wanglab/gogpt-training-data huggingface dataset:
Protein: ABC transporter domain-containing protein (S6EZS3)
Organism: Caenorhabditis elegans
Interaction partners:
- Multidrug resistance-associated protein lethal
- p-GlycoProtein related
- p-GlycoProtein related
Sequence:
MSSVLSSFSSARRSIRNIWQKDLNYFRSNHPFFILIFIVLSLAFYNVWWHNSPTRDQSGDASKFHLFDNFRLSKQKFVKMIVCIPETVVDYRFSTVIDAIHLTHLDYPHLEFTKKLEKAKNKLEDGEVDFLVLFKTLIETGKKIEYKIISEQGVFDKHCIQCDVHRKKTWGNAVEAQVVVNRFLYWLVKSRGFNKRSPHWQLSNVYVKHSGNDPMFLKRQSDLFLLWILLLPICSRLIDLWNNDRSSGYYNMFLSLHARRFHYFIAKFVFWYGIALIISLIVFIVNVLVVPAVFCSTYLQFVVCYAACIISFAIFLATTFPGSPLFAKIVGFLSMVAGEFGFGTVYHGIGFFQLCVRHFGKSEFDGPWIDAVCTLCMTGNCVLLITVSIYFDTYFCLFTMEPLAFYFPLEKDYWMPEARSPQLDTFFVKQIILLKPGRSEITVKKAHDEILPAKTSTGSKYIPPTPIVKGVPLVVLYGICKRIENHWRVKQVSLTVHLGEVVTLYGHHGCGSGEILSIIAGQMKPEYGEVMMEQSQRPLMISKTTDVPNVNYLNVIQYLRLISKMRGVSASTSHIDEMLEELDLIKVKNRSLDLLSTTQKERLRIAAVFVGQPDLVLIDFPTMECLPEWKFMVFRFIEKRKEKRSIIVSSYDPEETEAISDKVVLMSEGYVVLNGSCEAFKHSINSVFEIRIWPNNRFTDEQIKGMMKTLTLGDNQMKNDARFFETPNGKIRVTLPILYRRSIPLILRELDAVHEKFRIEFYELGKPNIHDIYANACYEHQQLDPLSTFDQLRDHYTKQQPLNKKTYFFKNMIHIFKDGRFLIETAAVVGLFLILTVIILLSYHSVESDSHQTREISLTSYESPITIYCDECEKEVIEGVTFEKKSRVLQLENNQAVLYWKDTAKADKELITVSRGDALFTMIVQNFAVSQMISKITGKHPQIKLFLESENVRTATEISGFSTVFNDISSSKAAMILTESYSLMYITAVFQMFVYTFSVVLPLRLVSTNMGPQSMILPWPRYVYFGFIYVFQLVVFLVIAIILGFAVLSMGFFATNTTSCYLRFLSAWFLSYASTLPLIYFLVFNIQNTKSVIPIILAISSLSVTFPNLVASFSAENQVSLQSLIQFVSWSCMLNPPSSLQVLAAFLNAGESLEKNSGTITSLILFCGAQFWIIVIFVLVIFQPGFSYIQQYWFKSSTVLYSSFERGTTLKPGARIKNSYIFVTNPLGTMEDAQDKGASGNIPNRPAAGTEPVQKPTSDYIAGSSMSIDDMSYITNYEENLVEKMATMTSWNDKQEVPVDNSATFLMGDQTKLKSALLTTIAKINKNEHIAFVPIVENISTIYTPFELLENAAYCNGFEITDDHISYLLDAFDLKEHANTQIKLLPCIDRRILMLLAKLVIKPNIVIIDQLEMFLPHSKMMTVWSFCARLRKNGLGIIYTSHHSGFAEHTATCCAHMYKGQFVRNLLPTSIKAKCTVLEVVPKTASDPKVLLHMLQKEMEESVKLPSTSRNITLAMYKDGVETIEKILELLRMLSPQIKRYSLRSGNCDEFLASAFGK
Protein: Long-chain-fatty-acid--CoA ligase 1 (EC 6.2.1.3) (Acyl-CoA synthetase 1) (ACS1) (Arachidonate--CoA ligase) (EC 6.2.1.15) (Long-chain acyl-CoA synthetase 1) (LACS 1) (Long-chain acyl-CoA synthetase 2) (LACS 2) (Long-chain fatty acid-CoA ligase 2) (Palmitoyl-CoA ligase 1) (Palmitoyl-CoA ligase 2) (Phytanate--CoA ligase) (EC 6.2.1.24) (P33121)
Organism: Homo sapiens (Human)
Function: Catalyzes the conversion of long-chain fatty acids to their active form acyl-CoAs for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses palmitoleate, oleate and linoleate. Preferentially activates arachidonate than epoxyeicosatrienoic acids (EETs) or hydroxyeicosatrienoic acids (HETEs) (By similarity).
Subcellular location: Mitochondrion outer membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Peroxisome membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Microsome membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:24269233}; Single-pass type III membrane protein {ECO:0000250}.
Interaction partners:
- Fatty acid synthase
- Carnitine O-palmitoyltransferase 1, liver isoform
- Beta-alanine-activating enzyme
- Lipoprotein lipase
- Long-chain fatty acid transport protein 2
- Monoglyceride lipase
- Long-chain specific acyl-CoA dehydrogenase, mitochondrial
- Long-chain fatty acid transport protein 6
- Fatty acid CoA ligase Acsl3
- Palmitoyl-protein thioesterase 1
Sequence:
MQAHELFRYFRMPELVDFRQYVRTLPTNTLMGFGAFAALTTFWYATRPKPLKPPCDLSMQSVEVAGSGGARRSALLDSDEPLVYFYDDVTTLYEGFQRGIQVSNNGPCLGSRKPDQPYEWLSYKQVAELSECIGSALIQKGFKTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFVDKPEKAKLLLEGVENKLIPGLKIIVVMDAYGSELVERGQRCGVEVTSMKAMEDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNPCPDDTLISFLPLAHMFERVVECVMLCHGAKIGFFQGDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRIFGQANTTLKRWLLDFASKRKEAELRSGIIRNNSLWDRLIFHKVQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGESLQAFLIAIVVPDVETLCSWAQKRGFEGSFEELCRNKDVKKAILEDMVRLGKDSGLKPFEQVKGITLHPELFSIDNGLLTPTMKAKRPELRNYFRSQIDDLYSTIKV
Protein: Actin-related protein (O96819)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MVCSTERAPVVILDGGSHHLRAGYASDGAPRLDIPALVGHPRNRGVAVAAGMNEYEIGDVALAKRGMLTVSSPIESGRVVSWENMEKLWGHVMYSELRVRPESHCFIVPQSVNTPASQKEKTLELMMETFHVHSLFLGASQVLSLYSYGLTTGLVIDSGKDRTMAVPVHEGYALGRHVAESDVAGEKLTEYFASLLRLEGNSFGTPMEMQVLNNAKEDICYVKPPIFNMTGPSAFFSPSEFPGECDYDLSLEGAPGEGFEDGREDHSSDERVFYLPDGNAIPISTHRSLTTEALFDFGILGSQYVPKSRYMTELGEIFQPSFPMGVSWLAFAAINNCQPVIRAQLYASIVLSGGNVSFPGTRERIETEVTQLYRETHTSEAVTPIAVNDIPCRVYSAWVGGSMLAGTSMFPHLAVSRQEYEEQGHRVVHCKCQ
Protein: Protein ten1 (P0C5Y7)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for telomere maintenance.
Subcellular location: Nucleus {ECO:0000269|PubMed:17715303}. Chromosome, telomere {ECO:0000269|PubMed:17715303}.
Interaction partners:
- Protein stn1
- Protection of telomeres protein tpz1
- Protection of telomeres protein poz1
- Coiled-coil quantitatively-enriched protein 1
- DNA-binding protein rap1
- Telomere length regulator taz1
- Telomerase reverse transcriptase
- Protection of telomeres protein 1
- Uncharacterized protein C16G5.19
- Putative amidase PB8B6.03
Sequence:
MDSAKLIFINQINDCKDGQKLRFLGCVQSYKNGILRLIDGSSSVTCDVTVVLPDVSIQKHEWLNIVGRKRQDGIVDVLLIRSAVGINLPRYRQMVSERQKCD
Protein: Large ribosomal subunit protein bL27m (39S ribosomal protein L27, mitochondrial) (L27mt) (MRP-L27) (Q9P0M9)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:11279069, ECO:0000269|PubMed:25278503, ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042}.
Interaction partners:
- Large ribosomal subunit protein uL22m
- Large ribosomal subunit protein uL16m
- Small ribosomal subunit protein uS5m
- Large ribosomal subunit protein bL20m
- Small ribosomal subunit protein uS7m
- Small ribosomal subunit protein uS15m
- Large ribosomal subunit protein bL9m
- Large ribosomal subunit protein bL19m
- Large ribosomal subunit protein mL62
- Large ribosomal subunit protein bL12m
Sequence:
MASVVLALRTRTAVTSLLSPTPATALAVRYASKKSGGSSKNLGGKSSGRRQGIKKMEGHYVHAGNIIATQRHFRWHPGAHVGVGKNKCLYALEEGIVRYTKEVYVPHPRNTEAVDLITRLPKGAVLYKTFVHVVPAKPEGTFKLVAML
Protein: UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase (EC 2.7.8.15) (GlcNAc-1-P transferase) (G1PT) (GPT) (N-acetylglucosamine-1-phosphate transferase) (Tunicamycin resistance protein 1) (P07286)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the initial step in the synthesis of dolichol-P-P-oligosaccharides.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P23338}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9H3H5}.
Interaction partners:
- UDP-N-acetylglucosamine transferase subunit ALG14
- UDP-N-acetylglucosamine transferase subunit ALG13
- Chitobiosyldiphosphodolichol beta-mannosyltransferase
- Dolichol-phosphate mannosyltransferase
- Dolichyl-phosphate beta-glucosyltransferase
- Dolichol kinase
- Dolichyldiphosphatase
- GDP-Man:Man
- Alpha-1,3/1,6-mannosyltransferase ALG2
- Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase
Sequence:
MLRLFSLALITCLIYYSKNQGPSALVAAVGFGIAGYLATDMLIPRVGKSFIKIGLFGKDLSKPGRPVLPETIGAIPAAVYLFVMFIYIPFIFYKYMVITTSGGGHRDVSVVEDNGMNSNIFPHDKLSEYLSAILCLESTVLLGIADDLFDLRWRHKFFLPAIAAIPLLMVYYVDFGVTHVLIPGFMERWLKKTSVDLGLWYYVYMASMAIFCPNSINILAGVNGLEVGQCIVLAILALLNDLLYFSMGPLATRDSHRFSAVLIIPFLGVSLALWKWNRWPATVFVGDTYCYFAGMVFAVVGILGHFSKTMLLLFIPQIVNFIYSCPQLFKLVPCPRHRLPKFNEKDGLMYPSRANLKEEPPKSIFKPILKLLYCLHLIDLEFDENNEIISTSNMTLINLTLVWFGPMREDKLCNTILKLQFCIGILALLGRHAIGAIIFGHDNLWTVR
Protein: ATPase ASNA1 homolog (EC 3.6.-.-) (Arsenical pump-driving ATPase homolog) (Arsenite-stimulated ATPase) (Q8T662)
Organism: Dictyostelium discoideum (Social amoeba)
Function: ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors, where the tail-anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane proteins. ATP hydrolysis is required for insertion. Subsequently, the homodimer reverts towards the open dimer state, lowering its affinity for the membrane-bound receptor, and returning it to the cytosol to initiate a new round of targeting.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03112}. Endoplasmic reticulum {ECO:0000255|HAMAP-Rule:MF_03112}.
Interaction partners:
- Golgi to ER traffic protein 4 homolog
- Low molecular weight phosphotyrosine protein phosphatase
- Putative transporter arsB
- UV excision repair protein RAD23 homolog
- t-SNARE family protein
- Vesicle-trafficking protein SEC22b
- Small glutamine-rich tetratricopeptide repeat-containing protein
- RING-type domain-containing protein
Sequence:
MADDEFEPTIENIINSEKLKWIFVGGKGGVGKTTTSCSVAIQLSKVKESVLLISTDPAHNLSDAFGQKFTKSPTLVEGFTNLFAMEIDPTPDQLAPEFMETQSDGFNLQEFTAAIPGIDEAMSFAEVMKLVKSLEFSVVVFDTAPTGHTLRLLSIPSLLDKGINKFLSMQQNFSGIFNAVSGMMGGNAPSLENMEGKIQSTKKVIEEINIQFKNPDLTTFIPVCIPEFLSVYETERLIQQLTKLDIDVHNVIVNQIVYPEKDCSLCNARQKMQKKYLDQIADLYFDFHVTKLPLLKAEVRGVPSLKLFSELLIKPYDPSTPLVLPNQEN
Protein: SWI/SNF related, matrix associated, actin dependent regulator of chromatin subfamily c member 2 (F8VXC8)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAVRKKDGGPNVKYYEAADTVTQFDNVRLWLGKNYKKYIQAEPPTNKSLSSLVVQLLQFQEEVFGKHVSNAPLTKLPIKCFLDFKAGGSLCHILAAAYKFKSDQGWRRYDFQNPSRMDRNVEMFMTIEKSLVQNNCLSRPNIFLCPEIEPKLLGKLKDIIKRHQGTVTEDKNNASHVVYPVPGNLEEEEWVRPVMKRDKQVLLHWGYYPDSYDTWIPASEIEASVEDAPTPEKPRKVHAKWILDTDTFNEWMNEEDYEVNDDKNPVSRRKKISAKTLTDEVNSPDSDRRDKKGGNYKKRKRSPSPSPTPEAKKKNAKKGPSTPYTKSKRGHREEEQEDLTKDMDEPSPVPNVEEVTLPKTVNTKKDSESAPVKGGTMTDLDEQEDESMETTGKDEDENSTGNKGEQTKNPDLHEDNVTEQTHHIIIPSYAAWFDYNSVHAIERRALPEFFNGKNKSKTPEIYLAYRNFMIDTYRLNPQEYLTSTACRRNLAGDVCAIMRVHAFLEQWGLINYQVDAESRPTPMGPPPTSHFHVLADTPSGLVPLQPKTPQGRQVDADTKAGRKGKELDDLVPETAKGKPELQTSASQQMLNFPDKGKEKPTDMQNFGLRTDMYTKKNVPSKSKAAASATREWTEQETLLLLEALEMYKDDWNKVSEHVGSRTQDECILHFLRLPIEDPYLEDSEASLGPLAYQPIPFSQSGNPVMSTVAFLASVVDPRVASAAAKSALEEFSKMKEEVPTALVEAHVRKVEEAAKVTGKADPAFGLESSGIAGTTSDEPERIEESGNDEARVEGQATDEKKEPKEPREGGGAIEEEAKEKTSEAPKKDEEKGKEGDSEKESEKSDGDPIVDPEKEKEPKEGQEEVLKEVVESEGERKTKVERDIGEGNLSTAAAAALAAAAVKAKHLAAVEERKIKSLVALLVETQMKKLEIKLRHFEELETIMDREREALEYQRQQLLADRQAFHMEQLKYAEMRARQQHFQQMHQQQQQPPPALPPGSQPIPPTGAAGPPAVHGLAVAPASVVPAPAGSGAPPGSLGPSEQIGQAGSTAGPQQQQPAGAPQPGAVPPGVPPPGPHGPSPFPNQQTPPSMMPGAVPGSGHPGVAGNAPLGLPFGMPPPPPPPAPSIIPFGSLADSISINLPAPPNLHGHHHHLPFAPGTLPPPNLPVSMANPLHPNLPATTTMPSSLPLGPGLGSAAAQSPAIVAAVQGNLLPSASPLPDPGTPLPPDPTAPSPGTVTPVPPPQ
Protein: Retinoic acid receptor alpha-B (RAR-alpha-B) (Nuclear receptor subfamily 1 group B member 1-B) (Retinoic acid receptor alpha-2.B) (RAR-alpha-2.B) (Q7ZTI3)
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 development and, in lateral plate mesoderm, for specification of the pectoral fins.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
Interaction partners:
- Retinoic acid receptor RXR-beta-A
- Arginyl-tRNA synthetase
- Retinoic acid receptor RXR-gamma-B
- Nuclear receptor corepressor 2
- Cellular retinoic acid binding protein type II
- Cytochrome P450 26A1
Sequence:
MYESVDVVGLTPSPNPFLSMDYYHQNRGCLIPDKGLVSGAARGFRNPHWSGSNHSVETQSTSSEEIVPSPPSPPPPPRVYKPCFVCQDKSSGYHYGVSACEGCKGFFRRSIQKNMVYTCHREKSCIINKVTRNRCQYCRLQKCLEVGMSKESVRNDRNKRKKDDKKQECLENYVLSPDTEKMIEQVRKAHQETFPSLCQLGKYTTNNSADHRVALDVDLWDKFSELSTKCIIKTVEFAKQLPGFTTLTIADQITLLKAACLDILILRICTRYTPDQDTMTFSDGLTLNRTQMHNAGFGPLTDLVFAFANQLLPLEMDDAETGLLSAICLLCGDRQDLEQSDKVDELQEPLLEALKIYVRNRRPHKPHMFPKMLMKITDLRSISAKGAERVITLKMEIPGSMPPLIQEMLENSEGLEGGGSKGAGGGGGGGGGKGAPPGSCSPSLSPSSAHSSPSAHSP
Protein: EIN3-binding F-box protein 2 (Q708Y0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of SCF(EBF1) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins (probably including EIN3 and EIL1). Regulator of the ethylene signaling cascade by modulating the stability of EIN3 and EIL1 proteins.
Subcellular location: Nucleus {ECO:0000269|PubMed:14675533}.
Interaction partners:
- Protein ETHYLENE INSENSITIVE 3
- ETHYLENE INSENSITIVE 3-like 1 protein
- EIN3-binding F-box protein 1
- ETHYLENE INSENSITIVE 3-like 3 protein
- Ethylene-insensitive protein 2
- ETHYLENE INSENSITIVE 3-like 2 protein
- Serine/threonine-protein kinase CTR1
- ETHYLENE INSENSITIVE 3-like 5 protein
- Putative ETHYLENE INSENSITIVE 3-like 4 protein
- Ethylene response sensor 1
Sequence:
MSGIFRFSGDEDCLLGGSMYLSPGSCPGVYYPARKRLRVAATSFYSGFEEKQTSIDVLPEECLFEILRRLPSGQERSACACVSKHWLNLLSSISRSEVNESSVQDVEEGEGFLSRSLEGKKATDLRLAAIAVGTSSRGGLGKLQIRGSGFESKVTDVGLGAVAHGCPSLRIVSLWNLPAVSDLGLSEIARSCPMIEKLDLSRCPGITDSGLVAIAENCVNLSDLTIDSCSGVGNEGLRAIARRCVNLRSISIRSCPRIGDQGVAFLLAQAGSYLTKVKLQMLNVSGLSLAVIGHYGAAVTDLVLHGLQGVNEKGFWVMGNAKGLKKLKSLSVMSCRGMTDVGLEAVGNGCPDLKHVSLNKCLLVSGKGLVALAKSALSLESLKLEECHRINQFGLMGFLMNCGSKLKAFSLANCLGISDFNSESSLPSPSCSSLRSLSIRCCPGFGDASLAFLGKFCHQLQDVELCGLNGVTDAGVRELLQSNNVGLVKVNLSECINVSDNTVSAISVCHGRTLESLNLDGCKNITNASLVAVAKNCYSVNDLDISNTLVSDHGIKALASSPNHLNLQVLSIGGCSSITDKSKACIQKLGRTLLGLNIQRCGRISSSTVDTLLENLWRCDILY
Protein: Inscuteable (Q24367)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSFQRSYSKVWWGSEQSSLTSGGFYSSFSGGSSTSSTSNYPQRQPASLGPLGNLSCIQEVEDEQNSSKLSWHKHDSPGSLRSQDSGFSDNEESHQLQHQQNLSPPSPQSDKQQTPAATPTSVHSVATPPTVVRRVGNSSFYSPLISVTRRISFTSGQITPKTRSGDEDAEDAELEASRSRLFEQLDSMKLDDGEAEAEEDSPPRPAIRRRRRLMRKPMPEPEAASASEEEEVVIAPPPPPPYNNETVYLGEAPPPYNNETVTFGATEQDESLQQQPSPLRVRSLRFTASTSTPKSGSKIAKRGKKHPEPVASWMSEQRWAGEPEVMCTLQHKSIAQEAYKNYTITTSAVCKLVRQLQQQALSLQVHFERSERVLSGLQASSLPEALAGATQLLSHLDDFTATLERRGVFFNDAKIERRRYEQHLEQIRTVSKDTRYSLERQHYINLESLLDDVQLLKRHTLITLRLIFERLVRVLVISIEQSQCDLLLRANINMVATLMNIDYDGFRSLSDAFVQNEAVRTLLVVVLDHKQSSVRALALRALATLCCAPQAINQLGSCGGIEIVRDILQVESAGERGAIERREAVSLLAQITAAWHGSEHRVPGLRDCAESLVAGLAALLQPECCTQTLLLCAAALNNLSRMEATSHYSIMSNEAIFRLIDTLEHQTCGTSVFLYEQIVGMLHNMSLNKKCHSHLANGVIINFITSVYQTEFYQTYGSRAESDAQRRTIKTILHTLTRLASDSPTLGAELLEQWHLPDLLRQSLALKPANSQQQQHLDSSYGGDISQLARQLLRAHGQEQQLLEATPAPGGSFSSGHQTPEAQTQTNSSGMSSSGSKTKAKSSASRLLKFNLTRQESFV
Protein: ATP synthase F(0) complex subunit C3, mitochondrial (ATP synthase lipid-binding protein) (ATP synthase membrane subunit c locus 3) (ATP synthase proteolipid P3) (ATPase protein 9) (ATPase subunit c) (P56384)
Organism: Mus musculus (Mouse)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. A homomeric c-ring of probably 10 subunits is part of the complex rotary element.
Subcellular location: Mitochondrion membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- ATP synthase peripheral stalk subunit b, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit d, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit F6, mitochondrial
- ATP synthase F
Sequence:
MFACAKLARTPALIRAGSRVAYRPISASVLSRPETRTGEGSTVFNGAQNGVCQLIRREFQTSVISRDIDTAAKFIGAGAATVGVAGSGAGIGTVFGSLIIGYARNPSLKQQLFSYAILGFALSEAMGLFCLMVAFLILFAM
Protein: Glutamine synthetase (GS) (EC 6.3.1.2) (Glutamate--ammonia ligase) (Glutamine synthetase I beta) (GSI beta) (P77961)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Function: Involved in nitrogen metabolism via ammonium assimilation. Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P9WN39}.
Interaction partners:
- Ferredoxin-dependent glutamate synthase 2
- Ferredoxin-dependent glutamate synthase 1
- Ferredoxin--nitrite reductase
- NADP-specific glutamate dehydrogenase
- NADH-glutamate synthase small subunit
- Glutamate--ammonia ligase
- Glutamine--fructose-6-phosphate aminotransferase
- Carbamoyl phosphate synthase small chain
- L-glutamate gamma-semialdehyde dehydrogenase
- Glutamate decarboxylase
Sequence:
MARTPQEVLKWIQDENIKIIDLKFIDTPGIWQHCSFYYDQLDENSFTEGIPFDGSSIRGWKAINESDMCMVPDPNTATIDPFCKEPTLSMICSIKEPRTGEWYNRDPRTIAAKAVEYLRGTGIADTVYFGPEAEFFLFDDIRFGQTENSSYYFADSVEGRWNTGREEEGGNLGYKPGYKQGYFPVAPTDTAQDIRTEMLLTMAGLCVPIEKHHHEVASGGQNELGIKFDKLVNSADNLMIYKYVIKNVAKKYGKTVTFMPKPIFNDNGSGMHVHQSLWKDGQPLFAGDKYAGFSQMGLWYIGGILKHAPALLAFTNPTTNSYKRLVPGFEAPVNLAYSQGNRSASVRIPLSGGNPKAKRLEFRCPDATSNPYLAFAAMLCAGIDGIKNQIDPGEPLDVDIYDLSPEELAKIPSTPGSLEAALEALEKDHEFLTGTGVFSPDFVESWIEYKLDNEVNPMRLRPHPYEFSLYYDC
Protein: Brain-specific homeobox protein homolog (Q3C1V8)
Organism: Homo sapiens (Human)
Function: DNA binding protein that function as transcriptional activator. Is essential for normal postnatal growth and nursing. Is an essential factor for neuronal neuropeptide Y and agouti-related peptide function and locomotory behavior in the control of energy balance (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q810B3}.
Interaction partners:
- Agouti-related protein
- Pro-neuropeptide Y
Sequence:
MNLNFTSPLHPASSQRPTSFFIEDILLHKPKPLREVAPDHFASSLASRVPLLDYGYPLMPTPTLLAPHAHHPLHKGDHHHPYFLTTSGMPVPALFPHPQHAELPGKHCRRRKARTVFSDSQLSGLEKRFEIQRYLSTPERVELATALSLSETQVKTWFQNRRMKHKKQLRKSQDEPKAPDGPESPEGSPRGSEAATAAEARLSLPAGPFVLTEPEDEVDIGDEGELGSGPHVL
Protein: Thiosulfate transporter TsuA (Thiosulfate uptake protein A) (P33015)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Putative sulfur carrier protein TsuB
- L-cystine transporter TcyP
- Sulfate adenylyltransferase subunit 1
- Thiosulfate-binding protein
- Sulfate adenylyltransferase subunit 2
- Putative sulfur carrier protein YedF
- Sulfite reductase flavoprotein alpha-component
- Sulfate/thiosulfate import ATP-binding protein CysA
- Adenylyl-sulfate kinase
- Sulfite reductase hemoprotein beta-component
Sequence:
MFSMILSGLICGALLGFVMQRGRFCLTGGFRDMYIVKNNRMFYALLIAISVQSVGVFALIQAGLLTYEAGAFPWLGTVIGGYIFGLGIVLAGGCATGTWYRAGEGLIGSWIALFTYMVMSAVMRSPHASGLNQTLQHYSTEHNSIAETFNLSVWPLVAVLLVITLWVVMKELKKPKLKVATLPPRRTGIAHILFEKRWHPFVTAVLIGLIALLAWPLSEATGRMFGLGITSPTANILQFLVAGDMKYINWGVFLVLGIFVGSFIAAKASREFRVRAADAQTTLRSGLGGVLMGFGASIAGGCSIGNGLVMTAMMTWQGWIGLVFMILGVWTASWLVYVRPQRKARLATAAAN
Protein: Tribbles homolog 3 (TRB-3) (Neuronal cell death-inducible putative kinase) (Q8K4K2)
Organism: Mus musculus (Mouse)
Function: Inactive protein kinase which acts as a regulator of the integrated stress response (ISR), a process for adaptation to various stress. Inhibits the transcriptional activity of DDIT3/CHOP and is involved in DDIT3/CHOP-dependent cell death during ER stress (By similarity). May play a role in programmed neuronal cell death but does not appear to affect non-neuronal cells (By similarity). Acts as a negative feedback regulator of the ATF4-dependent transcription during the ISR: while TRIB3 expression is promoted by ATF4, TRIB3 protein interacts with ATF4 and inhibits ATF4 transcription activity. Disrupts insulin signaling by binding directly to Akt kinases and blocking their activation. May bind directly to and mask the 'Thr-308' phosphorylation site in AKT1. Interacts with the NF-kappa-B transactivator p65 RELA and inhibits its phosphorylation and thus its transcriptional activation activity (By similarity). Interacts with MAPK kinases and regulates activation of MAP kinases (By similarity). Can inhibit APOBEC3A editing of nuclear DNA.
Subcellular location: Nucleus {ECO:0000269|PubMed:12749859, ECO:0000269|PubMed:22977230}.
Interaction partners:
- RAC-alpha serine/threonine-protein kinase
- Glutathione-specific gamma-glutamylcyclotransferase 1
- Cyclic AMP-dependent transcription factor ATF-4
- RAC-beta serine/threonine-protein kinase
- Peroxisome proliferator-activated receptor alpha
- RAC-gamma serine/threonine-protein kinase
- DNA damage-inducible transcript 3 protein
- E3 ubiquitin-protein ligase COP1
- Asparagine synthetase
- RIB43A-like with coiled-coils protein 2
Sequence:
MRATPLAASADVSCRKKPLEFDDNIDAKCPVLKRVRDEPEPGPLPSLLPPSPPPASDLSPAVAPATRLGPYILLEREQGSCSYRALHCPTGTEYTCKVYPASEAQAVLAPYARLPTHQHVARPTEVLLGSRLLYIFFTKTHGDLHSLVRSRRGIPESEAAGLFRQMASAVAHCHKHGLVLRDLKLRRFVFSNCERTKLVLENLEDACVMTGSDDSLWDKHACPAYVGPEILSSRPSYSGKAADVWSLGVALFTMLAGRYPFHDSEPVLLFGKIRRGTFALPEGLSAPARCLIRCLLRKEPSERLVALGILLHPWLREDHGRVSPPQSDRREMDQVVPDGPQLEEAEEGEVGLYG
Protein: Rap guanine nucleotide exchange factor (GEF) 1 (Rapgef1 protein) (A1L338)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MSSGLGLRRSPEMSGKIEKADSQRSHLSSFTMKLMDKFHSPKIKRTPSKKGKPAEVSKIPEKPVSKNLCWLEEKEKEVVSALRYFKTIVDKMAIDKKVLEMLPGSASKVLEAILPLVQTDPRIQHSSALSSCYSRVYQSLANLIRWSDQVMLEGVNSEDKEMVTTVKGVIKAVLDGVKELVRLTIEKQGRPSPTSPVKPSSPASKPDGQPELPLTDREMEILNKTTSVSPSAELLPDSTSEEVAPPKPPLPGIRVVDNSPPALPPKKRQSAPSPTRVAVVAPMSRATSGSSLPVGINRQDFDVECYTQRRLSGGSRSCGGESPRLSPCSSTGKLSRSDEQLSSLDRDSGQCSRNTSCETLDHYDPDYEFLQQDLSNADQIPPQAACNLSPLPESLGESGPPFLGHPFQLPLGSCLQQEGQQTDTPPALPEKKRRSAVSQTTDSSGCRVSYERHPSQYDNISEGDLQNPVPVQPVPYPPFAAVLPFQQGASSASAEFVGDFSVPELAGDTEKPPPLPEKKNKHMLAYMQLLEDYSEPQPSMFYQTPQSEHIYQQKNKMLMEVYGFSESFCGSDSTQELAPPPALPPKQRQLASYAASSFSVSYCVQQTKVAFTPEDGSAAQGLSVSVSNSFLNRHGSLPVPSYKSVFRSYSQDFMPHHQASVQPFLPPTSSSSPHFPPVHTSQSSDLAVPTVSSPPPSTVDGPLSSSQDSSFHGNPVRLPSETSFTDSEPPSGKDGHPRDPSVSSASGKDSRENGERSPKSLDGLESAQSEEEVDELSLIDHNEIMARLTLKQEGDDGPDVRGGSGDILLVHATETDRKDLVLYCEAFLTTYRTFISPEELIKKLQYRYEKFSPFADTFKKRVSKNTFFVLVRVVDELCLVELTEEILKLLMELVFRLVCSGELSLARVLRKNILDKVDQKKLLRCAHSDQPLAARGVAARPGTLHDFHSHEIAEQLTLLDAELFYKIEIPEVLLWAKEQNEEKSPNLTQFTEHFNNMSYWVRSIIMLQEKAQDRERLLLKFIKIMKHLRKLNNFNSYLAILSALDSAPIRRLEWQRQTSEGLAEYCTLIDSSSSFRAYRAALSEVEPPCIPYLGLILQDLTFVHLGNPDYIDGKVNFSKRWQQFNILDSMRCFQQAHYEIRRNDDIINFFNDFSDHLAEEALWELSLKIKPRNITRRKTDREEKT
Protein: Signal transducer and activator of transcription (R9QE65)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU046415}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU046415}.
Interaction partners:
Sequence:
MAQWEMLQNLDSPFQDQLHQLYSHSLLPVDIRQYLAVWIEDQNWQEAALGSDDSKATMLFFHFLDQLNYECGRCSQDPESLLLQHNLRKFCRDIQPFSQDPTQLAEMIFNLLLEEKRILIQAQRAQLEQGEPVLETPVESQQHEIESRILDLRAMMEKLVKSISQLKDQQDVFCFRYKIQAKGKTPSLDPHQTKEQKILQETLNELDKRRKEVLDASKALLGRLTTLIELLLPKLEEWKAQQQKACIRAPIDHGLEQLETWFTAGAKLLFHLRQLLKELKGLSCLVSYQDDPLTKGVDLRNAQVTELLQRLLHRAFVVETQPCMPQTPHRPLILKTGSKFTVRTRLLVRLQEGNESLTVEVSIDRNPPQLQGFRKFNILTSNQKTLTPEKGQSQGLIWDFGYLTLVEQRSGGSGKGSNKGPLGVTEELHIISFTVKYTYQGLKQELKTDTLPVVIISNMNQLSIAWASVLWFNLLSPNLQNQQFFSNPPKAPWSLLGPALSWQFSSYVGRGLNSDQLSMLRNKLFGQNCRTEDPLLSWADFTKRESPPGKLPFWTWLDKILELVHDHLKDLWNDGRIMGFVSRSQERRLLKKTMSGTFLLRFSESSEGGITCSWVEHQDDDKVLIYSVQPYTKEVLQSLPLTEIIRHYQLLTEENIPENPLRFLYPRIPRDEAFGCYYQEKVNLQERRKYLKHRLIVVSNRQVDELQQPLELKPEPELESLELELGLVPEPELSLDLEPLLKAGLDLGPELESVLESTLEPVIEPTLCMVSQTVPEPDQGPVSQPVPEPDLPCDLRHLNTEPMEIFRNCVKIEEIMPNGDPLLAGQNTVDEVYVSRPSHFYTDGPLMPSDF