wanglab/gogpt-training-data huggingface dataset:
Protein: Small ribosomal subunit biogenesis GTPase RsgA (EC 3.6.1.-) (P39286)
Organism: Escherichia coli (strain K12)
Function: One of at least 4 proteins (Era, RbfA, RimM and RsgA/YjeQ) that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Binds the 30S subunit contacting the head, platform, and rRNA helix 44, which may assist the last maturation stages. Removes RbfA from mature, but not immature 30S ribosomes in a GTP-dependent manner; 95% removal in the presence of GTP, 90% removal in GMP-PNP and 65% removal in the presence of GDP. Circulary permuted GTPase that catalyzes rapid hydrolysis of GTP with a slow catalytic turnover. Dispensible for viability, but important for overall fitness. The intrinsic GTPase activity is stimulated by the presence of 30S (160-fold increase in kcat) or 70S (96-fold increase in kcat) ribosomes. Mature 30S ribosomes stimulate intrinsic GTPase more than do immature 30S ribosomes. Ribosome-associated GTPase activity is stimulated by RbfA. The GTPase is inhibited by aminoglycoside antibiotics such as neomycin and paromycin streptomycin and spectinomycin. This inhibition is not due to competition for binding sites on the 30S or 70S ribosome.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01820, ECO:0000269|PubMed:14973029}. Note=Associates with 30S ribosomes (PubMed:14973029). {ECO:0000269|PubMed:14973029}.
Interaction partners:
- 30S ribosome-binding factor
- Small ribosomal subunit protein uS12
- Small ribosomal subunit protein uS13
- Thiamine-phosphate synthase
- Thiamine-monophosphate kinase
- Thiamine kinase
- Adenylate kinase
- Alkaline phosphatase
- Ribosome maturation factor RimM
- GTPase ObgE/CgtA
Sequence:
MSKNKLSKGQQRRVNANHQRRLKTSKEKPDYDDNLFGEPDEGIVISRFGMHADVESADGDVHRCNIRRTIRSLVTGDRVVWRPGKPAAEGVNVKGIVEAVHERTSVLTRPDFYDGVKPIAANIDQIVIVSAILPELSLNIIDRYLVACETLQIEPIIVLNKIDLLDDEGMAFVNEQMDIYRNIGYRVLMVSSHTQDGLKPLEEALTGRISIFAGQSGVGKSSLLNALLGLQKEILTNDISDNSGLGQHTTTAARLYHFPHGGDVIDSPGVREFGLWHLEPEQITQGFVEFHDYLGLCKYRDCKHDTDPGCAIREAVEEGKIAETRFENYHRILESMAQVKTRKNFSDTDD
Protein: Actin-related protein 2/3 complex subunit 1 (Arp2/3 complex 41 kDa subunit) (p41-Arc) (O96622)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Functions as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the pointed end of the daughter actin filament. The Arp2/3 complex is involved in organizing the actin system in cell motility and chemotaxis, in phagocytosis and macropinocytosis, at late steps of endosome processing, and in mitosis. In concert with a group of other proteins, the Arp2/3 complex plays a general role in the rapid activation and adaptation of the actin system to its multiple functions.
Subcellular location: Cytoplasm, cytoskeleton. Cell projection. Cytoplasm, cytosol. Cytoplasm, cell cortex. Cell projection, pseudopodium.
Interaction partners:
- Actin-related protein 2/3 complex subunit 4
- Actin-related protein 2/3 complex subunit 5
- Actin-related protein 3
- Actin-related protein 2/3 complex subunit 3
- Actin-related protein 2/3 complex subunit 2
- Actin-related protein 2
- Wiscott-Aldrich syndrome protein
- WASP-related protein
- ADF-H domain-containing protein
- SPIN90/Ldb17 leucine-rich domain-containing protein
Sequence:
MSAFEIEHLASCITAHAWNADRSRVALCPNNNEVHIYAKQGTSWVVEHVLAEHDQLVTSIDWAPKTNRILTSSQDRNAYVWTFKDGQWKPVLVLLRINRAATHVKWSPQENKFAVATGAKLVCICFFEEEHDWWASNHIKKHKSTVLKVDWHPNNLLLATSSSDYKVRVFDAYIKKADGRSVTRPYGEVAFGEPVFEFDQCASWVHALKWSPSGSTLAYSSHDGVFAVANFSTNPPTIEKLRVRNLPLRDLLYITENSIAGVGYDCAPLLITNQNGWKYSGEMDKASEGGAAAGSETSARKLFQNKVDLGESKSADKKLTTVHQNCITSIVPFKSVGGVVSDFSTSGLDGNIVVWHVKALEAKNKFKVI
Protein: N-alpha-acetyltransferase NAT5 (NatA complex subunit NAT5) (EC 2.3.1.258) (Q08689)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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. Non-essential component of the NatA N-terminal acetyltransferase.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- N-terminal acetyltransferase A complex catalytic subunit ARD1
- N-terminal acetyltransferase A complex subunit NAT1
- N-terminal acetyltransferase B complex catalytic subunit NAT3
- N-alpha-acetyltransferase 30
- N-terminal acetyltransferase B complex subunit MDM20
- N-alpha-acetyltransferase 35, NatC auxiliary subunit
- SAGA complex subunit SGF29
- N-alpha-acetyltransferase 40
- N-alpha-acetyltransferase 38, NatC auxiliary subunit
- SAGA complex subunit NGG1
Sequence:
MGRDICTLDNVYANNLGMLTKLAHVTVPNLYQDAFFSALFAEDSLVAKNKKPSSKKDVHFTQMAYYSEIPVGGLVAKLVPKKQNELSLKGIQIEFLGVLPNYRHKSIGSKLLKFAEDKCSECHQHNVFVYLPAVDDLTKQWFIAHGFEQVGETVNNFIKGVNGDEQDAILLKKHIS
Protein: Progesterone receptor (PR) (Nuclear receptor subfamily 3 group C member 3) (Q690N0)
Organism: Bos taurus (Bovine)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU368037}. Cytoplasm {ECO:0000256|RuleBase:RU368037}.
Interaction partners:
Sequence:
AVSGSALECVLYKAEGAPPQPGPFAPPPCKAPAAGACLLPRDLPSTSAAAAAAAGATPALYQPLGLNGLPQLGYQAAVLKEGLPQVYQPYLNYLRPDSEASQSPQYSFESLPQKICLICGDEASGCHYGVLTCGSCKVFFKRAMEGQHNYLCAGRNDCIVDKIRRKNCPACRLRKCCQAGMVLGGRKFKKFNKVRVMRTLDAVALPQPVGIPNESQALSQRITFSPSQDLQLIPPLINLLMSIEPDVVYAGHDNSKPDTSSSLLTSLNQLGERQLLSVVKWSKSLPGFRNLHIDDQITLIQYSWMSLMVFGLGWRSYKHVSGQMLYFAPDLILNEQRMKESSFYSLCLTMWQIPQEFVKLQVSQEEFLCMKVLLLLNTIPLEGLRSQNQFEEMRSSYIRELIKAIGLRQKGVVPSSQRFYQLTKLLDNLHDLVKQLHLYCLNTFIQSRALSVEFPEMMSEVIAAQLPKILAGMVKPLLFHKK
Protein: Methylthioribulose-1-phosphate dehydratase (MTRu-1-P dehydratase) (EC 4.2.1.109) (APAF1-interacting protein) (hAPIP) (Q96GX9)
Organism: Homo sapiens (Human)
Function: Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P). Functions in the methionine salvage pathway, which plays a key role in cancer, apoptosis, microbial proliferation and inflammation. May inhibit the CASP1-related inflammatory response (pyroptosis), the CASP9-dependent apoptotic pathway and the cytochrome c-dependent and APAF1-mediated cell death.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03116, ECO:0000269|PubMed:15262985, ECO:0000269|PubMed:23285211}.
Interaction partners:
- Enolase-phosphatase E1
- Methylthioribose-1-phosphate isomerase
- Apoptotic protease-activating factor 1
- Acireductone dioxygenase-requiring))
- Xylulose kinase
- Caspase-9
- Cytochrome c
- Triosephosphate isomerase
- S-methyl-5'-thioadenosine phosphorylase
Sequence:
MSGCDAREGDCCSRRCGAQDKEHPRYLIPELCKQFYHLGWVTGTGGGISLKHGDEIYIAPSGVQKERIQPEDMFVCDINEKDISGPSPSKKLKKSQCTPLFMNAYTMRGAGAVIHTHSKAAVMATLLFPGREFKITHQEMIKGIKKCTSGGYYRYDDMLVVPIIENTPEEKDLKDRMAHAMNEYPDSCAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAVSMKKVGLDPSQLPVGENGIV
Protein: Glutathione S-transferase Mu 3 (EC 2.5.1.18) (GST class-mu 3) (Glutathione S-transferase GT9.3) (P19639)
Organism: Mus musculus (Mouse)
Function: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
Subcellular location: Cytoplasm.
Interaction partners:
- Glutathione S-transferase theta-1
- Glutathione S-transferase omega-1
- Glutathione S-transferase theta-2
- Cytochrome P450 2B10
- Glutathione S-transferase kappa 1
- Epoxide hydrolase 1
- Cytochrome P450 2C55
- Glutathione S-transferase theta-3
- Glutathione S-transferase Mu 1
- Glutathione S-transferase Mu 6
Sequence:
MPMTLGYWNTRGLTHSIRLLLEYTDSSYEEKRYVMGDAPNFDRSQWLSEKFNLGLDFPNLPYLIDGSHKVTQSNAILRYLGRKHNLCGETEEERIRVDTLENQVMDTRIQLMIVCCSPDFEKQKPEFLKAIPEKMKLYSEFLGKRPWFAGDKVTYVDFLAYDILDQYRMFEPKCLDAFPNLRDFLARFEGLKKISAYMKSSRFLPRPVFTKIAQWGTD
Protein: UDP-glycosyltransferase 71K1 (EC 2.4.1.-) (UDP-glucose:chalcone 2'-O-glucosyltransferase) (UDP-glucose:flavonol 2'-O-glucosyltransferase) (D3UAG0)
Organism: Malus domestica (Apple) (Pyrus malus)
Function: Glycosyltransferase that possesses chalcone and flavonol 2'-O-glycosyltransferase activity. Converts phloretin to phlorizin (phloretin 2'-O-glucoside), a potent antioxidant. Possesses glycosyltransferase activity toward quercetin, isoliquiritigenin, butein and caffeic acid.
Interaction partners:
Sequence:
MKKVELVFIPSPGAGHHLPTLQFVKRLIDRNDRISITILAIQSYFPTTLSSYTKSIAASEPRIRFIDVPQPQDRPPQEMYKSRAQIFSLYIESHVPSVKKIITNLVSSSANSSDSIRVAALVVDLFCVSMIDVAKELNIPSYLFLTSNAGYLAFMLHLPILHEKNQIAVEESDPDWSIPGIVHPVPPRVLPAALTDGRLSAYIKLASRFRETRGIIVNTFVELETHAITLFSNDDRVPPVYPVGPVIDLDDGQEHSNLDQAQRDKIIKWLDDQPQKSVVFLCFGSMGSFGAEQVKEIAVGLEQSGQRFLWSLRMPSPKGIVPSDCSNLEEVLPDGFLERTNGKKGLICGWAPQVEILAHSATGGFLSHCGWNSILESLWHGVPIATWPMYAEQQLNAFRMVRELGMALEMRLDYKAGSADVVGADEIEKAVVGVMEKDSEVRKKVEEMGKMARKAVKDGGSSFASVGRFIEDVIGQN
Protein: RNA-binding motif protein, Y chromosome, family 1 member A1 (RNA-binding motif protein 1) (RNA-binding motif protein 2) (Y chromosome RNA recognition motif 1) (hRBMY) (P0DJD3)
Organism: Homo sapiens (Human)
Function: RNA-binding protein involved in pre-mRNA splicing. Required for sperm development. Acts additively with TRA2B to promote exon 7 inclusion of the survival motor neuron SMN. Binds non-specifically to mRNAs.
Subcellular location: Nucleus {ECO:0000269|PubMed:9108067}.
Interaction partners:
- Testis-specific Y-encoded protein 1
- Ubiquitin carboxyl-terminal hydrolase 9Y
- Testis-specific chromodomain protein Y 1
- Testis-specific basic protein Y 2
- ATP-dependent RNA helicase DDX3Y
- PTPN13-like protein, Y-linked
- Histone demethylase UTY demethylase UTY)
- RNA-binding motif protein, Y chromosome, family 1 member B
- RNA-binding motif protein, Y chromosome, family 1 member E
- RNA-binding motif protein, Y chromosome, family 1 member D
Sequence:
MVEADHPGKLFIGGLNRETNEKMLKAVFGKHGPISEVLLIKDRTSKSRGFAFITFENPADAKNAAKDMNGKSLHGKAIKVEQAKKPSFQSGGRRRPPASSRNRSPSGSLRSARGSRGGTRGWLPSHEGHLDDGGYTPDLKMSYSRGLIPVKRGPSSRSGGPPPKKSAPSAVARSNSWMGSQGPMSQRRENYGVPPRRATISSWRNDRMSTRHDGYATNDGNHPSCQETRDYAPPSRGYAYRDNGHSNRDEHSSRGYRNHRSSRETRDYAPPSRGHAYRDYGHSRRDESYSRGYRNRRSSRETREYAPPSRGHGYRDYGHSRRHESYSRGYRNHPSSRETRDYAPPHRDYAYRDYGHSSWDEHSSRGYSYHDGYGEALGRDHSEHLSGSSYRDALQRYGTSHGAPPARGPRMSYGGSTCHAYSNTRDRYGRSWESYSSCGDFHYCDREHVCRKDQRNPPSLGRVLPDPREACGSSSYVASIVDGGESRSEKGDSSRY
Protein: Chitinase 8 (EC 3.2.1.14) (Q9W2M7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- N-acetyl-D-glucosamine kinase
- beta-N-acetylhexosaminidase
- beta-N-acetylhexosaminidase
Sequence:
MWSVSGLVKLLLGVILMAASSSAQGNSSKNVVCYQGTWSVYRPGLGKFGMEDIDPFLCTHLIYAFLGIEETGQLRVIDAYLDLEENSGRGNIKSFNALKLKNPVLKTLVAVGGWNEGSKRFSLVARDPSKREKFVDDVVRFLQRHGFDGLDLDWEYPGQRHSLDNEDRSNYITFLKELKEGLEPFGFILSAAVGSAQFSAEISYDIPAMVPYLDLINVMAYDLHGPWDQVVGINAPLYAAEKDASDSSGRQQQLNVDAVVKYWLKAGAPAEKLILGVPFYGRSFTLATAEGNQPGAPHIGKGIAGNYSREPGVLGYNELCEMMEREEWTQKWEATQQVPYAYRQRQWVGYEDPRSLALKAQYVMDNHLGGIMIWSLESDDFRGTCGQQPYPLLHEINRVLFGGNTPSGLTTESNRESPSEGFSCPADAPAGYIRDPDNCSKFYYCSGGKTHNFDCPSGLNFDLDTKSCNYSGSVKC
Protein: EKC/KEOPS complex subunit PCC1 (Polarized growth chromatin-associated controller 1) (Q3E833)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. PCC1 functions as a dimerization module for the complex. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators.
Subcellular location: Nucleus {ECO:0000305}. Chromosome, telomere {ECO:0000305}.
Interaction partners:
- EKC/KEOPS complex subunit CGI121
- EKC/KEOPS complex subunit BUD32
- EKC/KEOPS complex subunit GON7
- tRNA N6-adenosine threonylcarbamoyltransferase
- tRNA N6-adenosine threonylcarbamoyltransferase, mitochondrial
- Threonylcarbamoyl-AMP synthase
Sequence:
MTSKREKSLDHTLELKIPFETERQATIATKVLSPDPILKPQDFQVDYSSEKNVMLVQFRSIDDRVLRVGVSSIIDSIKTIVEAMDVLS
Protein: Proteasome subunit alpha type (H0YMZ1)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU000551}. Nucleus {ECO:0000256|RuleBase:RU000551}.
Interaction partners:
Sequence:
MSRRYDSRTTIFSPEGRLYQVEYAMEAIGHAGTCLGILANDGVLLAAERRNIHKLLDEVFFSEKIYKLNEDMACSVAGITSDANVLTNELRLIAQRYLLQYQEPIPCEQLVTALCDIKQAYTQFGGKRPFGVSLLYIGWDKHYGFQLYQSDPSGNYGGWKATCIGNNSAAAVSMLKQDYKEGEMTLKSALALAIKVLNKTMDVSKLSAEKVEIATLTREN
Protein: Band 4.1-like protein 2 (Erythrocyte membrane protein band 4.1-like 2) (Generally expressed protein 4.1) (4.1G) (O43491)
Organism: Homo sapiens (Human)
Function: Required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000269|PubMed:23870127}. Cell membrane {ECO:0000269|PubMed:22361696}.
Interaction partners:
- Nuclear mitotic apparatus protein 1
- Band 4.1-like protein 3
- Spectrin beta chain, non-erythrocytic 1
- Spectrin beta chain, non-erythrocytic 4
- Band 4.1-like protein 1
- Spectrin alpha chain, non-erythrocytic 1
- Spectrin beta chain, non-erythrocytic 5
- Spectrin beta chain, non-erythrocytic 2
- Spectrin beta chain, erythrocytic
- Glutamate receptor 1
Sequence:
MTTEVGSVSEVKKDSSQLGTDATKEKPKEVAENQQNQSSDPEEEKGSQPPPAAESQSSLRRQKREKETSESRGISRFIPPWLKKQKSYTLVVAKDGGDKKEPTQAVVEEQVLDKEEPLPEEQRQAKGDAEEMAQKKQEIKVEVKEEKPSVSKEEKPSVSKVEMQPTELVSKEREEKVKETQEDKLEGGAAKRETKEVQTNELKAEKASQKVTKKTKTVQCKVTLLDGTEYSCDLEKHAKGQVLFDKVCEHLNLLEKDYFGLLFQESPEQKNWLDPAKEIKRQLRNLPWLFTFNVKFYPPDPSQLTEDITRYFLCLQLRQDIASGRLPCSFVTHALLGSYTLQAELGDYDPEEHGSIDLSEFQFAPTQTKELEEKVAELHKTHRGLSPAQADSQFLENAKRLSMYGVDLHHAKDSEGVDIKLGVCANGLLIYKDRLRINRFAWPKILKISYKRSNFYIKVRPAELEQFESTIGFKLPNHRAAKRLWKVCVEHHTFYRLVSPEQPPKAKFLTLGSKFRYSGRTQAQTRQASTLIDRPAPHFERTSSKRVSRSLDGAPIGVMDQSLMKDFPGAAGEISAYGPGLVSIAVVQDGDGRREVRSPTKAPHLQLIEGKKNSLRVEGDNIYVRHSNLMLEELDKAQEDILKHQASISELKRNFMESTPEPRPNEWEKRRITPLSLQTQGSSHETLNIVEEKKRAEVGKDERVITEEMNGKEISPGSGPGEIRKVEPVTQKDSTSLSSESSSSSSESEEEDVGEYRPHHRVTEGTIREEQEYEEEVEEEPRPAAKVVEREEAVPEASPVTQAGASVITVETVIQENVGAQKIPGEKSVHEGALKQDMGEEAEEEPQKVNGEVSHVDIDVLPQIICCSEPPVVKTEMVTISDASQRTEISTKEVPIVQTETKTITYESPQIDGGAGGDSGTLLTAQTITSESVSTTTTTHITKTVKGGISETRIEKRIVITGDGDIDHDQALAQAIREAREQHPDMSVTRVVVHKETELAEEGED
Protein: Protein IQ-DOMAIN 5 (AtIQD5) (F4J061)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in cooperative interactions with calmodulins or calmodulin-like proteins (By similarity). Recruits calmodulin (CaM) calcium sensor proteins to cortical microtubule arrays, thus being a potential scaffold in cellular signaling and trafficking. Binds to microtubules (MTs) and promotes MT assembly and dynamics to modulate pavement cell (PC) morphogenesis via cellulose deposition-dependent anisotropic cell expansion triggered by cellulose synthase complexes (CSCs). May associate with nucleic acids and regulate gene expression at the transcriptional or post-transcriptional level (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:28115582, ECO:0000269|PubMed:29976837, ECO:0000269|PubMed:30407556}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:29976837}. Cytoplasm, cytoskeleton, phragmoplast {ECO:0000269|PubMed:29976837}. Note=Localized to microtubules (MTs) arrays in dynamic pattern, including cortical MT in leaf pavement and hypocotyl epidermal cells (in a discontinuous and punctate manner corresponding to indentation regions), as well as preprophase bands, mitotic spindles, and phragmoplasts of mitotic cells in root tips. {ECO:0000269|PubMed:29976837, ECO:0000269|PubMed:30407556}.
Interaction partners:
- Protein KINESIN LIGHT CHAIN-RELATED 1
- At1g23060/T26J12_16
- GPI-anchored adhesin-like protein, putative
Sequence:
MGASGRWIKALVGFTKSDKSRSSKKDENVKVATKSRFGRKNSVDFDFEKFQDGFEDSNTRSMVDTGVSTSTSLQSYGGVAYDEQSRENRAATRIQTAYRGFLARRALRALKGLVRLQALVRGHAVRKQAAVTLRCMQALVRVQARVRARRVRLALELESETSQQTLQQQLADEARVREIEEGWCDSIGSVEQIQAKLLKRQEAAAKRERAMAYALTHQWQAGTRLLSAHSGFQPDKNNWGWNWLERWMAVRPWENRFLDSNLRDDAKLGENGMEQSENVPKTQIKSVSKMPNTSNLVSGVSSQMTGPCQSDGDSSSPGISSSIPVVSKAKSKPAKDDLAVEVNSRPGAGPRSHSNPKERSREPNRSSKERLSLPNSGKSLGSQSTKANRAGKLTPASQKVVEEKSAQNQRRRNSDPIKQRLA
Protein: Proteasome subunit beta (Q95SA6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU004203}. Nucleus {ECO:0000256|RuleBase:RU004203}.
Interaction partners:
Sequence:
MQPDFDFTGTPVSTGTTIMAVEFDGGVVIGADSRTSSGAYVANRVTDKLTRITDKVYCCRSGSAADTQAIADIVAYSLNYHENQTNKDALVFEAASEFRNYCYSYRESLLAGIIVAGWDEQRGGQVYSIPLGGMLTRESCTIGGSGSSFIYGFVREHYRPNMALEDCVTFVKKAVQHAIYHDGSSGGVVRIGIITKDGIERRIFYNTESGASAVSSTPSFISSE
Protein: Pentatricopeptide repeat-containing protein At1g05750, chloroplastic (Protein PIGMENT DEFECTIVE 247) (Q9MA50)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- RNI-like superfamily protein
- RNA recognition motif
- Ribosomal protein L1p/L10e family
- Peptidyl-tRNA hydrolase, mitochondrial
- Pentatricopeptide repeat-containing protein At1g02370
- H/ACA ribonucleoprotein complex non-core subunit NAF1
- Pentatricopeptide repeat-containing protein At1g06270
- Protein OSB4, chloroplastic
- At3g46020
Sequence:
MGLLPVVGITSPALITHKNHANPKIQRHNQSTSETTVSWTSRINLLTRNGRLAEAAKEFSDMTLAGVEPNHITFIALLSGCGDFTSGSEALGDLLHGYACKLGLDRNHVMVGTAIIGMYSKRGRFKKARLVFDYMEDKNSVTWNTMIDGYMRSGQVDNAAKMFDKMPERDLISWTAMINGFVKKGYQEEALLWFREMQISGVKPDYVAIIAALNACTNLGALSFGLWVHRYVLSQDFKNNVRVSNSLIDLYCRCGCVEFARQVFYNMEKRTVVSWNSVIVGFAANGNAHESLVYFRKMQEKGFKPDAVTFTGALTACSHVGLVEEGLRYFQIMKCDYRISPRIEHYGCLVDLYSRAGRLEDALKLVQSMPMKPNEVVIGSLLAACSNHGNNIVLAERLMKHLTDLNVKSHSNYVILSNMYAADGKWEGASKMRRKMKGLGLKKQPGFSSIEIDDCMHVFMAGDNAHVETTYIREVLELISSDLRLQGCVVETLAGDLLNA
Protein: Peroxiredoxin OsmC (EC 1.11.1.-) (Osmotically-inducible protein C) (P0C0L2)
Organism: Escherichia coli (strain K12)
Function: Preferentially metabolizes organic hydroperoxides over inorganic hydrogen peroxide.
Subcellular location: Cytoplasm.
Interaction partners:
- Catalase HPII
- Osmotically-inducible protein Y
- Osmotically-inducible putative lipoprotein OsmE
- Potassium binding protein Kbp
- Osmotically-inducible lipoprotein B
- Stationary-phase-induced ribosome-associated protein
- Protein ElaB
- DNA protection during starvation protein
- Uncharacterized protein YqjD
- Superoxide dismutase
Sequence:
MTIHKKGQAHWEGDIKRGKGTVSTESGVLNQQPYGFNTRFEGEKGTNPEELIGAAHAACFSMALSLMLGEAGFTPTSIDTTADVSLDKVDAGFAITKIALKSEVAVPGIDASTFDGIIQKAKAGCPVSQVLKAEITLDYQLKS
Protein: Aspartate aminotransferase, cytoplasmic (cAspAT) (EC 2.6.1.1) (EC 2.6.1.3) (Cysteine aminotransferase, cytoplasmic) (Cysteine transaminase, cytoplasmic) (cCAT) (Glutamate oxaloacetate transaminase 1) (Transaminase A) (P13221)
Organism: Rattus norvegicus (Rat)
Function: Biosynthesis of L-glutamate from L-aspartate or L-cysteine. Important regulator of levels of glutamate, the major excitatory neurotransmitter of the vertebrate central nervous system. Acts as a scavenger of glutamate in brain neuroprotection. The aspartate aminotransferase activity is involved in hepatic glucose synthesis during development and in adipocyte glyceroneogenesis. Using L-cysteine as substrate, regulates levels of mercaptopyruvate, an important source of hydrogen sulfide. Mercaptopyruvate is converted into H(2)S via the action of 3-mercaptopyruvate sulfurtransferase (3MST). Hydrogen sulfide is an important synaptic modulator and neuroprotectant in the brain.
Subcellular location: Cytoplasm.
Interaction partners:
- Malate dehydrogenase, mitochondrial
- Alanine aminotransferase 1
- Aspartate aminotransferase, mitochondrial
- L-lactate dehydrogenase B chain
- L-lactate dehydrogenase C chain
- Glutamate dehydrogenase 1, mitochondrial
- Malate dehydrogenase, cytoplasmic
- L-lactate dehydrogenase A chain
- Tyrosine aminotransferase
- Thiosulfate sulfurtransferase
Sequence:
MAPPSFFAQVPQAPPVLVFKLIADFRDDPDPRKVNLGVGAYRTDDSQPWVLPVVRKVEQKIANDHSLNHEYLPILGLAEFRSCASQLVLGDNSPALRENRVGGVQSLGGTGALRIGADFLGRWYNGTDNKNTPVYVSSPTWENHNGVFSAAGFKDIRSYRYWDAEKRGLDLQGFLNDLENAPEFSIFVLHACAHNPTGTDPTEEEWKQIAAVMKRRFLFPFFDSAYQGFASGDLEKDAWAIRYFVSEGFELFCAQSFSKNFGLYNERVGNLTVVGKEHDSVLRVLSQMEKIVRITWSNPPAQGARIVATTLSNPELFKEWKGNVKTMADRILTMRSELRARLEALKTPGTWSHITEQIGMFSFTGLNPKQVEYLVNEKHIYLMPSGRINMCGLTTKNLDYVATSINEAVTKFQ
Protein: Immunoglobulin kappa variable 1D-12 (Ig kappa chain V-I region Wes) (P01611)
Organism: Homo sapiens (Human)
Function: V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen.
Subcellular location: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
Interaction partners:
Sequence:
MDMMVPAQLLGLLLLWFPGSRCDIQMTQSPSSVSASVGDRVTITCRASQGISSWLAWYQQKPGKAPKLLIYAASSLQSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQANSFP
Protein: peptidylprolyl isomerase (EC 5.2.1.8) (G1T0U7)
Organism: Oryctolagus cuniculus (Rabbit)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Sarcoplasmic reticulum {ECO:0000256|ARBA:ARBA00004369}.
Interaction partners:
Sequence:
GRTFPKKGQTCVVHYTGMLQNGKKFDSSRDRNKPFKFRIGKQEVIKGFEEGAAQMSLGQRAKLTCTPDVAYGATGHPGVIPPNATLIFDVELLNLE
Protein: histidine kinase (EC 2.7.13.3) (Q8A3A5)
Organism: Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50)
Interaction partners:
- histidine kinase
- histidine kinase
- histidine kinase
- histidine kinase
- histidine kinase
- Two-component system sensor histidine kinase/response regulator, hybrid
- histidine kinase
- histidine kinase
- Two-component system response regulator
- histidine kinase
Sequence:
MKTYIAAFFLLLSATFVAAHPYLIQRLGIEQGLSNNYVLSITQDKQGFLWFATEEGLNKFDGTRFITYYKEEQSSSVQSITGNELNEVYTDPVQPVIWIATQRAGLNAYNYETQSFSVYQYNPEDPQSLITNDVTHITSSVQAGKGLWVCTYYRGIEYLDIATGKFTHYNKSTVPALPSEQTWTATEAEDGKLYIGHVEGGLSILSLNDKSVKHFVHDPQNPNSLPGNDVRCIYKDTNGNIWIGTSKGLALFNANTETFTNFHNNPGNIHGALSSYIFSIKQLKDNKLWIATELNGIMILDLQQNQFLLPEQIRFEFIREGDNNYSLSNASARYIFQDSFNNIWIGTWGGGINFISNAPPTFHTWSYSPTQMNESSLSNKVVSSVCDDGQGKLWIGTDGGGINVFENGKRVAIYNKENRELLSNSVLCSLKDSEGNLWFGTYLGNISYYNTRLKKFQIIELEKNELLDVRVFYEDKNKKIWIGTHAGVFVIDLASKKVIHHYDTSNSQLLENFVRSIAQDSEGRFWIGTFGGGVGIYTPDMQLVRKFNQYEGFCSNTINQIYRSSKGQMWLATGEGLVCFPSARNFDYQVFQRKEGLPNTHIRAISEDKNGNIWASTNTGISCYITSKKCFYTYDHSNNIPQGSFISGCVTKDHNGLIYFGSINGLCFFNPDIAINSPQIPPVVITKVRIPGRLTSREKNETAIPISEGEIELTHEQNSFNLTFNVQDYSLANQVEYAYMLKGLENSWYTINEQNSVTFRNIPPGKYEFLVKARLHNQDWSEDTTSLRIHINPPLWLTWWAKLIYILITISIIYTIIHAYKKKIDLESLYTLEKKNHEQEQELNQERLRFYTNITHELRTPLTLILGPLEDMQKDTSLPTRQAQKLSVIHLSALRLLNLINQILEFRKTETQNKKLCVCKGNIVPLIHEIGLKYKELNQKKAIDFQIQIEKEEMPLFFDKEIITIILDNLISNAIKYTEQGKITLSLYPTTRNGVTYTEIKVSDTGYGISAEALPHVFDRYYQESGKHQASGTGIGLALVRNLVELHEGEIRVESIQNEGSTFYISLLTDNIYPNALHGDSTKQTEEEMISEAVPEDSQNTEPETSKPILLIVEDNEDIQKYIAESFSDSFEVITGSNGEEGKQQALNRIPDIIVSDIMMPVMDGITLCRQLKEDVRTSHIPVILLTAKDSLQDKEEGYEVGADSYLTKPFSASLLRSRINNLLDSRKKLIAQFQQTGTNHNPNSHLDEKRSIITEALSKLDNEFIEKITQLVEDNLSSEKIDITYLSDKMCMSGSTLYRKMKALTGLSTNEYIRKVKMQNAERLLLEGKYNISEIAYKIGMNSTGYFRQCFKDEFGVSPSDYLKQFTSPTPPPSS