wanglab/gogpt-training-data huggingface dataset:
Protein: Holliday junction branch migration complex subunit RuvA (P0A809)
Organism: Escherichia coli (strain K12)
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. The RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR); RFR and homologous recombination required for UV light survival can be separated. The RuvA-RuvB complex promotes Holliday junction (HJ) branch migration. RuvA binds to HJ cruciform DNA, conferring on it an open structure. In the presence of RuvB, ATP and Mg(2+) the junction is dissociated; hydrolyzable (d)NTPs can replace ATP but other analogs cannot. The RuvB hexamer acts as a pump, pulling dsDNA into and through the RuvAB complex. Can bypass UV-induced lesions and physically cross-linked DNA strands. RuvA gives specificity by binding to cruciform junctions, while the RuvB ATPase provides the motor force for branch migration; excess RuvB can promote branch migration in the absence of RuvA. Overexpression of RuvA alone leads to UV sensitivity. RuvA stimulates the weak ATPase activity of RuvB in the presence of DNA; the addition of HJ DNA further stimulates ATPase about 10-fold. Inhibits RuvC endoDNase activity by binding to HJ DNA, including DNA to which RuvC is already bound. Does not bind dsDNA. May act as a collar that slides at HJ which promotes branch migration while inhibiting other DNA remodeling activities (Probable).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00031, ECO:0000269|PubMed:21219465}. Note=In 15% of cell localizes to discrete nucleoid foci (probable DNA damage sites) upon treatment with mitomycin C (MMC) for 2 hours.
Interaction partners:
- Crossover junction endodeoxyribonuclease RuvC
- Holliday junction branch migration complex subunit RuvB
- ATP-dependent DNA helicase RecG
- UvrABC system protein A
- DNA helicase II
- Protein RecA
- UvrABC system protein B
- UvrABC system protein C
- ATP-dependent DNA helicase RecQ
- DNA repair protein RecN
Sequence:
MIGRLRGIIIEKQPPLVLIEVGGVGYEVHMPMTCFYELPEAGQEAIVFTHFVVREDAQLLYGFNNKQERTLFKELIKTNGVGPKLALAILSGMSAQQFVNAVEREEVGALVKLPGIGKKTAERLIVEMKDRFKGLHGDLFTPAADLVLTSPASPATDDAEQEAVAALVALGYKPQEASRMVSKIARPDASSETLIREALRAAL
Protein: Small ribosomal subunit protein uS7 (40S ribosomal protein S5) (RP14) (S2) (YS8) (P26783)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22096102}.
Interaction partners:
- Small ribosomal subunit protein eS26B
- Small ribosomal subunit protein eS17A
- Large ribosomal subunit protein uL10
- Periodic tryptophan protein 2
- Large ribosomal subunit protein eL30
- Small ribosomal subunit protein uS8B
- Large ribosomal subunit protein eL24A
- Small ribosomal subunit protein eS30A
- Large ribosomal subunit protein eL34A
- Small ribosomal subunit protein uS14A
Sequence:
MSDTEAPVEVQEDFEVVEEFTPVVLATPIPEEVQQAQTEIKLFNKWSFEEVEVKDASLVDYVQVRQPIFVAHTAGRYANKRFRKAQCPIIERLTNSLMMNGRNNGKKLKAVRIIKHTLDIINVLTDQNPIQVVVDAITNTGPREDTTRVGGGGAARRQAVDVSPLRRVNQAIALLTIGAREAAFRNIKTIAETLAEELINAAKGSSTSYAIKKKDELERVAKSNR
Protein: Calmodulin (CaM) (P05933)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:9635188}. Note=In the growing tips and spindle pole body during interphase and in the septum during septation. Component of a ring structure that forms prior to septation.
Interaction partners:
- Myosin-1
- Actin
- Calcium-channel protein cch1
- Calcium/calmodulin-dependent protein kinase type II
- Peptidyl-prolyl cis-trans isomerase
- Tubulin beta chain
- Myosin 1 light chain cam2
- Transcriptional regulator prz1
- Serine/threonine-protein phosphatase 2B catalytic subunit
- Calcium/calmodulin-dependent protein kinase type I
Sequence:
MTTRNLTDEQIAEFREAFSLFDRDQDGNITSNELGVVMRSLGQSPTAAELQDMINEVDADGNGTIDFTEFLTMMARKMKDTDNEEEVREAFKVFDKDGNGYITVEELTHVLTSLGERLSQEEVADMIREADTDGDGVINYEEFSRVISSK
Protein: Homeotic protein ultrabithorax (Q24703)
Organism: Drosophila virilis (Fruit fly)
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. Binds the consensus region 5'-TTAAT[GT][GA]-3'. This homeotic protein controls development of the cells in the posterior thoracic and first abdominal segments. It activates the synthesis of the decapentaplegic (DPP) growth factor (By similarity).
Subcellular location: Nucleus.
Interaction partners:
Sequence:
SGAAAAQTAAASSLHQASNHTFYPWMAIAGESTADPSKSKIRSDLTQYGGISTDMGKRYSESLAGSLLPDWLGTNGLRRRGRQTYTR
Protein: Protein MICRORCHIDIA 1 (AtMORC1) (EC 3.6.-.-) (Protein COMPROMISED RECOGNITION OF TCV 1) (Q84WV6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mediator of defense signaling triggered by distinct classes of R proteins. Required during hypersensitive response (HR) that confers disease resistance to turnip crinkle virus (TCV). Exhibits ATPase activity. Contributes to resistance against Pseudomonas syringae and Hyaloperonospora arabidopsidis, at early stages prior to cytosolic calcium ions Ca(2+) accumulation. Required for pathogen-associated molecular pattern (PAMP)-triggered immunity (PTI), basal resistance, non-host resistance and systemic acquired resistance (SAR). Binds DNA/RNA in a non-specific manner and exhibits endonuclease activity. Probably involved in DNA repair. Required for both RPP8- and SSI4-mediated resistance responses, thus being involved in both TIR- and CC-NB-LRR pathways. Involved in RNA-directed DNA methylation (RdDM) as a component of the RdDM machinery and required for gene silencing. May also be involved in the regulation of chromatin architecture to maintain gene silencing.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:22555433, ECO:0000269|PubMed:23250427}. Endosome {ECO:0000269|PubMed:20332379}. Note=Present in nuclear bodies near chromocenters (PubMed:22555433). Localized in endosome-like vesicles displaying rapid cytosolic streaming (PubMed:20332379). Accumulates in the nucleus following pathogen-associated molecular pattern (PAMP) treatment or infection with an avirulent pathogen (PubMed:23250427). {ECO:0000269|PubMed:20332379, ECO:0000269|PubMed:22555433, ECO:0000269|PubMed:23250427}.
Interaction partners:
- Histone-lysine N-methyltransferase family member SUVH9
- Histone-lysine N-methyltransferase family member SUVH2
- Protein DEFECTIVE IN MERISTEM SILENCING 3
- Helicase protein MOM1
- Protein RDM1
- Protein SAWADEE HOMEODOMAIN HOMOLOG 1
- Serine/threonine-protein phosphatase 7 long form homolog
- Protein INVOLVED IN DE NOVO 2
Sequence:
MAKNYTVADVVNIDSDSDSDDDNGGVIGMVPSLASLIENQKVSIADAATVAPRETLECRSFWKAGENFVIPSSVTLTAIGMVEHARVHPKFLHSNATSHKWAFGAIAELLDNAVDEIQNGATVVKIDKINIVKDNTPALVFQDNGGGMDPNGIRKCMSLGYSSKKSNTTIGQYGNGFKTSTMRLGADAMVFSRSTRGGKSTQSIGLLSYTFLRKTGQDDVIVPMIDFDISSDSPQPIIYGSPGDWSTNLNILLKWSPFSTMVELLQQFEDIGTHGTKVIIYNLWLNDEGIYELSFDDDDVDIRLRDENAQDGKRLHAKTLEVRSHISYRYRHSLRAYISMLYLKKFKNFKIILRGVSVAQFNIADEFRHPETIMYKPQAAAVDYAATGIKVGFIKEAPKLPICGFNVYHKNRLIRPFWKVVLEGSTRGNGVMGVLEANFIEPAHDKQDFERSSLFLRLEARLKRITSDYWQNHCHIFGYQTAQIPADKSKRTVIPDQPPTVNTYNPSPLPSDRISHGGPIIREINLSNATSSRTAAVAAPHLRNYTGLRNNFQPVQLNPQPPAAGDTGNNLVGKLAAEIREENLQLFMRCEEYVKKENEVEQTVKSLEKELEEIKSKCAQLALLVDAKKKEMQQV
Protein: Mitogen-activated protein kinase kinase kinase 7 (EC 2.7.11.25) (TGF-beta-activated kinase 1) (dTAK1) (Q9V3Q6)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of a protein kinase signal transduction cascade. Mediator of TGF-beta signal transduction. Responsible for activation of the JNK MAPK pathway (basket, bsk and hemipterous, hep) in response to LPS. Component of the NF-kappa-B pathway; relish-mediated JNK inhibition involves proteasomal degradation of Tak1; certain targets of Relish that are induced during immune responses may facilitate destruction of Tak1 and switch off the JNK cascade. Participates in diverse roles such as control of cell shape and regulation of apoptosis.
Interaction partners:
- LD40663p
- GH01161p
- Protein immune deficiency
- mitogen-activated protein kinase kinase
- NF-kappa-B essential modulator
- Dual specificity mitogen-activated protein kinase kinase hemipterous
- mitogen-activated protein kinase kinase
- Death-associated inhibitor of apoptosis 2
- Mitogen-activated protein kinase
- LD20892p
Sequence:
MATASLDALQAAYVDFSEITLREKVGHGSYGVVCKAVWRDKLVAVKEFFASAEQKDIEKEVKQLSRVKHPNIIALHGISSYQQATYLIMEFAEGGSLHNFLHGKVKPAYSLAHAMSWARQCAEGLAYLHAMTPKPLIHRDVKPLNLLLTNKGRNLKICDFGTVADKSTMMTNNRGSAAWMAPEVFEGSKYTEKCDIFSWAIVLWEVLSRKQPFKGIDNAYTIQWKIYKGERPPLLTTCPKRIEDLMTACWKTVPEDRPSMQYIVGVMHEIVKDYTGADKALEYTFVNQQIVTKESDGTVAAQPDSLSSQEGELSPSSTQLTPTTAANANVNAIAISKTTTSSMTENTSSTSSDITPTNSGQLDNNPLFYMVTNRWDAIPEEESNESRNDSFNLTSSAEATQRLETIRNGMILMACKPMEQLTLDVEANGFDLSPSESSSSSTNAKSDGRERLTVTDTKPVMMTTDLSNNNGGIHAHSNGLLSHANGWQARDEELQEQEHEQEIVNSLDVDVDPDEDENDGTEQSLAEILDPELQPEPPIPNDAESQLIYRDHRHMAKEYLSVDTNLYYAQDFKDKLIVQMDRTEREQKQELLRKMKDKEGLQSLYNNLQQQYASRQLAAGHHPQPHPHPHPNQLQHPHSHPPMHFLQDEGCGLLPGSVCGGSESVEEGWVVIPPHHNA
Protein: Cell growth regulator with RING finger domain protein 1 (Cell growth regulatory gene 19 protein) (P97587)
Organism: Rattus norvegicus (Rat)
Function: Able to inhibit growth in several cell lines.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q99675}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q99675}.
Interaction partners:
Sequence:
MAAVFLVTLYEYSPLFYIAVVFTCFIATTGLVLGWLGWDVPVILRNSEETQFSTRAFKKQMRQVKNPFGLEITNSSAASLATGVTLTTDCLEDSRLTCYWGCSVQKLYEALQKHVYCFRISTPQALEEALYSDYLHREQYFIKKHSKEEIYCQLPSSTGVEDFGPVPRSRYPLVALLTLADEDDREIYDIISMVSVIHIPDKTYKLPCRILYQYLILAQGQFYDLKQLFMSANNSATPSRDQSPADGSVEHSLLEKAGLAGAEVDPVEESSKDCVVCQNGGVNWVLLPCRHACLCDSCVCYFKQCPMCRQFVQESFALCGQKEADKDILETS
Protein: Hydroxysteroid 11-beta-dehydrogenase 1-like protein (11-beta-hydroxysteroid dehydrogenase type 3) (A0A087WWR3)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MANLGTLQLLPPRFKRFSCLSLPNIWITGMPVPATSVPCPSAGPHRTMKVLLLTGLGALFFAYYWDDNFDPASLQGARVLLTGANAGVGEELAYHYARLGSHLVLTAHTEALLQKVVGNCRKLGAPKVFYIAADMASPEAPESVVQFALDKLGGLDYLVLNHIGGAPAGTRARSPQATRWLMQVNFVSYVQLTSRALPSLTDSKGSLVVVSSLLGRVPTSFSTPYSAAKFALDGFFGSLRRELDVQDVNVAITMCVLGLRDRASAAEAVRGVTRVKAAPGPKAALAVIRGGATRAAGVFYPWRFRLLCLLRRWLPRPRAWFIRQELNVTAAAA
Protein: Ubinuclein-1 (HIRA-binding protein) (Protein VT4) (Ubiquitously expressed nuclear protein) (Q9NPG3)
Organism: Homo sapiens (Human)
Function: Acts as a novel regulator of senescence. Involved in the formation of senescence-associated heterochromatin foci (SAHF), which represses expression of proliferation-promoting genes. Binds to proliferation-promoting genes. May be required for replication-independent chromatin assembly.
Subcellular location: Nucleus, nucleoplasm. Nucleus, PML body. Cell junction, tight junction. Note=Localized as a nuclear speckled-like pattern in proliferating primary fibroblasts. Colocalizes with HIRA, PML and SP100 in PML bodies of senescent cells. Colocalizes with TJP1 and CLDN1. Detected along the upper granular cell layer of epidermis. When overexpressed, accumulates in the nucleus in cells showing defective cytokinesis.
Interaction partners:
- Protein HIRA
- Calcineurin-binding protein cabin-1
- Histone chaperone ASF1A
- Histone H3.3
- Histone chaperone ASF1B
- Endoplasmic reticulum-Golgi intermediate compartment protein 2
- Pre-mRNA-splicing regulator WTAP
- UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
- Regulator of nonsense transcripts 1
Sequence:
MSEPHRVQFTSLPGSLNPAFLKKSRKEEAGAGEQHQDCEPAAAAVRITLTLFEPDHKRCPEFFYPELVKNIRGKVKGLQPGDKKKDLSDPFNDEEKERHKVEALARKFEEKYGGKKRRKDRIQDLIDMGYGYDESDSFIDNSEAYDELVPASLTTKYGGFYINSGTLQFRQASESEDDFIKEKKKKSPKKRKLKEGGEKIKKKKKDDTYDKEKKSKKSKFSKAGFTALNASKEKKKKKYSGALSVKEMLKKFQKEKEAQKKREEEHKPVAVPSAEAQGLRELEGASDPLLSLFGSTSDNDLLQAATAMDSLTDLDLEHLLSESPEGSPFRDMDDGSDSLGVGLDQEFRQPSSLPEGLPAPLEKRVKELAQAARAAEGESRQKFFTQDINGILLDIEAQTRELSSQVRSGVYAYLASFLPCSKDALLKRARKLHLYEQGGRLKEPLQKLKEAIGRAMPEQMAKYQDECQAHTQAKVAKMLEEEKDKEQRDRICSDEEEDEEKGGRRIMGPRKKFQWNDEIRELLCQVVKIKLESQDLERNNKAQAWEDCVKGFLDAEVKPLWPKGWMQARTLFKESRRGHGHLTSILAKKKVMAPSKIKVKESSTKPDKKVSVPSGQIGGPIALPSDHQTGGLSIGASSRELPSQASGGLANPPPVNLEDSLDEDLIRNPASSVEAVSKELAALNSRAAGNSEFTLPAPSKAPAEKVGGVLCTEEKRNFAKPSPSAPPPASSLQSPLNFLAEQALALGQSSQEKKPESSGYKELSCQAPLNKGLPEVHQSKAKHHSLPRTSHGPQVAVPVPGPQVKVFHAGTQQQKNFTPPSPFANKLQGPKASPTQCHRSLLQLVKTAAKGQGFHPSAPATSGGLSASSSSSHKTPASSSSALSHPAKPHSVSSAGSSYKNNPFASSISKHGVSSGSSSSGGTPVQSSVSGSLVPGIQPPSVGQATSRPVPSSAGKKMPVSQKLTLVAPPGGPNGDSSGGTQGVAKLLTSPSLKPSAVSSVTSSTSLSKGASGTVLLAGSSLMASPYKSSSPKLSGAMSSNSLGIITPVPIPVHVLSFSADSSAKAGVSKDAIVTGPAPGSFHHGLGHSLLAGLHSSPPHAAPLPHAAVPTHIPQSLPGASQLHGKGPAVPRKL
Protein: Histone H2AX (H2a/x) (Histone H2A.X) (Q7ZUY3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Required for checkpoint-mediated arrest of cell cycle progression in response to low doses of ionizing radiation and for efficient repair of DNA double strand breaks (DSBs) specifically when modified by C-terminal phosphorylation (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P27661}. Chromosome {ECO:0000250|UniProtKB:P27661}.
Interaction partners:
- Peptidyl-prolyl cis-trans isomerase
- Mediator of DNA damage checkpoint 1.
- Histone H2B 3
- Histone H2B
- non-specific serine/threonine protein kinase
- Histone H3.3
- Checkpoint kinase 2.
- DNA helicase
- E3 ubiquitin-protein ligase rnf168
- Histone H3.2
Sequence:
MSGRGKTGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEELNKLLGGVTIAQGGVLPNIQAVLLPKKTGQAAASSGKSGKKGSSQSQEY
Protein: ATP synthase F(1) complex subunit epsilon, mitochondrial (ATPase subunit epsilon) (ATP synthase F1 subunit epsilon) (P56381)
Organism: Homo sapiens (Human)
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 of the central stalk which is part of the complex rotary element. 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 (By similarity).
Subcellular location: Mitochondrion. Mitochondrion inner membrane.
Interaction partners:
- ATP synthase F
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit b, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit d, mitochondrial
Sequence:
MVAYWRQAGLSYIRYSQICAKAVRDALKTEFKANAEKTSGSNVKIVKVKKE
Protein: Neuronal pentraxin-2 (NP2) (Neuronal pentraxin II) (NP-II) (O70340)
Organism: Mus musculus (Mouse)
Function: Likely to play role in the modification of cellular properties that underlie long-term plasticity. Binds to agar matrix in a calcium-dependent manner (By similarity).
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Glutamate receptor 4
- Glutamate receptor 2
Sequence:
MLALLTVGVALAVAAGRAQDSPIPGSRFVCTALPPEAARAGCPLPAMPMQGGALSPEEELRAAVLQLRETVVQQKETLGAQREAIRELTGKLARCEGLAGGKARGTGKDTMGDLPRDPGHVVEQLSRSLQTLKDRLESLELQLRTNVSNAGLPSDFREVLQRRLGELERQLLRKVAELEDEKSLLHNETSAHRQKTESTLNALLQRVTELERGNSAFKSPDAFKVSLPLRTNYLYGKIKKTLPELYAFTICLWLRSSASPGIGTPFSYAVPGQANEIVLIEWGNNPIELLINDKVAQLPLFVSDGKWHHICITWTTRDGMWEAFQDGEKLGTGENLAPWHPIKPGGVLILGQEQDTVGGRFDATQAFVGELSQFNIWDRVLRAQEIINIANCSTNMPGNIIPWVDNNVDVFGGASKWPVETCEERLLDL
Protein: Pre-mRNA-processing protein PRP40 (P33203)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for pre-spliceosome formation, which is the first step of pre-mRNA splicing. This protein is associated with snRNP U1. Two commitment complexes, CC1 and CC2, have been defined in yeast. CC1 is a basal complex dependent only on the 5' splice site. CC2 is a complex of lower mobility and is dependent on a branchpoint as well as a 5' splice site region. This protein is involved in CC2 formation where it binds to the branchpoint binding protein MSL5, bridging the U1 snRNP-associated 5' splice site and the MSL5-associated branch point 3' intron splice site.
Subcellular location: Nucleus {ECO:0000269|PubMed:15020406}.
Interaction partners:
- Protein NAM8
- Nuclear cap-binding protein subunit 2
- Small nuclear ribonucleoprotein E
- U1 small nuclear ribonucleoprotein component PRP42
- 56 kDa U1 small nuclear ribonucleoprotein component
- U1 small nuclear ribonucleoprotein C
- U1 small nuclear ribonucleoprotein component SNU71
- Small nuclear ribonucleoprotein Sm D1
- U2 small nuclear ribonucleoprotein A'
- Protein LUC7
Sequence:
MSIWKEAKDASGRIYYYNTLTKKSTWEKPKELISQEELLLRENGWKAAKTADGKVYYYNPTTRETSWTIPAFEKKVEPIAEQKHDTVSHAQVNGNRIALTAGEKQEPGRTINEEESQYANNSKLLNVRRRTKEEAEKEFITMLKENQVDSTWSFSRIISELGTRDPRYWMVDDDPLWKKEMFEKYLSNRSADQLLKEHNETSKFKEAFQKMLQNNSHIKYYTRWPTAKRLIADEPIYKHSVVNEKTKRQTFQDYIDTLIDTQKESKKKLKTQALKELREYLNGIITTSSSETFITWQQLLNHYVFDKSKRYMANRHFKVLTHEDVLNEYLKIVNTIENDLQNKLNELRLRNYTRDRIARDNFKSLLREVPIKIKANTRWSDIYPHIKSDPRFLHMLGRNGSSCLDLFLDFVDEQRMYIFAQRSIAQQTLIDQNFEWNDADSDEITKQNIEKVLENDRKFDKVDKEDISLIVDGLIKQRNEKIQQKLQNERRILEQKKHYFWLLLQRTYTKTGKPKPSTWDLASKELGESLEYKALGDEDNIRRQIFEDFKPESSAPTAESATANLTLTASKKRHLTPAVELDY
Protein: Auxin-responsive protein IAA21 (Indoleacetic acid-induced protein 21) (Q5Z749)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Aux/IAA proteins are short-lived transcriptional factors that function as repressors of early auxin response genes at low auxin concentrations.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Auxin response factor 11
- Transport inhibitor response 1-like protein Os05g0150500
- Auxin response factor 9
- Auxin response factor 7
- Auxin response factor 3
- Auxin response factor 15
- Auxin response factor 14
- Auxin response factor 1
- Auxin response factor 16
Sequence:
MAPPQERDYIGLSPAAAAALATELRLGLPGTAEEAESEGGGGGGTDAAPLTLELLPKGGAKRGFADAIVGGPAGQRREAAGGKAAAAAAEAEEEEEKKKAQAPAAKAQVVGWPPIRSYRKNTMAMSQPALKGKDDGEAKQAPASGCLYVKVSMDGAPYLRKVDLKMYKNYKELSLALEKMFSCFTVGHGESNGKSGRDGLSDCRLMDLKNGTELVLTYEDKDEDWMLVGDVPWRMFTDSCRRLRIMKGSDAVGLAPRATDKSKNRN
Protein: J domain-containing protein (Q9TY07)
Organism: Caenorhabditis elegans
Interaction partners:
- Heat shock protein hsp-1
- Heat shock protein 110
- Heat shock protein 70
- Heat shock 70 kDa protein C
- DUF148 domain-containing protein
- Heat shock protein hsp-6
- Heat-shock protein 12.1
- BAG domain-containing protein
- Activator of Hsp90 ATPase AHSA1-like N-terminal domain-containing protein
- Heat shock protein 70
Sequence:
MAPREDSPYITLGISSTSDDVEIKKAYRKLALKWHPDKHTDDKSKEEAEQKFKKIAQAYEILTDKKKRADLDRTENPGLHRRRSTPGGMHRMHSHDMFRSPFDIFREFFGNRDPFENVFFDDAFTFPDVDSYAFKHPPRSADFTTKNHYHRFPSSRVHIFYDENKNTKERDDKNTFSTVIRFSSPTEPGKNATVRKTSTSTKLVDGKKIVTKTVENGDEHIVEVHEDGELKCRTVTTPPTSPTVTVAAI
Protein: Putative bifunctional exonuclease/endonuclease protein Rv2191 (EC 3.1.-.-) (P9WLJ1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- UvrABC system protein B
- DNA polymerase III subunit alpha
- DNA polymerase III subunit delta'
- Beta sliding clamp
- Probable DNA polymerase III subunit delta
- DNA polymerase III subunit gamma/tau
- Probable DNA polymerase III
- DNA polymerase I
- DNA 3'-5' helicase
- Error-prone DNA polymerase
Sequence:
MQGPNVAAMGATGGTQLSFADLAHAQGAAWTPADEMSLRETTFVVVDLETTGGRTTGNDATPPDAITEIGAVKVCGGAVLGEFATLVNPQHSIPPQIVRLTGITTAMVGNAPTIDAVLPMFFEFAGDSVLVAHNAGFDIGFLRAAARRCDITWPQPQVLCTMRLARRVLSRDEAPSVRLAALARLFAVASNPTHRALDDARATVDVLHALIERVGNQGVHTYAELRSYLPNVTQAQRCKRVLAETLPHRPGVYLFRGPSGEVLYVGTAADLRRRVSQYFNGTDRRKRMTEMVMLASSIDHVECAHPLEAGVRELRMLSTHAPPYNRRSKFPYRWWWVALTDEAFPRLSVIRAPRHDRVVGPFRSRSKAAETAALLARCTGLRTCTTRLTRSARHGPACPELEVSACPAARDVTAAQYAEAVLRAAALIGGLDNAALAAAVQQVTELAERRRYESAARLRDHLATAIEALWHGQRLRALAALPELIAAKPDGPREGGYQLAVIRHGQLAAAGRAPRGVPPMPVVDAIRRGAQAILPTPAPLGGALVEEIALIARWLAEPGVRIVGVSNDAAGLASPVRSAGPWAAWAATARSAQLAGEQLSRGWQSDLPTEPHPSREQLFGRTGVDCRTGPPQPLLPGRQPFSTAG
Protein: Uncharacterized protein C1002.01 (Q9US57)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MLPPTIRISGLAKTLHIPSRSPLQALKGSFILLNKRKFHYSPFILQEKVQSSNHTIRSDTKLWKRLLKITGKQAHQFKDKPFSHIFAFLFLHELSAILPLPIFFFIFHSLDWTPTGLPGEYLQKGSHVAASIFAKLGYNLPLEKVSKTLLDGAAAYAVVKVSYFVENNMVSSTRPFVSN
Protein: Zinc transporter Slc39a7 (Q20693)
Organism: Caenorhabditis elegans
Interaction partners:
- VWFA domain-containing protein
- C-type lectin domain-containing protein
- Lysozyme-like protein 5
- C-type LECtin
- C-type lectin domain-containing protein
- Invertebrate-type lysozyme 3
- Flavin-containing monooxygenase
- Saposin B-type domain-containing protein
- C-type lectin domain-containing protein
Sequence:
MSHQEHGHGDGDHHDHHDEHHHEDHHEHGADGEHVHHAGDHCDTQHGGNHQAGEHCAKTQHQDGEHHEQHHDAHDSHAHDSHEGHQH
Protein: Small ribosomal subunit protein uS9B (40S ribosomal protein S16-B) (P0CT65)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Large ribosomal subunit protein uL5B
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS2A
- Small ribosomal subunit protein eS7
- Small ribosomal subunit protein uS15
- Elongation factor 3
- Small ribosomal subunit protein uS14
- Small ribosomal subunit protein eS30B
Sequence:
MQSVQCFGKKGNATAVAHCKVGKGLIKVNGAPLSLVQPEILRMKVYEPILVAGADKFAGVDIRVRVSGGGHVSQIYAIRQAISKAIVAYYQKFVDEHSKAELKKALITYDRTLLVADPRRMEPKKFGGHGARARQQKSYR