wanglab/gogpt-training-data huggingface dataset:
Protein: Polyribonucleotide nucleotidyltransferase 1, mitochondrial (EC 2.7.7.8) (3'-5' RNA exonuclease OLD35) (PNPase old-35) (Polynucleotide phosphorylase 1) (PNPase 1) (Polynucleotide phosphorylase-like protein) (Q8K1R3)
Organism: Mus musculus (Mouse)
Function: RNA-binding protein implicated in numerous RNA metabolic processes. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'-to-5' direction. Mitochondrial intermembrane factor with RNA-processing exoribonulease activity. Component of the mitochondrial degradosome (mtEXO) complex, that degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality in an ATP-dependent manner. Involved in the degradation of non-coding mitochondrial transcripts (MT-ncRNA) and tRNA-like molecules (By similarity). Required for correct processing and polyadenylation of mitochondrial mRNAs. Plays a role as a cytoplasmic RNA import factor that mediates the translocation of small RNA components, like the 5S RNA, the RNA subunit of ribonuclease P and the mitochondrial RNA-processing (MRP) RNA, into the mitochondrial matrix. Plays a role in mitochondrial morphogenesis and respiration; regulates the expression of the electron transport chain (ETC) components at the mRNA and protein levels. In the cytoplasm, shows a 3'-to-5' exoribonuclease mediating mRNA degradation activity; degrades c-myc mRNA upon treatment with IFNB1/IFN-beta, resulting in a growth arrest in melanoma cells. Regulates the stability of specific mature miRNAs in melanoma cells; specifically and selectively degrades miR-221, preferentially. Also plays a role in RNA cell surveillance by cleaning up oxidized RNAs. Binds to the RNA subunit of ribonuclease P, MRP RNA and miR-221 microRNA.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q8TCS8}. Mitochondrion matrix {ECO:0000250|UniProtKB:Q8TCS8}. Mitochondrion intermembrane space {ECO:0000269|PubMed:16966381}; Peripheral membrane protein {ECO:0000269|PubMed:16966381}.
Interaction partners:
- ATP-dependent RNA helicase SUPV3L1, mitochondrial
- ATP-dependent RNA helicase A
- Exosome complex component RRP41
- Elongation factor 2
- Exosome complex component 10
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein uL2
- Large ribosomal subunit protein uL1
- Exosome complex exonuclease RRP44
- Small ribosomal subunit protein uS12
Sequence:
MAACRLCCLCPCLRPLGCGPLGRPGRNRALSYLQMRALWSSTGSRAVTVDLGHRKLEISSGKLARFADGCAVIQSGDTAVMVTAVSKTKASPSQFMPLVVDYRQKAAAAGRIPTNYLRREIGSSDREVLTSRVIDRSIRPLFPAGYFYDTQVLCNLLAVDGINEPDILAVNGASVALSLSDIPWNGPVGAVRIGMIDGECVVNPTRREMSSSTLNLVVAGAPKSQIVMLEASAENILQQDFCHAIKVGVKYTQQIIQGIQQLVKEIGVAKRTPQKIFTPSAEIVKYTKIIAMEKLYAVFTDYEHDKVSRDEAVNKIRLDTEEHLKEKFPEVDQFEIIESFNIVAKEVFRSIILNEYKRCDGRDLTSLRNISCEVDMFKTLHGSALFQRGQTQVLCTVTFDSLESSIKSDQIITAINGVKDKNFMLHYEFPPYATNETGKVTGVNRRELGHGALAEKALCPVIPKDFPFTIRVTSEVLESNGSSSMASACGGSLALMDAGVPISSAVAGVAVGLVTKTNPEKGEIEDYRLLTDILGIEDYNGDMDFKIAGTNKGITALQADIKLPGVPIKIIMEAIQQASVAKKEILQIMNKTISKPRASRKENGPVVETVKVPLSKRAKFVGPGGYHLKKLQAETGVTISQVDEETFSIFAPTPTAMHEARDFITEICRDDQEQQLEFGAVYTATITEIRDTGVMVKLYPNMTAVLLHNSQLDQRKIKHPTALGLEVGQEIQVKYFGRDPADGRMRLSRKVLQSPATTALKTLNDRSSIVMGEPVSQSSNSNP
Protein: DNA-binding protein K10 (Female sterile protein K10) (P13468)
Organism: Drosophila melanogaster (Fruit fly)
Function: May have a regulatory function.
Subcellular location: Nucleus.
Interaction partners:
- FI21960p1
- Protein spire
- Protein cappuccino
- Protein gurken
- Egalitarian, isoform B
- FI20148p1
Sequence:
MVSKNQFYQNWTMQSQQQHPHQMQQQFQQQQQPNLQHRNNQSNNNNCNNNPRAAAAPYRKPFRSGKINSGPGGNGNGNRVNGNNQMMFSSSQMPSDPLYIDFSSPPPGFKHNQVGSPKKKSMKGIKQQQHPSPNQQQPPSPNQQQHPSPNQQQHPSPNQQQHPNSNQQQHLSPNQQQGKMNNQNNNHMNQSQQPFNNQMNGSDWQRHPGNNPNQIRGGFNGFQRGPPPNRPPPRLMMGPPMGPMGPGPRGPGPMGPGGPYPQMPFPPPVPGMRGPGPMGPMGGPPPPPPPLFMRRNGPGPGPMMGVPPPMHMMGPRMPPRGIPPVGPYGPMNMNGGRIMKPNPKLIKQVVKGKSSIKTLKNLINQYPIEKPWVTDEIRSEHDKKVDIENRLKGHKDDELFAQYKGQRDKFVSLYEAAREEYLKQEAATVKAKDAKSDKDKNAISSQSAAPKAGSAKDATIPNP
Protein: B3 domain-containing transcription factor NGA3 (Protein NGATHA3) (Q9MAN1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Regulates lateral organ growth. Functionally redundant with NGA1, NGA2 and NGA4.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00326}.
Interaction partners:
- AP-5 complex subunit beta-like protein
- Protein SHI RELATED SEQUENCE 1
- Protein SHORT INTERNODES
- Tubby-like F-box protein 1
- B3 domain-containing protein At4g34400
- Tetraspanin-13
- Transcription factor IND
- Peroxidase 6
Sequence:
MDLSLAPTTTTSSDQEQDRDQELTSNIGASSSSGPSGNNNNLPMMMIPPPEKEHMFDKVVTPSDVGKLNRLVIPKQHAERYFPLDSSNNQNGTLLNFQDRNGKMWRFRYSYWNSSQSYVMTKGWSRFVKEKKLDAGDIVSFQRGIGDESERSKLYIDWRHRPDMSLVQAHQFGNFGFNFNFPTTSQYSNRFHPLPEYNSVPIHRGLNIGNHQRSYYNTQRQEFVGYGYGNLAGRCYYTGSPLDHRNIVGSEPLVIDSVPVVPGRLTPVMLPPLPPPPSTAGKRLRLFGVNMECGNDYNQQEESWLVPRGEIGASSSSSSALRLNLSTDHDDDNDDGDDGDDDQFAKKGKSSLSLNFNP
Protein: Uncharacterized protein C1142.09 (Q9P7F5)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
Sequence:
MEDSLLLSVNISDSLFTFSLKPLFSQYRKHIYFNDCFYSTFNKTKTIIVVILSGKLSDLIDFKSYIEFVLKTNNSYSAILISYYRCIFIISLFHRPLTIHFLTNLTHGCTRSFTK
Protein: Small ubiquitin-related modifier 5 (AtSUMO5) (Q8VZI7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Ubiquitin-like protein which can be covalently attached to target lysines as a monomer. Does not seem to be involved in protein degradation and may function as an antagonist of ubiquitin in the degradation process (By similarity).
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
Interaction partners:
- SUMO-conjugating enzyme SCE1
- SUMO-activating enzyme subunit 2
- E3 SUMO-protein ligase SIZ1
- SUMO-activating enzyme subunit 1B-1
- SUMO-activating enzyme subunit 1A
- E4 SUMO-protein ligase PIAL1
- E4 SUMO-protein ligase PIAL2
- Ubiquitin-like-specific protease ESD4
- E3 SUMO-protein ligase MMS21
- Structural maintenance of chromosomes protein 5
Sequence:
MVSSTDTISASFVSKKSRSPETSPHMKVTLKVKNQQGAEDLYKIGTHAHLKKLMSAYCTKRNLDYSSVRFVYNGREIKARQTPAQLHMEEEDEICMVMELGGGGPYTP
Protein: Error-prone DNA polymerase (EC 2.7.7.7) (P9WNT5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: DNA polymerase involved in damage-induced mutagenesis and translesion synthesis (TLS). It is not the major replicative DNA polymerase. Does not appear to be essential for chromosomal replication. May be involved in generating antibiotic resistance.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Uncharacterized protein Rv3395c
- UmuC domain-containing protein
- Beta sliding clamp
- Probable DNA polymerase III subunit delta
- Protein RecA
- Putative bifunctional exonuclease/endonuclease protein Rv2191
- DNA polymerase IV 1
- LexA repressor
- Single-stranded DNA-binding protein
- Single-stranded DNA-binding protein
Sequence:
MFDILWNVGWSNGPPSWAEMERVLNGKPRHAGVPAFDADGDVPRSRKRGAYQPPGRERVGSSVAYAELHAHSAYSFLDGASTPEELVEEAARLGLCALALTDHDGLYGAVRFAEAAAELDVRTVFGAELSLGATARTERPDPPGPHLLVLARGPEGYRRLSRQLAAAHLAGGEKGKPRYDFDALTEAAGGHWHILTGCRKGHVRQALSQGGPAAAQRALADLVDRFTPSRVSIELTHHGHPLDDERNAALAGLAPRFGVGIVATTGAHFADPSRGRLAMAMAAIRARRSLDSAAGWLAPLGGAHLRSGEEMARLFAWCPEAVTAAAELGERCAFGLQLIAPRLPPFDVPDGHTEDSWLRSLVMAGARERYGPPKSAPRAYSQIEHELKVIAQLRFPGYFLVVHDITRFCRDNDILCQGRGSAANSAVCYALGVTAVDPVANELLFERFLSPARDGPPDIDIDIESDQREKVIQYVYHKYGRDYAAQVANVITYRGRSAVRDMARALGFSPGQQDAWSKQVSHWTGQADDVDGIPEQVIDLATQIRNLPRHLGIHSGGMVICDRPIADVCPVEWARMANRSVLQWDKDDCAAIGLVKFDLLGLGMLSALHYAKDLVAEHKGIEVDLARLDLSEPAVYEMLARADSVGVFQVESRAQMATLPRLKPRVFYDLVVEVALIRPGPIQGGSVHPYIRRRNGVDPVIYEHPSMAPALRKTLGVPLFQEQLMQLAVDCAGFSAAEADQLRRAMGSKRSTERMRRLRGRFYDGMRALHGAPDEVIDRIYEKLEAFANFGFPESHALSFASLVFYSAWFKLHHPAAFCAALLRAQPMGFYSPQSLVADARRHGVAVHGPCVNASLAHATCENAGTEVRLGLGAVRYLGAELAEKLVAERTANGPFTSLPDLTSRVQLSVPQVEALATAGALGCFGMSRREALWAAGAAATGRPDRLPGVGSSSHIPALPGMSELELAAADVWATGVSPDSYPTQFLRADLDAMGVLPAERLGSVSDGDRVLIAGAVTHRQRPATAQGVTFINLEDETGMVNVLCTPGVWARHRKLAHTAPALLIRGQVQNASGAITVVAERMGRLTLAVGARSRDFR
Protein: Aldo-keto reductase 1B (EC 1.1.1.21) (EC 1.1.1.300) (EC 1.1.1.372) (EC 1.1.1.54) (Aldose reductase) (dAR1) (M9PF61)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:38283991}.
Interaction partners:
Sequence:
MNTLMKIQLVRPVFRITLRNYGKPERFMWCQKEYARAPKVVCLDGNEIPVIGLGTFNSPKGQVTEAVKVAIDAGYRHIDCAYVYQNEDEVGDGVEAKIKEGVVKREDLFITSKLWNTFHRPDLVKSALENTLSSLKLKYLDLYLIHWPMGYKEGCDLFPTDKDGKTLYSPVDYVDTWKAMEKLVEEGLVKSIGVSNFNRRQIERVLEVATIPPVTNQIECHPYLTQKKLIDFCKSKDITITAYSPLGSPNRPWAKAGDPVILEEAKIKEIAAKKKKTPGQILIRYQVQRANIVIPKSVTKDRIESNFQVFDFELTPEEIEIIESFECNGRLVPLLNQYGHPHHPFEKDEY
Protein: Probable transcriptional regulator (Q9HU98)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Probable transcriptional regulator
- Probable transcriptional regulator
- Probable transcriptional regulator
- Probable transcriptional regulator
- Probable transcriptional regulator
- Probable transcriptional regulator
- Probable transcriptional regulator
- Probable transcriptional regulator
- Probable transcriptional regulator
- Probable transcriptional regulator
Sequence:
MNKDGQGINPGYGLAPMKLRHIEVFQAIRQAGSVSGAAQLLHVSQPAVSKVLQHAEQQLGFPLFLRVRGKLLATPEALELEREVAKLSDSLQAVRRLAQNLRRQPGHSLRIGATPALALSLLPRAIGEWSARYPQSGCELATLHSRELVQGLLMRELDLALSLKQPEHPGLRGEAIASGVLVALAPREHWPEAERRQPLSLAGLAGEALIGLSTADPLFARLEDYLSAVEPPPQVKIAVQTYALARALVEAGAGLALVDPFTALGADPHSTAIRPLSPAFPVTLYAITRADETPPHTLAPLLRMLARQAEERLRAVQM
Protein: Ubiquitin-fold modifier 1 (P61960)
Organism: Homo sapiens (Human)
Function: Ubiquitin-like modifier which can be covalently attached via an isopeptide bond to lysine residues of substrate proteins as a monomer or a lysine-linked polymer. The so-called ufmylation, requires the UFM1-activating E1 enzyme UBA5, the UFM1-conjugating E2 enzyme UFC1, and the UFM1-ligase E3 enzyme UFL1. Ufmylation is involved in reticulophagy (also called ER-phagy) induced in response to endoplasmic reticulum stress. Ufmylation of TRIP4 regulates nuclear receptors-mediated transcription.
Subcellular location: Nucleus {ECO:0000269|PubMed:15071506}. Cytoplasm {ECO:0000269|PubMed:15071506}.
Interaction partners:
- Ubiquitin-like modifier-activating enzyme 5
- Ubiquitin-fold modifier-conjugating enzyme 1
- Ufm1-specific protease 2
- Ufm1-specific protease 1
- E3 UFM1-protein ligase 1
- DDRGK domain-containing protein 1
- Ubiquitin-related modifier 1
- NEDD8-conjugating enzyme Ubc12
- Ubiquitin-like protein NEDD8
- Gamma-aminobutyric acid receptor-associated protein-like 2
Sequence:
MSKVSFKITLTSDPRLPYKVLSVPESTPFTAVLKFAAEEFKVPAATSAIITNDGIGINPAQTAGNVFLKHGSELRIIPRDRVGSC
Protein: Fgf23 (Fibroblast growth factor 23) (Q5MK87)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MRCALSNLHMLHSSVLALWFTALQGLRPADAAPNPSPLLGSNWGNPRRYIHLQTTSDLNNYYLEISPSGHVRKTTNRGSYSVILLKTESRDRLAIFGVKSNRFLCMDTGGTLFTSTICNKEDCLFHHKLLENHRDVYYSTKHSILLNLDGAKQAFIAGQNLPQSSLFLSEKNTVPLERLQHRERRNRQVNPTDPLNALRYAEESDSRAAQEDDGDMDFEPSEGQNISRETLVSPSDDDPWDLLHDTSPGSPRIAAIVG
Protein: ATP-dependent RNA helicase dbp5 (EC 3.6.4.13) (Q09747)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: ATP-dependent RNA helicase associated with the nuclear pore complex and essential for mRNA export from the nucleus. May participate in a terminal step of mRNA export through the removal of proteins that accompany mRNA through the nucleopore complex. May also be involved in early transcription (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus, nuclear pore complex. Nucleus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Nuclear pore complex cytoplasmic fibrils. {ECO:0000250}.
Interaction partners:
- mRNA export factor gle1
- Nucleoporin nup146
- mRNA export factor mex67
- Poly
Sequence:
MSTTLGQESKTDWASLDSDEEVQRISDKVNQLNTSENKNEDQKATNLSDRLGPKITENVDAKSEQDKATNTIAEDANTKQSENDESNLIPNKNEVRVKLADLQADPNSPLFSVKSFEELELKPELLKGIYSMKFQKPSKIQEKALPLLLSNPPRNMIGQSQSGTGKTAAFALTMLSRVDASVPKPQAICLAPSRELARQIMDVVTEMGKYTEVKTAFGIKDSVPKGAKIDAQIVIGTPGTVMDLMKRRQLDARDIKVFVLDEADNMLDQQGLGDQSMRIKHLLPRNTQIVLFSATFSERVEKYAERFAPNANEIRLKTEELSVEGIKQLYMDCQSEEHKYNVLVELYGLLTIGQSIIFCKKKDTAEEIARRMTADGHTVACLTGNLEGAQRDAIMDSFRVGTSKVLVTTNVIARGIDVSQVNLVVNYDMPLDQAGRPDPQTYLHRIGRTGRFGRVGVSINFVHDKKSWEEMNAIQEYFQRPITRVPTDDYEELEKVVKNALKM
Protein: Cyclin-D3-3 (G1/S-specific cyclin-D3-3) (CycD3;3) (Q9SN11)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Promotes divisions in the guard cells (GCs) after the guard mother cells (GMC) symmetric division.
Interaction partners:
- Retinoblastoma-related protein 1
- Cyclin-dependent kinase A-1
- Cyclin-D3-2
- Cyclin-D3-1
- Cyclin-dependent kinase B2-1
- Transcription factor E2FA
- Dof zinc finger protein DOF3.4
- Cyclin-dependent kinase B1-1
- Cyclin-dependent kinase B2-2
- Cyclin-dependent kinases regulatory subunit 2
Sequence:
MALEEEEESQNAPFCVLDGLFCEEESEFHEQVDLCDESVEKFPFLNLGLSDHDMLWDDDELSTLISKQEPCLYDEILDDEFLVLCREKALDWIFKVKSHYGFNSLTALLAVNYFDRFITSRKFQTDKPWMSQLTALACLSLAAKVEEIRVPFLLDFQVEEARYVFEAKTIQRMELLVLSTLDWRMHPVTPISFFDHIIRRYSFKSHHQLEFLSRCESLLLSIIPDSRFLSFSPSVLATAIMVSVIRDLKMCDEAVYQSQLMTLLKVDSEKVNKCYELVLDHSPSKKRMMNWMQQPASPIGVFDASFSSDSSNESWVVSASASVSSSPSSEPLLKRRRVQEQQMRLSSINRMFFDVLSSSPR
Protein: MARVEL domain-containing protein (O44511)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- C2 domain-containing protein
- C2 domain-containing protein
- C2 domain-containing protein
- C2 domain-containing protein
- C2 domain-containing protein
- Synaptotagmin-1
- ATP-grasp domain-containing protein
- Synaptotagmin 2
- MoaB/Mog domain-containing protein
- Syntaxin-1A homolog
Sequence:
MPSIPAQLNISAFKFPLGFIRIIQFVFIIIAIAAINSWGLELNYHCVDGTGNITRNSTQKVYTFSLSKVKLTGCDNQTRTFWSGDDSASGSAGFFYFVNVTALIYVIFICFVYVIFWNIYQTEKRIPLVDLGATALLFILFFFCSSIWWAGANTIGNATSDERLTELFGQGSWKGQNAQFLSRDVNNGKLAISVLANWVCVLCFAFNCWFIWKEVVPRDSSNPSDIA
Protein: Voltage-dependent calcium channel subunit alpha-2/delta-2 (Voltage-gated calcium channel subunit alpha-2/delta-2) [Cleaved into: Voltage-dependent calcium channel subunit alpha-2-2; Voltage-dependent calcium channel subunit delta-2] (Q8CFG6)
Organism: Rattus norvegicus (Rat)
Function: The alpha-2/delta subunit of voltage-dependent calcium channels regulates calcium current density and activation/inactivation kinetics of the calcium channel. Acts as a regulatory subunit for P/Q-type calcium channel (CACNA1A), N-type (CACNA1B), L-type (CACNA1C OR CACNA1D) and possibly T-type (CACNA1G). Overexpression induces apoptosis (By similarity).
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Colocalizes with CACNA1A in lipid raft fractions. {ECO:0000250}.
Interaction partners:
- Voltage-dependent L-type calcium channel subunit alpha-1C
- Voltage-dependent L-type calcium channel subunit beta-2
- Voltage-dependent calcium channel gamma-1 subunit
- Voltage-dependent L-type calcium channel subunit alpha-1D
- Voltage-dependent R-type calcium channel subunit alpha-1E
- Voltage-dependent P/Q-type calcium channel subunit alpha-1A
- Voltage-dependent N-type calcium channel subunit alpha-1B
- Voltage-dependent L-type calcium channel subunit beta-4
- Voltage-dependent L-type calcium channel subunit beta-1
- Voltage-dependent L-type calcium channel subunit beta-3
Sequence:
MAVPARTCGASWPGPVRTARPWPGRGPRPCPDPRGPASGPARPLLLLLPPLLLLPLLTAPGASAYSFPQQHTMQHWARRLEQEIDGVMRIFGGVQQLREIYKDNRNLFDVQENEPQKLVEKVAGDIESLLDRKVQALKRLADAAENFQKAHRWQDNIKEEDIMYYDAKADAELDDPESEDMERGSKTSALRLDFIEEPNFKNKVNYSYTAVQIPTDIYKGSTVILNELNWTEALENVFIENRRQDPTLLWQVFGSATGVTRYYPATPWRAPKKIDLYDVRRRPWYIQGASSPKDMVIIVDVSGSVSGLTLKLMKTSVCEMLDTLSDDDYVNVASFNEKAQPVSCFTHLVQANVRNKKVFKEAVQGMVAKGTTGYKAGFEYAFDQLQNSNITRANCNKMIMMFTDGGEDRVQDVFEKYNWPNRTVRVFTFSVGQHNYDVTPLQWMACTNKGYYFEIPSIGAIRINTQEYLDVLGRPMVLAGKDAKQVQWTNVYEDALGLGLVVTGTLPVFNLTQDGPGDKKNQLILGVMGIDVALNDIKRLTPNYTLGANGYVFAIDLNGYVLLHPNLKPQITNFREPVTLDFLDAELEDENKEEIRRSMIDGDKGHKQIRTLVKSLDERYIDEVIRNYTWVPIRSTNYSLGLVLPPYSTYYLQANLSDQILQVKLPISKLKDFEFLLPSSFESEGHVFIAPREYCKDLNASDNNTEFLKNFIELMEKVTPDSKQCNNFLLHNLILDTGITQQLVERVWRDQDLNTYSLLAVFAATDGGITRVFPNKAAEDWTENPEPFNASFYRRSLDNRGYIFKPPHQDSLLRPLELENDTVGVLVSTAVELSLGRRTLRPAVVGVKLDLEAWAEKFKVLASNRTHQDQPQKQCGPSSHCEMDCEVNNEDLLCVLIDDGGFLVLSNQNHQWDQVGRFFSEVDANLMLALYNNSFYTRKESYDYQAACAPQPPGNLGAAPRGVFVPTIADFLNLAWWTSAAAWSLFQQLLYGLIYHSWFQADPAEAEGSPETRESSCVMKQTQYYFGSVNASYNAIIDCGNCSRLFHAQRLTNTNLLFVVAEKPLCSQCEVGRLLQKETHCPADGPEQCELVQRPRYRTGPHICFDYNATEDTSDCGRGASFPPSLGVLVSLQLLLLLGLPPRPQPQIHSFTPSRRL
Protein: N-alpha-acetyltransferase 50 (hNaa50p) (EC 2.3.1.258) (N-acetyltransferase 13) (N-acetyltransferase 5) (hNAT5) (N-acetyltransferase san homolog) (hSAN) (N-epsilon-acetyltransferase 50) (EC 2.3.1.-) (NatE catalytic subunit) (Q9GZZ1)
Organism: Homo sapiens (Human)
Function: N-alpha-acetyltransferase that acetylates the N-terminus of proteins that retain their initiating methionine. Has a broad substrate specificity: able to acetylate the initiator methionine of most peptides, except for those with a proline in second position. Also displays N-epsilon-acetyltransferase activity by mediating acetylation of the side chain of specific lysines on proteins. Autoacetylates in vivo. The relevance of N-epsilon-acetyltransferase activity is however unclear: able to acetylate H4 in vitro, but this result has not been confirmed in vivo. Component of N-alpha-acetyltransferase complexes containing NAA10 and NAA15, which has N-alpha-acetyltransferase activity. Does not influence the acetyltransferase activity of NAA10. However, it negatively regulates the N-alpha-acetyltransferase activity of the N-terminal acetyltransferase A complex (also called the NatA complex). The multiprotein complexes probably constitute the major contributor for N-terminal acetylation at the ribosome exit tunnel, with NAA10 acetylating all amino termini that are devoid of methionine and NAA50 acetylating other peptides. Required for sister chromatid cohesion during mitosis by promoting binding of CDCA5/sororin to cohesin: may act by counteracting the function of NAA10.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16507339, ECO:0000269|PubMed:17502424, ECO:0000269|PubMed:25732826, ECO:0000269|PubMed:27422821}. Nucleus {ECO:0000269|PubMed:25732826}. Note=Localizes to the cytoplasm in interphase cells (PubMed:17502424). {ECO:0000269|PubMed:17502424}.
Interaction partners:
- N-alpha-acetyltransferase 15, NatA auxiliary subunit
- N-alpha-acetyltransferase 10
- Huntingtin-interacting protein K
- N-alpha-acetyltransferase 16, NatA auxiliary subunit
- N-alpha-acetyltransferase 11
- N-alpha-acetyltransferase 20
- N-alpha-acetyltransferase 35, NatC auxiliary subunit
- N-alpha-acetyltransferase 40
- N-alpha-acetyltransferase 25, NatB auxiliary subunit
- N-alpha-acetyltransferase 38, NatC auxiliary subunit
Sequence:
MKGSRIELGDVTPHNIKQLKRLNQVIFPVSYNDKFYKDVLEVGELAKLAYFNDIAVGAVCCRVDHSQNQKRLYIMTLGCLAPYRRLGIGTKMLNHVLNICEKDGTFDNIYLHVQISNESAIDFYRKFGFEIIETKKNYYKRIEPADAHVLQKNLKVPSGQNADVQKTDN
Protein: Peptide methionine sulfoxide reductase A3 (AtMSRA3) (EC 1.8.4.11) (Peptide-methionine (S)-S-oxide reductase) (Peptide Met(O) reductase) (Protein-methionine-S-oxide reductase) (Q9LY14)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the reduction of methionine sulfoxide (MetSO) to methionine in proteins. Plays a protective role against oxidative stress by restoring activity to proteins that have been inactivated by methionine oxidation. May prevent cellular oxidative damage due to light exposure. MSRA family specifically reduces the MetSO S-enantiomer.
Subcellular location: Cytoplasm, cytosol.
Interaction partners:
- Peptide methionine sulfoxide reductase B1, chloroplastic
- Peptide methionine sulfoxide reductase B2, chloroplastic
- Peptide methionine sulfoxide reductase B8
- Peptide methionine sulfoxide reductase B3
- Peptide methionine sulfoxide reductase B9
- Peptide methionine sulfoxide reductase B7
- Peptide methionine sulfoxide reductase B4
- Peptide methionine sulfoxide reductase B6
- Peptide methionine sulfoxide reductase B5
- Protein MANNAN SYNTHESIS-RELATED 2
Sequence:
MNILNRLGLGSSGQTNMDPSPIAQGNDDDTPAPGNQFAQFGAGCFWGVELAFQRVPGVTQTEAGYTQGTVDNPSYGDVCSGTTGHSEVVRVQYDLNDCTYESLLDLFWSRHDPTTLNRQGNDVGTQYRSGIYFYTPEQEKLARESLERHQQQMERKIMTEILPAKKFYRAEEHHQQYLSKGGRFGQGQSTAKGCNDPIRCYG
Protein: Trichohyalin (Q383R7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSQSRHLNNFLCLKGKLLEGRCLCARGNPECALFSLRRSKRLTTSCICACDERFALTEAVAVEMSLNRKYSSAKDRGPTIVIPNIPKITDIRSRGKLMCEYEKYEAELFKHHLGPPDTTCTMSVKQAPTDFDRRVPGMDEPTAADLLHERRKTRGGARWGLEKRFGAPVFAAGGTGGNTSTKQQAAGRHGSVPYSAADGGNSRGALPAVPSVTPLDVSTNNPPNQQGTAGNNRDNTSTYSPLSIRAPEEDPEDVLSSSARRRGTKGQRVSLQVPRRPPQGADPTVKIEEAEGKEPLGRTQEGKSKGGRRFRSLPRRAPLRVQSPLFDTEFLAPGGCNWTVCTGQDYSSWNAEHCAEVLRVLLKPPPEYGESFKVDMSHTDLRWMWNGRMPKNFTSLQSWRVEEVKGRVVPVVNSPRSALVMLRCGITVPDLLVHEIGDDAPLLPTDPEDRTMVKSIRMKQHKASVISILEQVRNEYCSLCCAVSLPDLVEAFRRKRQVNIEVAKSAMIRDALEKQKRLFECAERKLEVEANRAKNLQERERLIELRNERLQEMMMEKVRRKREEDLIAQQNAAARIKLQQERNAEREKEYQRELQERLERAEERTARQQAARDHLLEQRRIRRKKNAEERQARIERMAEMQEQQSEILRRKYEERDAKVQLVQEERERKQREAQELLAARAAKSQELREQARQRALLREEEVRQAALGQQQEVENRLRQLTKQREEEVAERAKKEAEKRERLKGVLTLTAEKQISLKEVSLKKQEKFKERHDEIQRHQAEEIMLKRERERDLMEAKAFAVLQKKRVAEFNKVEVVLQLIAKREATEALETQREMLLRENFKNHATLTQHRKSLKEDIARKKSLQG
Protein: Inactive chitinase-like protein 1 (HbCLP1) (allergen Hev b 11) (Q949H3)
Organism: Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis)
Function: Inactive chitinase-like protein that does not exhibit hydrolytic activity toward chitin. Binds strongly to chitin and possesses antifungal activity toward the fungal pathogen Altenaria alternata in plate assays. Inhibits the growth of Fusarium oxysporum on plate assays. Probably involved in defense against fungal pathogens through a mechanism that only involves carbohydrate binding.
Interaction partners:
Sequence:
MKEIVRALEGYGPPKDKAAEQCGWQAGGALCPGGLCCSQYGWCANTPEYCGSGCQSQCDGGGGGEDGGIDLGSIISRSTFEEMLKHRNDAACPAKGFYTYDAFISAAKAFPAFGTTGDVDTRKREIAAFFGQTSHATTGGWPTAPDGPYAWGYCYKEELNQASSYCSPSPAYPCAPGKKYYGRGPIQLSWNYNYGQCGQALGLDLLNNPDLVATDRVISFKAAIWFWMTPQFPKPSCHDVITGQWSPTGHDISAGRAPGYGVITNIINGGLECGRGWDARVEDRIGFYKRYCDMFAVGYGSNLDCYNQTPFGLG
Protein: Antitoxin Rv2654c (P9WJ11)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Antitoxin component of a type II toxin-antitoxin (TA) system. Upon expression in M.smegmatis neutralizes the effect of cognate toxin Rv2653c.
Interaction partners:
- Toxin Rv2653c
- Uncharacterized protein Rv2656c
- Probable PhiRv2 prophage protein
- Uncharacterized protein Rv2658c
- Putative prophage phiRv2 integrase
- Possible PhiRv2 prophage protein
Sequence:
MSGHALAARTLLAAADELVGGPPVEASAAALAGDAAGAWRTAAVELARALVRAVAESHGVAAVLFAATAAAAAAVDRGDPP
Protein: Biotin-dependent acetyl-/propionyl-coenzyme A carboxylase epsilon subunit (P96886)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Stimulates activity of the AccA3/AccD5 biotin-dependent acyl-CoA carboxylase complex. Interacts with AccD5 and modulates its carboxylase activity for acetyl-CoA and propionyl-CoA. Inhibits activity of the AccA3/AccD6 complex. Is also required for the activity of the long-chain acyl-CoA carboxylase (LCC) complex.
Interaction partners:
- Biotin-dependent acetyl-/propionyl-coenzyme A carboxylase beta5 subunit
- Biotin-dependent acyl-coenzyme A carboxylase alpha3 subunit
- Nucleoside triphosphate pyrophosphatase
- Biotin-dependent long chain acyl-coenzyme A carboxylase beta4 subunit
- Biotin-dependent acetyl-/propionyl-coenzyme A carboxylase beta6 subunit
- Biotin-dependent 3-methylcrotonyl-coenzyme A carboxylase alpha1 subunit
- Biotin--[acetyl-CoA-carboxylase] ligase
- Uncharacterized SufE-like protein Rv3284
- Putative thiosulfate sulfurtransferase SseA
- Possible carboxylase
Sequence:
MGTCPCESSERNEPVSRVSGTNEVSDGNETNNPAEVSDGNETNNPAEVSDGNETNNPAPVSRVSGTNEVSDGNETNNPAPVSRVSGTNEVSDGNETNNPAPVTEKPLHPHEPHIEILRGQPTDQELAALIAVLGSISGSTPPAQPEPTRWGLPVDQLRYPVFSWQRITLQEMTHMRR