wanglab/gogpt-training-data huggingface dataset:
Protein: Lipoyl synthase, mitochondrial (EC 2.8.1.8) (Lipoate synthase) (LS) (Lip-syn) (Lipoic acid synthase) (O13642)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Subcellular location: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03123, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Probable octanoyltransferase
- Putative lipoate-protein ligase A
- NifU-like protein C1709.19c
- Iron-sulfur cluster assembly factor IBA57
- Aconitate hydratase, mitochondrial
- Putative glycine cleavage system H protein, mitochondrial
- Probable cysteine desulfurase, mitochondrial
- Iron sulfur cluster assembly protein 1, mitochondrial
- Biotin synthase
- Monothiol glutaredoxin-5
Sequence:
MLKIGRNATILKNNFWFASVRFQSGGFSEKLAKGPSFADFLNMDKPLTADEAFELDRKVELPNGSIHKRLPSWLKTKVPLGTNFNRIKHDLRGSHLHTVCEEAKCPNIGECWGGKDKSRATATIMLMGDTCTRGCRFCSVKTSRRPGPLDPNEPENTAEAIKQWNLGYIVLTSVDRDDLTDLGANHIAKTIQKIKEKAPHILVEALTPDFSGRMDLVEIVAKSGLDVFAHNVETVEELTPFVRDRRATYRQSLSVLKHVKKTCPHLITKTSIMLGLGETDAEILTTLKDLLEHNVDVVTFGQYMRPTKRHLKVQEYVHPKKFEYWKEVAEKLGFLYVASGPLVRSSYKAGEYFMENLIKKRSGNPASMSV
Protein: Butyrophilin-like protein 2 (BTL-II) (Q9UIR0)
Organism: Homo sapiens (Human)
Function: Negative regulator of T-cell proliferation.
Subcellular location: Membrane {ECO:0000269|PubMed:15735647}; Single-pass type II membrane protein {ECO:0000269|PubMed:15735647}. Note=Isoform 2 is present in the nuclear, vesicle and plasma membranes, isoform 3 is found in cytoplasmic vesicle structures and is not membrane bound.
Interaction partners:
- HLA class II histocompatibility antigen, DRB1 beta chain
- Annexin A11
- HLA class II histocompatibility antigen, DR alpha chain
- HLA class II histocompatibility antigen, DQ beta 1 chain
- HLA class II histocompatibility antigen, DR beta 5 chain
Sequence:
MVDFPGYNLSGAVASFLFILLTMKQSEDFRVIGPAHPILAGVGEDALLTCQLLPKRTTMHVEVRWYRSEPSTPVFVHRDGVEVTEMQMEEYRGWVEWIENGIAKGNVALKIHNIQPSDNGQYWCHFQDGNYCGETSLLLKVAGLGSAPSIHMEGPGESGVQLVCTARGWFPEPQVYWEDIRGEKLLAVSEHRIQDKDGLFYAEATLVVRNASAESVSCLVHNPVLTEEKGSVISLPEKLQTELASLKVNGPSQPILVRVGEDIQLTCYLSPKANAQSMEVRWDRSHRYPAVHVYMDGDHVAGEQMAEYRGRTVLVSDAIDEGRLTLQILSARPSDDGQYRCLFEKDDVYQEASLDLKVVSLGSSPLITVEGQEDGEMQPMCSSDGWFPQPHVPWRDMEGKTIPSSSQALTQGSHGLFHVQTLLRVTNISAVDVTCSISIPFLGEEKIATFSLSESRMTFLWKTLLVWGLLLAVAVGLPRKRS
Protein: Cd6 molecule (D3ZVW6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MLQHGEWGTVCDDTWDLDDANVVCKQLKCGWAVKALAGLHFTPGQGPIHRDQVNCSGTEAYLWDCPGRPGDQYCGHKEDAGVVCSGSQRHPNLSTSEVPSRVPVTIESSVPVSVKDKDSQNLTLLIPCIVLGILLLVSLIFIVFLLLKAKGQYALPTSVNHQQLSTANPAGINNYHPVPITIAKEAPMLFIKPRVPEDSDSSSESDYEHYDFSSQPPVALTTFYNSQRHRVTEEEAQQNRFRMPPLEEGLEELHVSNIPAADPRPCVVDAPSLGSQYHTRNNSDSSTSSEEGYCNDPSSKPPPWNSQVFSEKSPLTEQPPNLELAGSQAMFSAGASADDSSSTSSGEWYQNFQPPPQHPPVEQFECPGPPDLQADSIDDDEEDYDDIGAA
Protein: Phosphodiesterase (EC 3.1.4.-) (A0A0G2K2K1)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Calmodulin-1
- Calmodulin-like protein 3
- Calmodulin-like protein 4
- Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1C
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
- Adenine phosphoribosyltransferase
- Adenosine kinase
Sequence:
MSSNVNVLRCLVKQLEKGDVNVVDLKKNIEYAASVLEAVYIDETRRLLDTEDELSDIQTDSVPSEVRDWLASTFTRKMGMTKKKPEEKPKFRSIVHAVQAGIFVERMYRKNYHMVGLTYPAAVIVTLKEVDKWSFDVFALNEASGEHSLKFMIYELFTRYDLINRFKIPVSCLIAFAEALEVGYSKHKNPYHNLVHAADVTQTVHYIMLHTGIMHWLTELEILAMVFAAAVHDYEHTGTTNNFHIQTRSDVAILYNDRSVLENHHVSAAYRLMQEEEMNILVNLSKDDWRDLRNLVIEMVLATDMSGHFQQIKNIRSSLQQPEGIDRAKTMSLILHAADISHPAKTWKLHYRWTMALMEEFFLQGDKEAELGLPFSPLCDRKSTMVAQSQIGFIDFIVEPTFSLLTDSTEKIVIPLIEEASKPESSNYGASSSSTMIGFHVADALRRSNTKGCMSDGTYAPDYSLSAVDLKSFKNNLVDIIQQNKERWKELAAQGELDLHKNSEDLEEKHADTHP
Protein: Prolyl-tRNA synthetase (A0A0H2UN86)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Interaction partners:
Sequence:
MNTVKNKQEILEAFRESPDMMAILTIIRDLGLKDSWLAAGSVRNFIWNLLSDKSPFDHETDIDVIFFDPDFSYEETLLLEKKLREDFPQYQWELKNQVYMHQHSPHTASYTSSRDAMSKYPERCTAVGLRLNEELDFELYVPYGLEDILNFQVRPTPHFLENEDRMELYQTRLSKKNWQEKWKNLIFKNT
Protein: Zinc finger protein 114 (Q8NC26)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B gamma isoform
- CAP-Gly domain-containing linker protein 4
- Transcription intermediary factor 1-beta
Sequence:
MSQDSVTFADVAVNFTKEEWTLLDPAQRNLYRDVMLENSRNLAFIDWATPCKTKDATPQPDILPKRTFPEANRVCLTSISSQHSTLREDWRCPKTEEPHRQGVNNVKPPAVAPEKDESPVSICEDHEMRNHSKPTCRLVPSQGDSIRQCILTRDSSIFKYNPVLNDSQKTHENNEDDGVLGWNIQWVPCGRKTELKSSTWTGSQNTVHHIRDEIDTGANRHQRNPFGKAFREDGSLRAHNTHGREKMYDFTQCENTSRNNSIHAMQMQLYTAETNKKDCQTGATSANAPNSGSHKSHCTGEKTHKCPECGRAFFYQSFLMRHMKIHTGEKPYECGKCGKAFRYSLHLNKHLRKHVVQKKPYECEECGKVIRESSKYTHIRSHTGEKPYKCKTCGKDFAKSSGLKKHLKTHKDEKPCE
Protein: Fumarase E (EC 4.2.1.2) (P11663)
Organism: Escherichia coli (strain K12)
Function: In vitro catalyzes the addition of water to fumarate, forming malate. Cannot catalyze the reverse reaction. Cannot use the cis-isomer maleate as substrate.
Interaction partners:
- Fumarase D
- Uncharacterized protein YggC
- Fumarate hydratase class II
- Fumarate hydratase class I, aerobic
- Fumarate hydratase class I, anaerobic
- NADP-dependent malic enzyme
- Malate synthase A
- Malate:quinone oxidoreductase
- NAD-dependent malic enzyme
- Malate synthase G
Sequence:
MATLTEDDVLEQLDAQDNLFSFMKTAHTILLQGIRQFLPSLFVDNDEEIVEYAVKPLLAQSGPLDDIDVALRLIYALGKMDKWLYADITHFSQFWHYLNEQDETPGFADDMTWDFISNVNSITRNAMLYDALKAMKFADFSVWSEARFSGMVKTALTLAVTTTLKELTP
Protein: Transforming growth factor beta-3 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-3 (TGF-beta-3)] (P17125)
Organism: Mus musculus (Mouse)
Function: Transforming growth factor beta-3 proprotein: Precursor of the Latency-associated peptide (LAP) and Transforming growth factor beta-3 (TGF-beta-3) chains, which constitute the regulatory and active subunit of TGF-beta-3, respectively.
Subcellular location: [Latency-associated peptide]: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P01137}.; SUBCELLULAR LOCATION: [Transforming growth factor beta-3]: Secreted {ECO:0000250|UniProtKB:P01137}.
Interaction partners:
- TGF-beta receptor type-2
- TGF-beta receptor type-1
- Endoglin
- Latent-transforming growth factor beta-binding protein 1
- Transforming growth factor beta receptor type 3
- Activin receptor type-1-like
- Transforming growth factor beta-1 proprotein
- Decorin
- Latent-transforming growth factor beta-binding protein 3
- Fibromodulin
Sequence:
MHLQRALVVLALLNLATISLSLSTCTTLDFGHIKKKRVEAIRGQILSKLRLTSPPEPSVMTHVPYQVLALYNSTRELLEEMHGEREEGCTQETSESEYYAKEIHKFDMIQGLAEHNELAVCPKGITSKVFRFNVSSVEKNGTNLFRAEFRVLRVPNPSSKRTEQRIELFQILRPDEHIAKQRYIGGKNLPTRGTAEWLSFDVTDTVREWLLRRESNLGLEISIHCPCHTFQPNGDILENVHEVMEIKFKGVDNEDDHGRGDLGRLKKQKDHHNPHLILMMIPPHRLDSPGQGSQRKKRALDTNYCFRNLEENCCVRPLYIDFRQDLGWKWVHEPKGYYANFCSGPCPYLRSADTTHSTVLGLYNTLNPEASASPCCVPQDLEPLTILYYVGRTPKVEQLSNMVVKSCKCS
Protein: Homeobox protein Hox-D12 (Homeobox protein Hox-4.7) (Homeobox protein Hox-5.6) (P23812)
Organism: Mus musculus (Mouse)
Function: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.
Subcellular location: Nucleus.
Interaction partners:
Sequence:
MCERSLYRAGYVGSLLNLQSPDSFYFSNLRANGSQLAALPPISYPRSALPWATTPASCTPAQPATASAFGGFSQPYLTGSGPIGLQSPGAKDGPEDQVKFYTPDAPTASEERSRTRPPFAPESSLVHSALKGTKYDYAGVGRTAPGSATLLQGAPCASSFKEDTKGPLNLNMAVQVAGVASCLRSSLPDGLPWGAAPGRARKKRKPYTKQQIAELENEFLVNEFINRQKRKELSNRLNLSDQQVKIWFQNRRMKKKRVVQREQALALY
Protein: Baseplate wedge protein gp25 (Outer wedge of baseplate protein) (Protein Gp25) (P09425)
Organism: Enterobacteria phage T4 (Bacteriophage T4)
Function: Baseplate protein that is located next to the tail tube (inner baseplate). Involved in sheath assembly. The gp25-(gp6)2-gp7 module is involved in sheath contraction.
Subcellular location: Virion {ECO:0000269|PubMed:15315755, ECO:0000269|PubMed:15342608, ECO:0000269|PubMed:2403438, ECO:0000269|PubMed:27193680}. Note=Present in 6 copies in the baseplate. {ECO:0000303|PubMed:21129200}.
Interaction partners:
Sequence:
MANINKLYSDIDPEMKMDWNKDVSRSLGLRSIKNSLLGIITTRKGSRPFDPEFGCDLSDQLFENMTPLTADTVERNIESAVRNYEPRIDKLAVNVIPVYDDYTLIVEIRFSVIDNPDDIEQIKLQLASSNRV
Protein: Interleukin-6 (M5EF24)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
Sequence:
MNSSTRYLSLLSALVVLVKGNPVPSALAELMTSGWTSGEELGTDGETGAPPKWEKMIKMLVHEVTTLRNQQFVEEFQKPVEEISSFSQHQVPSTPPHLSKTLCSTSNKEACLQEISRGLQVYQLLLQHVKAEYPQSTLLPSVTHQTTVLIGLVKDQMKVAEVVEDLSASERKRVLGEVSTGTEWERKTSVHAILRELRNFLVDTKRALRRMGKRGKDFQ
Protein: ATP synthase subunit gamma, mitochondrial (F-ATPase gamma subunit) (P38077)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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(1) domain and the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha(3)beta(3). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
Subcellular location: Mitochondrion. Mitochondrion inner membrane; Peripheral membrane protein.
Interaction partners:
- ATP synthase subunit delta, mitochondrial
- ATP synthase subunit beta, mitochondrial
- ATP synthase subunit alpha
- ATP synthase subunit a
- ATP synthase subunit 9, mitochondrial
- ATP synthase subunit 4
- ATP synthase subunit g, mitochondrial
- ATP synthase subunit epsilon, mitochondrial
- ATP synthase subunit d
- ATP synthase subunit 5, mitochondrial
Sequence:
MLSRIVSNNATRSVMCHQAQVGILYKTNPVRTYATLKEVEMRLKSIKNIEKITKTMKIVASTRLSKAEKAKISAKKMDEAEQLFYKNAETKNLDVEATETGAPKELIVAITSDKGLCGSIHSQLAKAVRRHLNDQPNADIVTIGDKIKMQLLRTHPNNIKLSINGIGKDAPTFQESALIADKLLSVMKAGTYPKISIFYNDPVSSLSFEPSEKPIFNAKTIEQSPSFGKFEIDTDANVPRDLFEYTLANQMLTAMAQGYAAEISARRNAMDNASKNAGDMINRYSILYNRTRQAVITNELVDIITGASSLG
Protein: Growth differentiation factor 11 (H0YI30)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
XAAAAAAAAAAAAAGVGGERSSRPAPSVAPEPDGCPVCVWRQHSRELRLESIKSQILSKLRLKEAPNISREVVKQLLPKAPPLQQILDLHDFQGDALQPEDFLEEDEYHATTETVISMAQETDPAVQTDGSPLCCHFHFSPKVMFTKVLKAQLWVYLRPVPRPATVYLQILRLKPLTGEGTAGGGGGGRRHIRIRSLKIELHSRSGHWQSIDFKQVLHSWFRQPQSNWGIEINAFDPSGTDLAVTSLGPGAEGLHPFMELRVLENTKRSRRNLGLDCDEHSSESRCCRYPLTVDFEAFGWDWIIAPKRYKANYCSGQCEYMFMQKYPHTHLVQQANPRGSAGPCCTPTKMSPINMLYFNDKQQIIYGKIPGMVVDRCGCS
Protein: Endoribonuclease toxin MazF (EC 3.1.27.-) (Toxin MazF) (mRNA interferase MazF) (P0AE70)
Organism: Escherichia coli (strain K12)
Function: Toxic component of a type II toxin-antitoxin (TA) system. A sequence-specific endoribonuclease it inhibits protein synthesis by cleaving mRNA and inducing bacterial stasis. It is stable, single-strand specific with mRNA cleavage independent of the ribosome, although translation enhances cleavage for some mRNAs. Cleavage occurs at the 5'-end of ACA sequences, yielding a 2',3'-cyclic phosphate and a free 5'-OH, although cleavage can also occur on the 3'-end of the first A. Digests 16S rRNA in vivo 43 nts upstream of the C-terminus; this removes the anti-Shine-Dalgarno sequence forming a mixed population of wild-type and 'stress ribosomes'. Stress ribosomes do not translate leader-containing mRNA but are proficient in translation of leaderless mRNA, which alters the protein expression profile of the cell; MazF produces some leaderless mRNA. The toxic endoribonuclease activity is inhibited by its labile cognate antitoxin MazE. Toxicity results when the levels of MazE decrease in the cell, leading to mRNA degradation. This effect can be rescued by expression of MazE, but after 6 hours in rich medium overexpression of MazF leads to programmed cell death. MazF-mediated cell death occurs following a number of stress conditions in a relA-dependent fashion and only when cells are in log phase; sigma factor S (rpoS) protects stationary phase cells from MazF-killing. Cell growth and viability are not affected when MazF and MazE are coexpressed. Both MazE and MazE-MazF bind to the promoter region of the mazE-mazF operon to inhibit their own transcription. MazE has higher affinity for promoter DNA in the presence of MazF. Cross-talk can occur between different TA systems, ectopic expression of this toxin induces transcription of the relBEF TA system operon with specific cleavage of the mRNA produced.
Interaction partners:
- Antitoxin MazE
- Antitoxin ChpS
- mRNA interferase toxin RelE
- Antitoxin DinJ
- mRNA interferase toxin YafQ
- Nucleoside triphosphate pyrophosphohydrolase
- Antitoxin RelB
- mRNA interferase toxin HigB
- Toxin YoeB
- mRNA interferase toxin MqsR
Sequence:
MVSRYVPDMGDLIWVDFDPTKGSEQAGHRPAVVLSPFMYNNKTGMCLCVPCTTQSKGYPFEVVLSGQERDGVALADQVKSIAWRARGATKKGTVAPEELQLIKAKINVLIG
Protein: Transcription factor 7-like 1 (HMG box transcription factor 3) (TCF-3) (mTCF-3) (Q9Z1J1)
Organism: Mus musculus (Mouse)
Function: Participates in the Wnt signaling pathway. Binds to DNA and acts as a repressor in the absence of CTNNB1, and as an activator in its presence. Necessary for the terminal differentiation of epidermal cells, the formation of keratohyalin granules and the development of the barrier function of the epidermis.
Subcellular location: Nucleus.
Interaction partners:
- Catenin beta-1
- Serine/threonine-protein kinase NLK
- Junction plakoglobin
- Transcription factor 7-like 2
- C-terminal-binding protein 1
- C-terminal-binding protein 2
- Transcription factor SOX-17
- Telomerase reverse transcriptase
- Transcription factor 7
- Histone acetyltransferase p300
Sequence:
MPQLGGGRGGAGGGGGGSGAGATSGGDDLGANDELIPFQDEGGEEQEPSSDTASAQRDLDEVKSSLVNESENQSSSSDSEAERRPQPARDAFQKPRDYFAEVRRPQDGAFFKGGAYPGYPFLMIPDLSSPYLSNGPLSPGGARTYLQMKWPLLDVPSSATVKDTRSPSPAHLSNKVPVVQHPHHMHPLTPLITYSNDHFSPASPPTHLSPEIDPKTGIPRPPHPSELSPYYPLSPGAVGQIPHPLGWLVPQQGQPMYSLPPGGFRHPYPALAMNASMSSLVSSRFPHMVAPAHPGLPTSGIPHPAIVSPIVKQEPAAPSLSPAVSAKSPVTVKKEEEKKPHVKKPLNAFMLYMKEMRAKVVAECTLKESAAINQILGRKWHNLSREEQAKYYELARKERQLHAQLYPTWSARDNYGKKKKRKREKQLSQTQSQQQIQEAEGALASKSKKPCIQYLPPEKPCDSPASSHGSALDSPATPSAALASPAAPAATHSEQAQPLSLTTKPEARAQLALHSAAFLSAKAAASNSSQMGSQPPLLSRPLPLGSMPAALLTSPPTFPATLHAHQALPVLQAQPLSLVTKSAH
Protein: Uncharacterized protein (Q584L0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- 60S ribosomal protein L24, putative
- Ribosome production factor 2 homolog
- 60S ribosome subunit biogenesis protein NIP7 homolog
- rRNA processing protein, putative
- Ribosome biogenesis protein, putative
- Ribosome assembly factor mrt4
Sequence:
MGILVVTHCRSADGKYTNLYLFIFLSSTSSAITDLYLNGHIGIYSEQGRVDLVRIMQSGSEKRNGQKRPRHAGEAAASSPAVALKQKKLKPKKKTDNAGEGNEDQLQQRRRQKEEKRNLPIASSSPAAAQQVKSPVLDQVQAKVPTEECRSALLVIGTYHSVMAGLLYRRRRFGLLFSIKHHVGCINAVTAGGGAKYMASAGTDERVFLFTNKSHSVQKQLKLLKKKQKRQAKRLKKGGEPCGNGGEMEETLAFAGPSAETNSGSSAEPLALRLTDLGHVSPPSEVRCMKITSNSQLMLCGCTDGQLITYRTRDWSINSAIPLHEKCISSIALHPGSNNDGGSGAALAITCSAEDHHIVVVDLLRGRLLSKWRYSTSLATAISRYRANKDNGGRDNVASPAAAQTTSDSDEPGRPVKLAKWERHDEPREVHFSPVGSYFAVLSSHALLVYETATMRAVAQYRAPSPLQPHNEMHTFCFMDEQTIMIGDESGNIRCCCGPWQGACVPGIVERRIPHGSEGGNVGVCGTNNSSGDTTGSFAAGSDASQHSGRHPTKHSTRVKALHCAGRTLFSLDAAGVAIAWNVDKGGISSNNSISASGKSSDLMLHYICSANCRGRVTTMDVLRL
Protein: UDP-glucose 4-epimerase (EC 5.1.3.2) (Q4WV46)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Interaction partners:
- Galactose-1-phosphate uridylyltransferase
- Galactokinase
- UTP--glucose-1-phosphate uridylyltransferase
- UDP-glucose 6-dehydrogenase
- UDP-glucose 6-dehydrogenase
- UDP-glucose 4-epimerase
- UDP-glucose 4-epimerase, putative
- Trehalase
- alpha,alpha-trehalase
Sequence:
MSAGSVLVTGGTGYIGSFTTLALLEAGYKVVVTDNLYNSSVEALNRIELICGKKAEFVQLDVTDEAGFDKVFEAHPDIDSVIHFAALKAVGESGERPLDYYMVNVYGTLCLLRSMVRHNVTNIVFSSSATVYGDATRFPNMIPIPEECPLGPTNPYGNTKFAVETAITDVINAQRNNATKAGKADEAEKWNAALLRYFNPAGAHPSGIMGEDPQGVPYNLLPLLAQVATGKREKLLVFGDDYASHDGTAIRDYIHILDLADGHLKALNYLRANNPGVRAWNLGTGKGSTVYEMIRAFSAAVGRDLPYEVAPRRAGDVLNLTSNPTRANKELGWKAQRTLEQACEDLWRWTKNNPQGYRQQPPAELLEQLKK
Protein: Proteasome subunit beta type-7 (EC 3.4.25.1) (Macropain chain Z) (Multicatalytic endopeptidase complex chain Z) (Proteasome subunit Z) (Proteasome subunit beta-2) (beta-2) (P70195)
Organism: Mus musculus (Mouse)
Function: Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). Within the 20S core complex, PSMB7 displays a trypsin-like activity.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q99436}. Nucleus {ECO:0000250|UniProtKB:Q99436}. Note=Translocated from the cytoplasm into the nucleus following interaction with AKIRIN2, which bridges the proteasome with the nuclear import receptor IPO9. {ECO:0000250|UniProtKB:Q99436}.
Interaction partners:
- Proteasome subunit alpha type-2
- Proteasome subunit alpha type-6
- Proteasome subunit alpha type-7
- Proteasome subunit alpha type-3
- Proteasome subunit beta type-2
- Proteasome subunit alpha type-1
- Proteasome subunit beta type-5
- Proteasome subunit beta type-3
- Proteasome subunit beta type-1
- Proteasome subunit alpha type-4
Sequence:
MAAVSVFQPPVGGFSFDNCRRNAVLEADFAKKGFKLPKARKTGTTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLTTGRLPRVVTANRMLKQMLFRYQGYIGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKKLVSEAIAAGIFNDLGSGSNIDLCVISKSKLDFLRPFSVPNKKGTRLGRYRCEKGTTAVLTEKVTPLEIEVLEETVQTMDTS
Protein: GH22790p (Sine oculis-binding protein, isoform A) (Sine oculis-binding protein, isoform B) (Q95TY2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSFLDVRCFGKSIARKLKRACESRKANFSPESYIPHPVEMSAKTSPSSTSRDANVGSSSAIPVQIKKELPSDEIKEFAHNTMNELLGWYGFEGVDVDRLDLTAKTSRLLQSAAAAAVANQQSHQLHQLEPHPNLERKRTSLLRSSSRSSLAAAYHNNNNNNNNNNNGSSSKNNGGVGGVGVGSGRKSGLMNCSSTTTTPSDHDTRSSREEDSKSPHSIGKPAGAAHTDEKIDFSNCCWCHRPIAENAPDYLTSCDGPRYCSESCFAQSRRASFKKAKTCDWCKHVRHAVSYVDFQDGASQLQFCSEKCLNQYKMQIFCHETQAHLDMHPHLRDQAMDAGSEAGLITPDLWLRNCRSRSASPASTLSVSPGPPPAPAVSRCPDSPPSHHPSKPLISVAPVSKLLAQKSPGPGPGAPPPPPPPVQRHLAGKLGRRKRRGISSSLGSETVASLLQKQQQQQAPQQHQAPPTLTADFGGSSVPLPPLSPMPSMQEAPQQQQAPQVPPTQALPRGPTAIPASYFATPSNGVPMGHPFAGRPPPPPHHFMHPPPHGMMPRGFGPHFGPPLPPQMPELGSLLGAVPPVTVMVPYPIIIPLPIPIPVPLPVIDFYKAHLTPEERKRFDEQRAAPTRAENAEEQEQPQPLDCSKSRSELEEEKPDVEKLSEPGQELDNDQEEDEKESIPKTNPDGDTNAASPSISQESSSSPQQTHCIVRDSTQSEPEADNQKLPKLKITRLQTKRTLIQTKEAAAECSRPLRKRKRIIDCDFQKMGLKEPEMANDGEQSNGSSNKEADADPEAECNMSGSHSNSGSAKAKK
Protein: N-acetylgalactosamine permease IID component (EIID-Aga) (PTS system N-acetylgalactosamine-specific EIID component) (P42911)
Organism: Escherichia coli (strain K12)
Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane. This system is involved in N-acetylgalactosamine transport.
Subcellular location: Cell inner membrane {ECO:0000255|PROSITE-ProRule:PRU00431, ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00431, ECO:0000269|PubMed:15919996}.
Interaction partners:
- N-acetylgalactosamine-specific phosphotransferase enzyme IIB component 1
- N-acetylgalactosamine permease IIC component 1
- Putative deaminase AgaI
- PTS system mannose-specific EIIC component
- N-acetylgalactosamine-specific phosphotransferase enzyme IIB component 2
- Putative D-galactosamine-6-phosphate deaminase AgaS
- Phosphocarrier protein HPr
- PTS system mannose-specific EIIAB component
- D-tagatose-1,6-bisphosphate aldolase subunit KbaY
- Putative phosphotransferase enzyme IIA component YadI
Sequence:
MGSEISKKDITRLGFRSSLLQASFNYERMQAGGFTWAMLPILKKIYKDDKPGLSAAMKDNLEFINTHPNLVGFLMGLLISMEEKGENRDTIKGLKVALFGPIAGIGDAIFWFTLLPIMAGICSSFASQGNLLGPILFFAVYLLIFFLRVGWTHVGYSVGVKAIDKVRENSQMIARSATILGITVIGGLIASYVHINVVTSFAIDNTHSVALQQDFFDKVFPNILPMAYTLLMYYFLRVKKAHPVLLIGVTFVLSIVCSAFGIL
Protein: Small ribosomal subunit protein eS28B (40S ribosomal protein S28-B) (S33) (P0CT80)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein eS27
- Small ribosomal subunit protein uS14
- Small ribosomal subunit protein uS19B
- Small ribosomal subunit protein uS15
- Elongation factor 3
- mRNA export factor elf1
- Small ribosomal subunit protein eS21
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS5
Sequence:
MDSSKVPVKLAKVIKVLGRTGSRGGVTQVRVEFMDDTSRSIIRNVKGPVREDDILVLLESEREARRLR
Protein: Cytochrome P450, family 708, subfamily A, polypeptide 2 (F4K051)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MDRRGKYWAGPMWIGLSMCGSGSDTILECRLRLFKLQRQNQMSFVWSAAVWVIAVAAVVISKWLYRWSNPKCNGKLPPGSMGLPIIGETCDFFEPHGLYEISPFVKKRMLKYGPLFRTNIFGSNTVVLTEPDIIFEVFRQENKSFVFSYPEAFVKPFGKENVFLKHGNIHKHVKQISLQHLGSEALKKKMIGEIDRVTYEHLRSKANQGSFDAKEAVESVIMAHLTPKIISNLKPETQATLVDNIMALGSEWFQSPLKLTTLISIYKVFIARRYALQVIKDVFTRRKASREMCGDFLDTMVEEGEKEDVIFNEESAINLIFAILVVAKESTSSVTSLAIKFLAENHKALAELKREHAAILQNRNGKGAGVSWEEYRHQMTFTNMVINETLRMANMAPIMYRKAVNDVEIKGYTIPAGWIVAVIPPAVHFNDAIYENPLEFNPWRWEGKELRSGSKTFMVFGGGVRQCVGAEFARLQISIFIHHLVTTYDFSLAQESEFIRAPLPYFPKGLPIKISQSL