wanglab/gogpt-training-data huggingface dataset:
Protein: Elongation factor 1-beta 1 (EF-1-beta 1) (Elongation factor 1-beta' 1) (EF-1-beta' 1) (Elongation factor 1B-alpha 1) (eEF-1B alpha 1) (Q84WM9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: EF-1-beta and EF-1-delta stimulate the exchange of GDP bound to EF-1-alpha to GTP.
Subcellular location: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Probable elongation factor 1-gamma 2
- Probable elongation factor 1-gamma 1
- Elongation factor 1-alpha 1
- Translationally-controlled tumor protein 1
- Translationally controlled tumor protein 2
- Elongation factor 1-delta 2
- Glutathione S-transferase Z2
- 60S acidic ribosomal protein family
- Large ribosomal subunit protein uL11x
- mRNA cap guanine-N
Sequence:
MAVTFSDLHTERGLKTLEEHLAGKTYISGDQLSVDDVKVYAAVLENPGDGFPNASKWYDSVASHLAKSFPGKADGVRVGGGVAPPSEAHPHTEEPAADGDGDDDDDIDLFADETEDEKKAAEEREAAKKDTKKTKESGKSSVLLEVKPWDDETDMKKLEEAVRSVQMPGLTWGASKLVPVGYGIKKLTIMMTIVDDLVSVDNLIEDHLTSEPNNEYIQSVDIVAFNKI
Protein: homocitrate synthase (EC 2.3.3.14) (Q59TC4)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Aconitate hydratase, mitochondrial
- Acetyltransferase component of pyruvate dehydrogenase complex
- 2-isopropylmalate synthase
- Acetyl-CoA acetyltransferase
- Acetyl-coenzyme A synthetase 2
- Acetyl-coenzyme A synthetase
- Malate synthase
- 2-isopropylmalate synthase
- Acetyl-CoA hydrolase
- homocitrate synthase
Sequence:
MSVASNPYGPNPSDFLSNVNKFEVIESTLREGEQFANAFFTTEKKIEIAKALDDFGVDYIELTSPVASEQSRRDCEAICKLGLKAKILTHIRCHMDDARVAVETGVDGVDVVIGTSQFLRQYSHGKDMNYIAQSAIEVIEFVKSKGIEIRFSSEDSFRSDIVDLLNIYRTVDKIGVNRVGIADTVGCANPRQVYELVKTLKSVVSCDIECHFHNDTGCAIANAYTALEAGAKLIDVSVLGIGERNGITPLGALMARMITADRDYVLSKYKLHKLRDLENLVADAVQINIPFNNPITGFCAFTHKAGIHAKAILANPSTYEILNPNDFGLTRYIHFANRLTGWNAIKSRVDQLNLHLTDDQVKEVTNKIKKLGDVRQLNIDDVDSIIKDFHAEQSTTNTPLLKPVEDDEGPEIKKQKV
Protein: Inositol polyphosphate 1-phosphatase (O76455)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSGVEEQASLLRVLINCAEKAANIARICRSNEQLLALLVQEKIGSEANERFEHDFKTLADVLIQETIKHEVGALFPAMKDAILGEESANFTNQLGESVTIAVGATEEDTAASLQAVLSGHEDAASALATEVHRDVSFSSEKLGEIAQLPDELDYGNLGIWIDPIDATAEYISGDTMFTDFPGITSTGLDCVTVLIGVYERDTGVPVMGVVAQPFGEKLEENVYSSSMFWGVCLPTVRAHNCDFEARDENRRLGIFSSSEQSDILQRFLDLGYEFAFSAGAGHKALKVITHEVDVYLLSKGSTFKWDTCAPQAILRALGGDVLDYAASVADQKAVPLKYLIEDAEADADWKRNAGGIISVRNVDVVDELLAKLAEQ
Protein: Alanine--glyoxylate aminotransferase (AGT) (EC 2.6.1.44) (Q9W3Z3)
Organism: Drosophila melanogaster (Fruit fly)
Function: Catalyzes the pyridoxal 5'-phosphate-dependent transamination of alanine with glyoxylate as an amino group acceptor. Can also catalyze, although with much less efficiency, the transamination of amino-butyrate, phenylalanine and serine with glyoxylate or pyruvate as an amino group acceptor. Does not catalyze the transamination of both 3-hydroxykynurenine and L-kynurenine. May play a role in the detoxification of glyoxylate, a toxic plant metabolite from the fly diet (Probable).
Subcellular location: Peroxisome {ECO:0000250|UniProtKB:P21549}.
Interaction partners:
- Alanine--glyoxylate aminotransferase 2, mitochondrial
- (S)-2-hydroxy-acid oxidase
- Aminomethyltransferase
- alanine transaminase
- Serine hydroxymethyltransferase
- D-amino acid oxidase 2, isoform A
- LD34157p
- Glycine cleavage system P protein
- Phosphoserine phosphatase
- Sarcosine dehydrogenase
Sequence:
MEVPPPLVLKRPLYVPSKTLMGPGPSNCSHRVLEAMSNPVLGHMHPECLQIMDEVKEGIKYIFQTLNDATMCISGAGHSGMEAALCNLIEDGDVVLMGITGVWGHRAGDMARRYGAEVHYVEASFGRALSHEEITFAFEAHRPKVFFIAQGDSSTGIIQQNIRELGELCRKYDCFLIVDTVASLGGTEFLMDEWKVDVAYTGSQKSLGGPAGLTPISFSKRALTRIRKRKTKPKVYYFDILLIGQYWGCYGTPRIYHHTISSTLLYGLREALAHFCAVGLKAVVRRHQECSKRLQLGIEELGLEMFVSREEERLPTVNTIKVPFGVDWKKVAEYAMRKYSVEISGGLGPTVEHVFRIGLMGENATVERVDMVLSILNEAIQSSKLGIKTDLSKI
Protein: Glutathione-specific gamma-glutamylcyclotransferase 2 (Gamma-GCG 2) (EC 4.3.2.7) (Cation transport regulator-like protein 2) (Q8WUX2)
Organism: Homo sapiens (Human)
Function: Catalyzes the cleavage of glutathione into 5-oxo-L-proline and a Cys-Gly dipeptide. Acts specifically on glutathione, but not on other gamma-glutamyl peptides.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:27913623}.
Interaction partners:
- Gamma-glutamylcyclotransferase
- 5-oxoprolinase
- Glutathione synthetase
- Phospholipid hydroperoxide glutathione peroxidase GPX4
- Glutathione hydrolase 1 proenzyme
- Glutathione hydrolase 7
- Glutathione hydrolase 5 proenzyme
- Glutathione-specific gamma-glutamylcyclotransferase 1
- Glutathione hydrolase 6
- Cytosol aminopeptidase
Sequence:
MWVFGYGSLIWKVDFPYQDKLVGYITNYSRRFWQGSTDHRGVPGKPGRVVTLVEDPAGCVWGVAYRLPVGKEEEVKAYLDFREKGGYRTTTVIFYPKDPTTKPFSVLLYIGTCDNPDYLGPAPLEDIAEQIFNAAGPSGRNTEYLFELANSIRNLVPEEADEHLFALEKLVKERLEGKQNLNCI
Protein: UvrABC system protein A (UvrA protein) (Excinuclease ABC subunit A) (Q5F7H1)
Organism: Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|HAMAP-Rule:MF_00205}.
Interaction partners:
- UvrABC system protein B
- UvrABC system protein C
- Transcription-repair-coupling factor
- Protein RecA
- Formamidopyrimidine-DNA glycosylase
Sequence:
MCNHHPRHSHDNDTIRIRGARTHNLKNIDLDIPRHKLVVVTGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQFLQMMDKPDVDLIEGLSPAISIEQKSTSHNPRSTVGTVTEIHDYLRLLYARVGTPYCPEHKLPLSSQTVSQMVDAVLKLPEDTRVMILGPAVRERKGEFVDFFADLQAQGFARVRVDGEVYQLDEVPKLEKNIKHNIDVVIDRVKVKADIKQRLAESFETALRHGNERALAMEMDSGEEHWFSARFACPVCSYSLPELEPRLFSFNNPMGSCPTCDGLGNTNFFDPEKVVAHPELSLATGAIDGWDKRNQFYFQMIQSLAHHYKFDVNVAWETLPEKVKKVVLHGSGKEVIDFTYLSERGTTFNRSHAFEGIIPNLERRYRETDSETVREKLREYQNHRACPSCGGARLRKEARYVYVGGEPLHEVSAWPLTKTHRFFETLDLDGNKKQIAEKILKEITERLGFLINVGLDYLNLSRSAETLSGGEAQRIRLASQIGSGLTGVMYVLDEPSIGLHQRDNDRLLATLKRLRDLGNSVIVVEHDEDAIREADFVVDMGPGAGEHGGNVLIADTPENVAKCEKSVTGQYLGGKKSIAVPSERTPVNPGRMLVLKGARGNNLKNVTLELPLGLITCITGVSGSGKSTLINDTLAKITARELNRAQEEPAPYDDIRGLEHLDKVINVDQSPIGRTPRSNPATYTGLFTPIRELFAGVPLSRERGYNVGRFSFNVKGGRCEACQGDGVIKVEMHFLPDVYVPCEVCHGKRYNRETLEIQYKGKNISQVLDMTVEEAREFFDAVPTVSRKLQTLMDVGLGYIRLGQSATTLSGGEAQRVKLALELSKRDTGRTLYILDEPTTGLHFADIALLLEVIGRLKGKGNSIVIIEHNLDVIKTADWIVDLGPEGGDGGGKVIAKGSPEEVAKVKGSYTGKYLKVVLK
Protein: Uncharacterized protein C6G9.15c (Q92360)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Ell1-associated factor 1
- RNA polymerase II elongation factor ell1
- FACT complex subunit pob3
- CTD kinase subunit gamma
- Transcription elongation factor spt5
- FACT complex subunit spt16
- Transcription elongation factor spt4
- Curved DNA-binding protein
- Nucleoporin nup184
- Tetratricopeptide repeat protein 1
Sequence:
MSNDSSDNQIRRRHHPVLPKGSFQKKDDSIVLEQELSTPKQVNQARPKFPSPITPTLPEMHLPVGNSKFQAVLPSLISPTLPPGFGMASDDSEASLAENDLHPLDNDSTRTSKTLKNSSEVLTASKLTDEGNSKPLLEEGEVAVSSPILLDSKDVIMGVTKSSKNLVEDAHKSKKASTNSSINNMVSTVNSENSNVNNGSSLNGNTSSNLKRKANVTLGDYKRLKVKNKNPSSQELITADVDKTSGSLSEKSEVNHASLKKTYMRLLNSGKMQKKECDKKGKFFEAYAVDAVLCYTVAFHLQNLSNLSRNHPATTSNWRTLPAYIQFLIKEEDKLDPCIQGLFFLLLGIAFREIFHIEVMRIRHSQLNLMRDIKESSSGLTSAKSLGDAQNLCENAVRLYSSYKHYITSMKKGSSLLTIEYISSTAPNTFNEFFVQKKANIPLPLDIDAPIGVTIRFSHNLLNEWIKKQGDVFESKLLKEDIENLQSLEESYPIAQYL
Protein: 2-5A-dependent ribonuclease (2-5A-dependent RNase) (EC 3.1.26.-) (Ribonuclease 4) (Ribonuclease L) (RNase L) (Q05823)
Organism: Homo sapiens (Human)
Function: Endoribonuclease that functions in the interferon (IFN) antiviral response. In INF treated and virus infected cells, RNASEL probably mediates its antiviral effects through a combination of direct cleavage of single-stranded viral RNAs, inhibition of protein synthesis through the degradation of rRNA, induction of apoptosis, and induction of other antiviral genes. RNASEL mediated apoptosis is the result of a JNK-dependent stress-response pathway leading to cytochrome c release from mitochondria and caspase-dependent apoptosis. Therefore, activation of RNASEL could lead to elimination of virus infected cells under some circumstances. In the crosstalk between autophagy and apoptosis proposed to induce autophagy as an early stress response to small double-stranded RNA and at later stages of prolonged stress to activate caspase-dependent proteolytic cleavage of BECN1 to terminate autophagy and promote apoptosis. Might play a central role in the regulation of mRNA turnover. Cleaves 3' of UpNp dimers, with preference for UU and UA sequences, to sets of discrete products ranging from between 4 and 22 nucleotides in length.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11585831}. Mitochondrion {ECO:0000269|PubMed:11585831}.
Interaction partners:
- ATP-binding cassette sub-family E member 1
- ATP-dependent RNA helicase DHX33
- 2'-5'-oligoadenylate synthase 1
- 2'-5'-oligoadenylate synthase 3
- Filamin-A
- 2'-5'-oligoadenylate synthase 2
- 2'-5'-oligoadenylate synthase-like protein
- 2',5'-phosphodiesterase 12
- Interferon-induced, double-stranded RNA-activated protein kinase
- Antiviral innate immune response receptor RIG-I
Sequence:
MESRDHNNPQEGPTSSSGRRAAVEDNHLLIKAVQNEDVDLVQQLLEGGANVNFQEEEGGWTPLHNAVQMSREDIVELLLRHGADPVLRKKNGATPFILAAIAGSVKLLKLFLSKGADVNECDFYGFTAFMEAAVYGKVKALKFLYKRGANVNLRRKTKEDQERLRKGGATALMDAAEKGHVEVLKILLDEMGADVNACDNMGRNALIHALLSSDDSDVEAITHLLLDHGADVNVRGERGKTPLILAVEKKHLGLVQRLLEQEHIEINDTDSDGKTALLLAVELKLKKIAELLCKRGASTDCGDLVMTARRNYDHSLVKVLLSHGAKEDFHPPAEDWKPQSSHWGAALKDLHRIYRPMIGKLKFFIDEKYKIADTSEGGIYLGFYEKQEVAVKTFCEGSPRAQREVSCLQSSRENSHLVTFYGSESHRGHLFVCVTLCEQTLEACLDVHRGEDVENEEDEFARNVLSSIFKAVQELHLSCGYTHQDLQPQNILIDSKKAAHLADFDKSIKWAGDPQEVKRDLEDLGRLVLYVVKKGSISFEDLKAQSNEEVVQLSPDEETKDLIHRLFHPGEHVRDCLSDLLGHPFFWTWESRYRTLRNVGNESDIKTRKSESEILRLLQPGPSEHSKSFDKWTTKINECVMKKMNKFYEKRGNFYQNTVGDLLKFIRNLGEHIDEEKHKKMKLKIGDPSLYFQKTFPDLVIYVYTKLQNTEYRKHFPQTHSPNKPQCDGAGGASGLASPGC
Protein: NAD(P) transhydrogenase subunit alpha (EC 7.1.1.1) (Nicotinamide nucleotide transhydrogenase subunit alpha) (Pyridine nucleotide transhydrogenase subunit alpha) (Q9ALA2)
Organism: Cereibacter sphaeroides (Rhodobacter sphaeroides)
Function: The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane.
Subcellular location: Cell inner membrane {ECO:0000250|UniProtKB:P07001}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P07001}.
Interaction partners:
Sequence:
MKIGAPREIFEGEARVAMTPDSALQLQKLGHHCVIETGAGMKAGFSDEAYAAAGVEVLPSAAALFEAADIVVKVRGPERAEAERLRRGQTLISFFWPAQNAELLELCKEKGATVVAMDMVPRISRAQKMDALSSMANIAGYRAVIEAGNNFGRFFTGQVTAAGKVPPAKVLVVGAGVAGLAAIGTATSLGAITYAFDVRPEVAEQIESMGAEFVYLEFEEAQDGAATGGYAAPSSPEFREKQLAKFRELAPEMDIVITTALIPGRPAPKLWTEDMVSAMKRGSVIVDLASERGGNCDLTVPDQKIVTPNGVTIVGYTDFPSRMAAQASTLYSTNIRHMLTDLTPKKDGVIHHNMEDDVIRGATVTHDGAITFPPPPPKVAAIAAAKPREKVKELTPEEKRAAEIATFRKQTVSQVAMLAVGTALLLFVGMYAPPSFMAHFIVFALACFVGFQVIWNVSHSLHTPLMAVTNAISGIVILGALLQIGSGNVLVVLLAAISVLIATINIVGGFLVTRRMLAMFQKS
Protein: Small nuclear ribonucleoprotein E (snRNP-E) (Sm protein E) (D6XI03)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU365053}.
Interaction partners:
- Sm protein F
- U1 small nuclear ribonucleoprotein, putative
- U2 small nuclear ribonucleoprotein B, putative
- PRP1 splicing factor N-terminal domain-containing protein
- Small nuclear ribonucleoprotein Sm D2
- PRP8 protein homologue
- G10 protein
- U5 small nuclear ribonucleoprotein component, putative
- Pre-mRNA-splicing factor Syf1-like N-terminal HAT-repeats domain-containing protein
- Sm protein B
Sequence:
MSVTTKQMVKPTVVVHRYLKESQRVCVWLVHETKMKIEGVLLGYDEFMNVVLGDATEVHLKTGEVVQLGKILLRSDNVGVIHPIGI
Protein: Photosystem II CP47 reaction center protein (PSII 47 kDa protein) (Protein CP-47) (P0C363)
Organism: Oryza sativa subsp. indica (Rice)
Function: One of the components of the core complex of photosystem II (PSII). It binds chlorophyll and helps catalyze the primary light-induced photochemical processes of PSII. PSII is a light-driven water:plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01495}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01495}.
Interaction partners:
- Photosystem I iron-sulfur center
- Photosystem II protein D1
- Photosystem II D2 protein
- Photosystem II CP43 reaction center protein
- Cytochrome b559 subunit alpha
- Cytochrome b559 subunit beta
- Cytochrome f
- NAD
- NAD
- 33 kDa subunit of oxygen evolving system of photosystem II
Sequence:
MGLPWYRVHTVVLNDPGRLLSVHIMHTALVSGWAGSMALYELAVFDPSDPVLDPMWRQGMFVIPFMTRLGITNSWGGWSISGGTVTNPGIWSYEGVAGAHIVFSGLCFLAAIWHWVYWDLEIFCDERTGKPSLDLPKIFGIHLFLAGVACFGFGAFHVTGLYGPGIWVSDPYGLTGKVQAVNPVWGAEGFDPFVPGGIASHHIAAGTLGILAGLFHLSVRPPQRLYKGLRMGNIETVLSSSIAAVFFAAFVVAGTMWYGSATTPIELFGPTRYQWDQGYFQQEIYRRVSDGLAENLSLSEAWSKIPEKLAFYDYIGNNPAKGGLFRAGSMDNGDGIAVGWLGHPIFRDKEGRELFVRRMPTFFETFPVVLVDEEGIVRADVPFRRAESKYSVEQVGVTVEFYGGELNGVSYSDPATVKKYARRSQLGEIFELDRATLKSDGVFRSSPRGWFTFGHATFALLFFFGHIWHGARTLFRDVFAGIDPDLDAQVEFGTFQKVGDPTTRRQPV
Protein: Structural maintenance of chromosomes protein 2 (SMC protein 2) (SMC-2) (Chromosome-associated protein E) (FGF-inducible protein 16) (XCAP-E homolog) (Q8CG48)
Organism: Mus musculus (Mouse)
Function: Central component of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases (By similarity).
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Chromosome {ECO:0000250}. Note=In interphase cells, the majority of the condensin complex is found in the cytoplasm, while a minority of the complex is associated with chromatin. A subpopulation of the complex however remains associated with chromosome foci in interphase cells. During mitosis, most of the condensin complex is associated with the chromatin. At the onset of prophase, the regulatory subunits of the complex are phosphorylated by CDC2, leading to condensin's association with chromosome arms and to chromosome condensation. Dissociation from chromosomes is observed in late telophase (By similarity). {ECO:0000250}.
Interaction partners:
- Structural maintenance of chromosomes protein 4
- Non-SMC condensin I complex, subunit G
- Condensin complex subunit 1
- Condensin complex subunit 2
- Condensin-2 complex subunit D3
- Condensin-2 complex subunit H2
- Condensin-2 complex subunit G2
- Kinesin-like protein KIF11
- Kinetochore protein NDC80 homolog
- DNA topoisomerase 2-alpha
Sequence:
MYVKSIILEGFKSYAQRTEVNGFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYKNGQAGITKASVSITFDNSDKKQSPLGFEAHDEITVTRQVVIGGRNKYLINGVNANNTRVQDLFCSVGLNVNNPHFLIMQGRITKVLNMKPPEILSMIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTILEEEITPTIQKLKEERSSYLEYQKVMREIEHLSRLYIAYQFLRAEDTKERSAGELKEMQDKIVNLQEVLSENEKKIKALNCEIEELERRKDKETGGKLKSLEDACAEAQRVNTKSQSAFDLKKKNLASEETKRKELQNSMAEDSKALAAKEKEVKKITDGLHGLQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEATLAGQMIACKNDISKAQTEAKQAQMKLKHAQQELKSKQAEVKKMDSGYKKDQDAFEAVKKAKEKLETEMKKLNYEENKEEKLLEKHRQLSRDINNLKGKHEALLAKFPNLQFAYKDPEKNWNRNSVKGLVASLINVKDNSTATALEVVAGERLYNVVVDTEVTAKKLLEKGELKRRYTIIPLNKISARCIAPETLRVAQNLVGPDNVHVALSLVDYKPELQKGMEFVFGTTFVCNNMDNAKKVAFDKRIMTRTVTLGGDVFDPHGTLSGGARSQAASILTKFQEVKDVQDELRTKENELRALEEELAGLKNVAEKYRQLKQQWEMKTEEGDLLQTKLQQSSYHKQQEELDALKKTIEESEETLKSTKEIQKKAEEKYEALENKMKNAEAEREKELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHASNEQQLDAVNEAIKAYEGQIEKMAAEVAKNKESVNKAQDELMKQKQIITAQDNIIKDKCAEVAKHNLQNNESQLKIKELDHSISKHKREADDAAAKVSKMLSDYDWINAEKHLFGQPNSAYDFKTNNPKEAGQRLQKLQEVKEKLGRNVNLRAMNVLTEAEERYNDLMKKKRIVENDKSKILATIEDLDQKKNQALNIAWQKVNKDFGSIFSTLLPGANAMLAPPEGQTVLDGLEFKVALGNTWKENLTELSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTHSQFIVVSLKEGMFNNANVLFKTKFVDGVSTVARFTQSQAGKIPKEAKSRGKEPN
Protein: poly(A)-specific ribonuclease (EC 3.1.13.4) (Q583U3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- NOT1
- Cell differentiation protein, putative
- Uncharacterized protein
- NOT2/NOT3/NOT5 C-terminal domain-containing protein
- Probable eukaryotic initiation factor 4A
- Endonuclease/exonuclease/phosphatase domain-containing protein
- Endonuclease/exonuclease/phosphatase, putative
- Ribosomal RNA processing protein 45
Sequence:
MMQYGGGTHYGAYAQQQPQPQPQPHQRFPSAALKAGNVSLIPSLSKSPMIRDVWEDNLEQEFGIIRSLIKDYPFVAMDTEFPGVVAKPVGNFKSTHEFYYQTLRCNVNLLKMIQLGITLLNEKGEVPENCCTWQFNFRFCLTEDVYAQDSIQLLCHGGINFDYFSEYGVEVTHFAELLISSGLVLNPDIRWLAFHAGYDFGYLIKVVGGKDLPEKEEDFLQTFHALFPCVYDIKYLLRSTELTHSLGLDHLADSLRVRRFGMAHQAGSDSLLTGHCYFKLLRDCFNSNIPVANNGVLYGLCEDSSSAGTPNSTTIPGSGGGGGHAFSNFTGSKNAAFPASPIMTQAVKGHS
Protein: COP9 signalosome complex subunit 2 (SGN2) (Signalosome subunit 2) (Alien homolog) (JAB1-containing signalosome subunit 2) (Thyroid receptor-interacting protein 15) (TR-interacting protein 15) (TRIP-15) (P61203)
Organism: Rattus norvegicus (Rat)
Function: Essential component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. Involved in early stage of neuronal differentiation via its interaction with NIF3L1.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12606288}. Nucleus {ECO:0000269|PubMed:12524175, ECO:0000269|PubMed:12606288}.
Interaction partners:
- COP9 signalosome complex subunit 3
- COP9 signalosome complex subunit 8
- COP9 signalosome complex subunit 5
- COP9 signalosome complex subunit 6
- COP9 signalosome complex subunit 1
- COP9 signalosome complex subunit 4
- COP9 signalosome subunit 7A
- COP9 signalosome subunit 7B
- E3 ubiquitin-protein ligase RBX1
- Cullin-4B
Sequence:
MSDMEDDFMCDDEEDYDLEYSEDSNSEPNVDLENQYYNSKALKEDDPKAALSSFQKVLELEGEKGEWGFKALKQMIKINFKLTNFPEMMNRYKQLLTYIRSAVTRNYSEKSINSILDYISTSKQMDLLQEFYETTLEALKDAKNDRLWFKTNTKLGKLYLEREEYGKLQKILRQLHQSCQTDDGEDDLKKGTQLLEIYALEIQMYTAQKNNKKLKALYEQSLHIKSAIPHPLIMGVIRECGGKMHLREGEFEKAHTDFFEAFKNYDESGSPRRTTCLKYLVLANMLMKSGINPFDSQEAKPYKNDPEILAMTNLVSAYQNNDITEFEKILKTNHSNIMDDPFIREHIEELLRNIRTQVLIKLIKPYTRIHIPFISKELNIDVADVESLLVQCILDNTIHGRIDQVNQLLELDHQKRGGARYTALDKWTNQLNSLNQAVVSKLA
Protein: Possible oxidoreductase (O53608)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Secreted protein
- Uncharacterized protein Rv1352
- Conserved protein
- N-acetylmuramoyl-L-alanine amidase Rv3717
- Tyrosine recombinase XerC
- Probable conserved proline, glycine, valine-rich secreted protein
- ECF RNA polymerase sigma factor SigD
- 1,4-beta-xylanase
- Conserved hypothetical threonine and proline rich protein
- Acyl-CoA:diacylglycerol acyltransferase
Sequence:
MAREISRQTFLRGAAGALAAGAVFGSVRATADPAASGWEALSSALGGKVLQPDDGPQFATAKQVFNTNYNGYTPAVIVTPTSQLDVQKAMAFAAANNLKVAPRGGGHSYVGASTANGAMVLDLRQLPGDINYDATTGRVTVTPATGLYAMHQVLAAAGRGIPTGTCPTVGVAGHALGGGLGANSRHAGLLCDQLTSASVVLPSGQAVTASATDHPDLFWALRGGGGGNFGVTTSLTFATFPSGDLDVVNLNFPPQSFAQVLVGWQNWLRTADRGSWALADATVDPLGTHCRILATCPAGSGGSVAAAIVSAVGTQPTGTENHTFNYLDLVRYLAVGNLNPSPLGYVGGSDVFTTITPATAQGIASAVDAFPRGAGRMLAIMHALDGALATVSPGATAFPWRRQSALVQWYVETSGSPSEATSWLNTAHQAVRAYSVGGYVNYLEVNQPPARYFGPNLSRLSAVRQKYDPSRVMFSGLNF
Protein: Tubulin epsilon chain (Epsilon-tubulin) (Q9UJT0)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:10620804}. Note=Associated with pericentriolar material. {ECO:0000269|PubMed:10620804}.
Interaction partners:
- Tubulin delta chain
- Tubulin epsilon and delta complex protein 2
- Centriolin
- Ninein
- Tubulin epsilon and delta complex protein 1
- Outer dense fiber protein 2
- Centrosomal protein of 170 kDa
- Spindle assembly abnormal protein 6 homolog
Sequence:
MTQSVVVQVGQCGNQIGCCFWDLALREHAAVNQKGIYDEAISSFFRNVDTRVVGDGGSISKGKICSLKARAVLIDMEEGVVNEILQGPLRDVFDTKQLITDISGSGNNWAVGHKVFGSLYQDQILEKFRKSAEHCDCLQCFFIIHSMGGGTGSGLGTFLLKVLEDEFPEVYRFVTSIYPSGEDDVITSPYNSILAMKELNEHADCVLPIDNQSLFDIISKIDLMVNSGKLGTTVKPKSLVTSSSGALKKQHKKPFDAMNNIVANLLLNLTSSARFEGSLNMDLNEISMNLVPFPQLHYLVSSLTPLYTLTDVNIPPRRLDQMFSDAFSKDHQLLRADPKHSLYLACALMVRGNVQISDLRRNIERLKPSLQFVSWNQEGWKTSLCSVPPVGHSHSLLALANNTCVKPTFMELKERFMRLYKKKAHLHHYLQVEGMEESCFTEAVSSLSALIQEYDQLDATKNMPVQDLPRLSIAM
Protein: ATP-dependent protease ATPase subunit HslU (Unfoldase HslU) (Q44772)
Organism: Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) (Borrelia burgdorferi)
Function: ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00249}.
Interaction partners:
- ATP-dependent protease subunit HslV
- Protein GrpE
- Co-chaperonin GroES
- Chaperonin GroEL
- Chaperone protein HtpG
- Cell division protein FtsZ
- Protein Smf
- TPR repeat-containing protein BB_0298
- Chaperone protein DnaJ
- Flagellar basal body rod protein FlgB
Sequence:
MNKLEEHYIVPKDVVAELDKYIIGQDEAKKLVSIALVNRYIRSRLPKEIKDEVMPKNIIMIGSTGIGKTEIARRLSKLIKAPFIKVEATKYTEVGYVGRDVESMVRDLMSIAVNMVKEEMYSTVRDDALVRTEERIVDSLFKGSSNSENMDPNEIKAEEKVKEKLRKKLRAGELDDTTIEIQISSKMPFSTIEIFTGGNFEEIDMGIGGLLGNIFDRKKKRELKIKKAKEIILAEELEKLVDHENISDIAKSKVENMGIIFIDEIDKIAAKNRSGNDVSREGVQRDILPIIEGSKVNTKYGIVDTSHILFIAAGAFNLAKPSDLIPELQGRFPIKVELKSLSIDDLKKILKQTKNSLIKQYVAMFKVYDLDLKFSEEAIDRIAELTFNMNLESENLGARRLHGVMEIVLADLFFEVPGSKLKKFEINLDYVNKKIQINEQKDLNYYII
Protein: Protein transport protein SSO2 (Q59YF0)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Late secretory t-SNARE protein required for secretion and proper cytokinesis. Plays an important role in the secretion of virulence-associated extracellular enzymes and vesicle-mediated polarized hyphal growth.
Subcellular location: Membrane {ECO:0000255}; Single-pass type IV membrane protein {ECO:0000255}.
Interaction partners:
- Sec1p
- Protein transport protein SEC9
- SNAP receptor
- Uncharacterized protein
- Synaptobrevin homolog YKT6
- Protein transport protein SEC22
- Vesicular-fusion protein SEC18
- t-SNARE syntaxin
- V-SNARE coiled-coil homology domain-containing protein
- Syntaxin
Sequence:
MSNPYQNSQNGYQQNNSYELNNYPNKQYSSSNEDDFVQFMNEIQDINSQLDNYSNIINLIDNKQKNFLHGLDLNDEDTDYDSKQIENLVNEAQSLQLDLKNRIKNVQTQAVHSRDQTKVDQAETCRKRFLDLIQDYRLVEARNKESTKEQAARQYQIIKPDATDEEIKAVVEDGSQQYFQQALMQSNRRGEARSVLNEVQVRHRELLKLEKTMAELTQLFHDMEELVIEQDQPIQQIEEQVGTAQHDIEQGVGHTNKAVKSAKSARKKKLWCFFICLLIVIILAVILGAYFGTRK