded DNA-binding protein DdrA (DNA damage response protein A) (Q9RX92)
Organism: Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1)
Function: ssDNA-binding protein that contributes to the ionizing radiation resistance of D.radiodurans. Plays a role in DNA repair and genome reconstitution, in a RecA-independent process, since DdrA is essential for recovery from severe genomic fragmentation as a result of exposure to severe levels of ionizing radiation in an environment lacking nutrients. In vitro, binds to the 3'-ends of single-stranded DNA, protecting them from nuclease degradation. Thus, DdrA is part of a DNA end-protection system that helps to preserve genome integrity following irradiation or desiccation. Does not display DNA strand annealing activity, unlike eukaryotic Rad52 protein homologs.
Interaction partners:
- Single-stranded DNA-binding protein DdrB
- Protein RecA
- DNA repair protein PprA
- DNA damage response protein D
- DNA damage response protein C
Sequence:
MKLSDVQKRLQAPFPAHTVSWKPAAFNAERTRALLLAHVDARAVQDRLDAVCPDDWSFEMEVVSGAEVPTVKGRLTVLGVTREDIGEAPEGSMAAYKAAASDAMKRCAVQFGIGRYLYDLPKQWADWDDARRGPKHLPELPEWARPDHERTPGGAHLVQAMEQLRYELPEDLDLQREVYKHLKAALGSIHPVPTGPVPTNPVQGGRAA
Protein: Alkyldihydroxyacetonephosphate synthase, peroxisomal (Alkyl-DHAP synthase) (EC 2.5.1.26) (Aging-associated gene 5 protein) (Alkylglycerone-phosphate synthase) (O00116)
Organism: Homo sapiens (Human)
Function: Catalyzes the exchange of the acyl chain in acyl-dihydroxyacetonephosphate (acyl-DHAP) for a long chain fatty alcohol, yielding the first ether linked intermediate, i.e. alkyl-dihydroxyacetonephosphate (alkyl-DHAP), in the pathway of ether lipid biosynthesis.
Subcellular location: Peroxisome membrane {ECO:0000250|UniProtKB:P97275}. Peroxisome {ECO:0000250|UniProtKB:P97275}.
Interaction partners:
- Dihydroxyacetone phosphate acyltransferase
- Peroxisomal targeting signal 1 receptor
- Peroxisomal targeting signal 2 receptor
- Peroxisomal membrane protein PEX14
- Peroxisome assembly protein 12
- Peroxisome biogenesis factor 10
- Peroxisomal membrane protein PEX13
- Peroxisomal leader peptide-processing protease
- Phytanoyl-CoA dioxygenase, peroxisomal
- Peroxisome biogenesis factor 2
Sequence:
MAEAAAAAGGTGLGAGASYGSAADRDRDPDPDRAGRRLRVLSGHLLGRPREALSTNECKARRAASAATAAPTATPAAQESGTIPKKRQEVMKWNGWGYNDSKFIFNKKGQIELTGKRYPLSGMGLPTFKEWIQNTLGVNVEHKTTSKASLNPSDTPPSVVNEDFLHDLKETNISYSQEADDRVFRAHGHCLHEIFLLREGMFERIPDIVLWPTCHDDVVKIVNLACKYNLCIIPIGGGTSVSYGLMCPADETRTIISLDTSQMNRILWVDENNLTAHVEAGITGQELERQLKESGYCTGHEPDSLEFSTVGGWVSTRASGMKKNIYGNIEDLVVHIKMVTPRGIIEKSCQGPRMSTGPDIHHFIMGSEGTLGVITEATIKIRPVPEYQKYGSVAFPNFEQGVACLREIAKQRCAPASIRLMDNKQFQFGHALKPQVSSIFTSFLDGLKKFYITKFKGFDPNQLSVATLLFEGDREKVLQHEKQVYDIAAKFGGLAAGEDNGQRGYLLTYVIAYIRDLALEYYVLGESFETSAPWDRVVDLCRNVKERITRECKEKGVQFAPFSTCRVTQTYDAGACIYFYFAFNYRGISDPLTVFEQTEAAAREEILANGGSLSHHHGVGKLRKQWLKESISDVGFGMLKSVKEYVDPNNIFGNRNLL
Protein: High affinity 3',5'-cyclic-AMP phosphodiesterase 7A (EC 3.1.4.53) (P2A) (cAMP-specific phosphodiesterase 7A) (P70453)
Organism: Mus musculus (Mouse)
Function: Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. May have a role in muscle signal transduction (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q13946}.
Interaction partners:
- RING finger protein 112
Sequence:
MGITLIWCLALVLIKWITSKRRGAISYDSSDQTALYIRMLGDVRVRSRAGFETERRGSHPYIDFRIFHSQSDIEASVSARNIRRLLSFQRYLRSSRVFRGATVCSSLDILDEDYNGQAKCMLEKVGNWNFDIFLFDRLTNGNSLVSLTFHLFSLHGLIEYFHLDMVKLRRFLVMIQEDYHSQNPYHNAVHAADVTQAMHCYLKEPKLASSVTPWDILLSLIAAATHDLDHPGVNQPFLIKTNHYLATLYKNSSVLENHHWRSAVGLLRESGLFSHLPLESRQEMEAQIGALILATDISRQNEYLSLFRSHLDKGDLHLDDGRHRHLVLQMALKCADICNPCRNWELSKQWSEKVTEEFFHQGDIEKKYHLGVSPLCDRQTESIANIQIGFMTYLVEPLFTEWARFSDTRLSQTMLGHVGLNKASWKGLQRQQPSSEDANAAFELNSQLLTQENRLS