wanglab/gogpt-training-data huggingface dataset:
Protein: Sarcoplasmic/endoplasmic reticulum calcium ATPase 1 (SERCA1) (SR Ca(2+)-ATPase 1) (EC 7.2.2.10) (Calcium pump 1) (Calcium-transporting ATPase sarcoplasmic reticulum type, fast twitch skeletal muscle isoform) (Endoplasmic reticulum class 1/2 Ca(2+) ATPase) (Q8R429)
Organism: Mus musculus (Mouse)
Function: Key regulator of striated muscle performance by acting as the major Ca(2+) ATPase responsible for the reuptake of cytosolic Ca(2+) into the sarcoplasmic reticulum. Catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Contributes to calcium sequestration involved in muscular excitation/contraction.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P04191}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P04191}. Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:26816378}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P04191}.
Interaction partners:
- Sarcolipin
- Troponin T, fast skeletal muscle
- Phospholamban
- Troponin I, fast skeletal muscle
- Troponin C, skeletal muscle
- Ryanodine receptor 1
- Histidine rich calcium binding protein
- Myosin regulatory light chain 11
- Calsequestrin-1
- Sarcoplasmic/endoplasmic reticulum calcium ATPase 2
Sequence:
MEAAHSKSTEECLSYFGVSETTGLTPDQVKRHLEKYGPNELPAEEGKSLWELVVEQFEDLLVRILLLAACISFVLAWFEEGEETVTAFVEPFVILLILIANAIVGVWQERNAENAIEALKEYEPEMGKVYRADRKSVQRIKARDIVPGDIVEVAVGDKVPADIRILSIKSTTLRVDQSILTGESVSVIKHTDPVPDPRAVNQDKKNMLFSGTNIAAGKAVGIVATTGVSTEIGKIRDQMAATEQDKTPLQQKLDEFGEQLSKVISLICVAVWLINIGHFNDPVHGGSWFRGAIYYFKIAVALAVAAIPEGLPAVITTCLALGTRRMAKKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVCKMFIIDKVDGDVCSLNEFSITGSTYAPEGEVLKNDKPVRAGQYDGLVELATICALCNDSSLDFNETKGVYEKVGEATETALTTLVEKMNVFNTEVRSLSKVERANACNSVIRQLMKKEFTLEFSRDRKSMSVYCSPAKSSRAAVGNKMFVKGAPEGVIDRCNYVRVGTTRVPLTGPVKEKIMSVIKEWGTGRDTLRCLALATRDTPPKREEMVLDDSAKFMEYEMDLTFVGVVGMLDPPRKEVTGSIQLCRDAGIRVIMITGDNKGTAIAICRRIGIFSENEEVTDRAYTGREFDDLPLAEQREACRRACCFARVEPSHKSKIVEYLQSYDEITAMTGDGVNDAPALKKAEIGIAMGSGTAVAKTASEMVLADDNFSTIVAAVEEGRAIYNNMKQFIRYLISSNVGEVVCIFLTAALGLPEALIPVQLLWVNLVTDGLPATALGFNPPDLDIMDRPPRSPKEPLISGWLFFRYMAIGGYVGAATVGAAAWWFLYAEDGPHVSYHQLTHFMQCTEHNPEFDGLDCEVFEAPEPMTMALSVLVTIEMCNALNSLSENQSLLRMPPWVNIWLLGSICLSMSLHFLILYVDPLPMIFKLRALDFTQWLMVLKISLPVIGLDELLKFIARNYLEG
Protein: Acetate kinase EutQ (EC 2.7.2.1) (Ethanolamine utilization protein EutQ) (Q9ZFV5)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: A bidirectional acetate kinase that may drive flux through the ethanolamine (EA) degradation pathway under anoxic conditions found when this bacteria infects the host intestine. It may generate ATP that can be used by other enzymes (EutA and EutT) in the eut pathway. Can use GTP instead of ATP with reduced efficiency. Might be required to correctly target EutE to bacterial microcompartments (BMC) (Probable). Required for the biogenesis of multiple mobile BMCs per cell. Might serve as an assembly hub for BMC shell proteins. Expression of eutK, eutL, eutM, eutN, eutS (eutSMNLK) in E.coli leads to formation of a single BMC; coexpression of eutQ with eutSMNLK permits E.coli to make cells with more than one mobile BMC, as is usual in vivo. EutS alone also forms BMCs, but in the presence of eutQ both BMCs and protein filaments are formed.
Subcellular location: Bacterial microcompartment {ECO:0000305|PubMed:26448059, ECO:0000305|PubMed:27063436}. Note=May be found on the cytoplasmic face of the BMC. {ECO:0000305|PubMed:27063436}.
Interaction partners:
- Probable acetate kinase EutP
- Corrinoid adenosyltransferase EutT
- Ethanolamine ammonia-lyase reactivase EutA
- Ethanolamine ammonia-lyase small subunit
- Bacterial microcompartment shell protein EutS
- Phosphate acetyltransferase EutD
- Ethanolamine utilization protein EutJ
- Bacterial microcompartment shell protein EutL
- Probable ethanolamine permease EutH
- Ethanolamine ammonia-lyase large subunit
Sequence:
MKKLITANDIRAAHARGEQAMSVVLRASIITPEAREVAELLGFTITECDESVPASTSAQACKSESQRIREAIIAQLPEGQFTESLVAQLMEKVLKEKQSLELGTMQPSFTSVTGKGGVKVIDGSSVKFGRFDGAEPHCVGLTDLVTEQDGSSMAAGFMQWDNAFFPWTLNYDEIDMVLEGELHVRHEGETMIAKAGDVMFIPKGSSIEFGTPTSVRFLYVAWPANWQSV
Protein: G-protein coupled receptors family 1 profile domain-containing protein (Q8MQC4)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- Protein kinase domain-containing protein
- Nematode cuticle collagen N-terminal domain-containing protein
- RUN domain-containing protein
- Uncharacterized protein
- Coelomocyte uptake defective protein 15
Sequence:
MAFSLSQRVVETMPSGTWNDFTDLPAEFISQFGSSSEAMQYSCYYSDSFIRFATAMDDVLIGACLISTVINFIVIACSAKLYKKKGDTLHLFILNMTIGDTILTLFCHPYELVTRRYSGAHVHFITVFLNFANWVGLAVSGLSLTLLNIDKLIFFCWPFKYDIWMSYFRAKLFCYLSWIISIGFATYYWMYSYMYFVNATVDIQQQFEIQFVFLTGLMNSGQFSPVNKIFYEVFTVVFCVIPIVSSLLVSCYLYDLTKRKRKTVIKTSSASKIENKATSFAFIFATTLWTSCSLLPYRIANLARIHIIAWPNLDCESRQNLSWLTWSMLYLLILNPIINPLITAFAYAPYRQMIYSRVRKSSRKNYQDQNSYETNKSNITSTNSVSSKVFYVDLTMAKQNHTKTLRKAPLAKFPSICSCGSFVTNENLQCTRF
Protein: Syncrip, isoform Q (A0A0B4KHI4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MLSQMEASKVQKDEGGGEALSRTILKTPSSFRTPSPIPSCSKMAEGNGELLDDINQKADDRGDGERTEDYPKLLEYGLDKKVAGKLDEIYKTGKLAHAELDERALDALKEFPVDGALNVLGQFLESNLEHVSNKSAYLCGVMKTYRQKSRASQQGVAAPATVKGPDEDKIKKILERTGYTLDVTTGQRKYGGPPPHWEGNVPGNGCEVFCGKIPKDMYEDELIPLFENCGIIWDLRLMMDPMTGTNRGYAFVTFTNREAAVNAVRQLDNHEIKPGKCLKINISVPNLRLFVGNIPKSKGKDEILEEFGKLTAGLYEVIIYSSPDDKKKNRGFCFLEYESHKAASLAKRRLGTGRIKVWGCDIIVDWADPQEEPDEQTMSKVKVLYVRNLTQDVSEDKLKEQFEQYGKVERVKKIKDYAFIHFEDRDSAVEAMRGLNGKEIGASNIEVSLAKPPSDKKKKEEILRARERRMMQMMQARPGIVGFETLSPYRNLSPTHPSIMSLTPMRPGARMPLRTPIPREYDYFYDFFGFSDYRQGGSFGNNVSYYDDMYRWIDGDYNYYDYPNGGGGGSGGGGGSVSGGTVLPLSAGGSQNSPMASGQRSARGSASGPSASPSLMGVGRGHGITVPRGRVVGQRGSISRLGAQTVPQAAGAAAAAGQAAAAVAQRGATGQGAPAATGGFRGVLPTRPSARGTQHVKPLQNLPVVGKRKFDGGHQNPADVKRRYPSGLIGNGGSWGSLPLPQQPLGTNGEQWYMDTFSAWS
Protein: SUMO specific peptidase 6 (F8W6D9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAAGKSGGSAGEITFLEALARSESKRDGGFKNNWSFDHEEESEGDTDKDGTNLLSVDEDEDSETSKGKKLNRRSEIVANSSGEFILKTYVRRNKSESFKTLKGNPIGLNMLSNNKKLSENTQNTSLCSGTVVHGRRFHHAHAQIPVVKTAAQRKEYPPHVQKVEINPVRLSRLQGVERIMKKTEESESQVEPEIKRKVQQKRHCSTYQPTPPLSPASKKCLTHLEDLQRNCRQAITLNESTGPLLRTSIHQNSGGQKSQNTGLTTKKFYGNNVEKVPIDIIVNCDDSKHTYLQTNGKVILPGAKIPKITNLKERKTSLSDLNDPIILSSDDDDDNDRTNRRESISPQPADSACSSPAPSTGKVEAALNENTCRAERELRSIPEDSELNTVTLPRKARMKDQFGNSIINTPLKRRKVFSQEPPDALALSCQSSFDSVILNCRSIRVGTLFRLLIEPVIFCLDFIKIQLDEPDHDPVEIILNTSDLTKCEWCNVRKLPVVFLQAIPAVYQKLSIQLQMNKEDKVWNDCKGVNKLTNLEEQYIILIFQNGLDPPANMVFESIINEIGIKNNISNFFAKIPFEEANGRLVACTRTYEESIKGSCGQKENKIKTVSFESKIQLRSKQEFQFFDEEEETGENHTIFIGPVEKLIVYPPPPAKGGISVTNEDLHCLNEGEFLNDVIIDFYLK
Protein: ATP-dependent RNA helicase DBP2 (EC 3.6.4.13) (DEAD box protein 2) (p68-like protein) (P24783)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: ATP-dependent RNA helicase involved nonsense-mediated mRNA decay and ribosome biogenesis through rRNA processing. Associates directly with chromatin, correlating with transcriptional activity. Required for assembly of mRNA-binding proteins YRA1, NAB2, and MEX67 onto poly(A)+ RNA.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22679025}.
Interaction partners:
- Nuclear localization sequence-binding protein
- Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP43
- RNA annealing protein YRA1
- ATP-dependent RNA helicase HAS1
- Nucleolar GTP-binding protein 1
- H/ACA ribonucleoprotein complex subunit CBF5
- Nucleolar GTP-binding protein 2
- Proteasome-interacting protein CIC1
- Protein arginine N-methyltransferase 1
- Ribosome biogenesis protein BMS1
Sequence:
MTYGGRDQQYNKTNYKSRGGDFRGGRNSDRNSYNDRPQGGNYRGGFGGRSNYNQPQELIKPNWDEELPKLPTFEKNFYVEHESVRDRSDSEIAQFRKENEMTISGHDIPKPITTFDEAGFPDYVLNEVKAEGFDKPTGIQCQGWPMALSGRDMVGIAATGSGKTLSYCLPGIVHINAQPLLAPGDGPIVLVLAPTRELAVQIQTECSKFGHSSRIRNTCVYGGVPKSQQIRDLSRGSEIVIATPGRLIDMLEIGKTNLKRVTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVKQLAADYLNDPIQVQVGSLELSASHNITQIVEVVSDFEKRDRLNKYLETASQDNEYKTLIFASTKRMCDDITKYLREDGWPALAIHGDKDQRERDWVLQEFRNGRSPIMVATDVAARGIDVKGINYVINYDMPGNIEDYVHRIGRTGRAGATGTAISFFTEQNKGLGAKLISIMREANQNIPPELLKYDRRSYGGGHPRYGGGRGGRGGYGRRGGYGGGRGGYGGNRQRDGGWGNRGRSNY
Protein: 3,2-trans-enoyl-CoA isomerase (EC 5.3.3.8) (Delta(3),Delta(2)-enoyl-CoA isomerase) (D3,D2-enoyl-CoA isomerase) (Dodecenoyl-CoA isomerase) (Q05871)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Essential for the beta oxidation of unsaturated fatty acids.
Subcellular location: Peroxisome {ECO:0000269|PubMed:10381339, ECO:0000269|PubMed:11302517, ECO:0000269|PubMed:9837886}. Note=This location is DCI1 dependent.
Interaction partners:
- Delta
- Acyl-coenzyme A oxidase
- Peroxisomal hydratase-dehydrogenase-epimerase
- Peroxisomal 2,4-dienoyl-CoA reductase SPS19 [
- 3-ketoacyl-CoA thiolase, peroxisomal
- Acetyl-CoA acetyltransferase
- Peroxisomal acyl-coenzyme A thioester hydrolase 1
- Large ribosomal subunit protein bL33m
- Peroxisomal catalase A
- Large ribosomal subunit protein mL43
Sequence:
MSQEIRQNEKISYRIEGPFFIIHLMNPDNLNALEGEDYIYLGELLELADRNRDVYFTIIQSSGRFFSSGADFKGIAKAQGDDTNKYPSETSKWVSNFVARNVYVTDAFIKHSKVLICCLNGPAIGLSAALVALCDIVYSINDKVYLLYPFANLGLITEGGTTVSLPLKFGTNTTYECLMFNKPFKYDIMCENGFISKNFNMPSSNAEAFNAKVLEELREKVKGLYLPSCLGMKKLLKSNHIDAFNKANSVEVNESLKYWVDGEPLKRFRQLGSKQRKHRL
Protein: Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1 (Oligosaccharyl transferase subunit DAD1) (Defender against cell death 1) (AtDAD1) (DAD-1) (Q39080)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1B
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1A
- Probable dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 3A
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B
- Probable dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 3B
- Dolichyl-diphosphooligosaccharide-protein glycosyltransferase subunit OST5
- AT2G34250 protein
Sequence:
MVKSTSKDAQDLFRSLRSAYSATPTNLKIIDLYVVFAVFTALIQVVYMALVGSFPFNSFLSGVLSCIGTAVLAVCLRIQVNKENKEFKDLAPERAFADFVLCNLVLHLVIINFLG
Protein: Serine/threonine-protein kinase SIK2 (EC 2.7.11.1) (Qin-induced kinase) (Salt-inducible kinase 2) (SIK-2) (Serine/threonine-protein kinase SNF1-like kinase 2) (Q9IA88)
Organism: Gallus gallus (Chicken)
Function: Phosphorylates IRS1 in insulin-stimulated adipocytes, potentially modulating the efficiency of insulin signal transduction. Inhibits CREB activity by phosphorylating and repressing the CREB-specific coactivators, CRTC1-3 (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11027514}.
Interaction partners:
Sequence:
MVIMSEDASVPAPSAAQPRPLRVGFYDIERTLGKGNFAVVKLARHRVTKTQVAIKIIDKTRLDPSNLEKIYREVQIMKLLNHPHIIKLYQVMETKDMLYIVTEFAKNGEMFDHLTSNGHLSESEARKKFWQILSAVEYCHSHHIVHRDLKTENLLLDANMNIKLADFGFGNFYKSGEPLSTWCGSPPYAAPEVFEGKEYEGPHLDIWSLGVVLYVLVCGSLPFDGPNLPTLRQRVLEGRFRIPYFMSEDCETLIRRMLVVDPTKRITISQIKQHKWMQADPSLRQQQSLSFSMQNYNSNLGDYNEQVLGIMQTLGIDRQRTVESLQNSSYNHFAAIYYLLLERLKEYRSSQLSSRPATGRQQRPRSSEISNAEMPQDSLTSETLRSSLLYQQPQSLIQPSLQAEMDCDMNNPLQPVFFPVDPNFNGLFRNRSISPSSLLETTISEEVRQEKELEDEIKAYDHPIRIPSNTSRRHTLAEVTTHFYQHAPPCIVISSSASPTEGTSSDSCLTSSSNDSSVALSSCLAGQVMTGSPATARMTSAFLASQSDAPVLQVQGCMGGASLLPVSFQEGRRASDTSLTQGLKAFRQQLRKNARAKGFLGLNKIKGFARQVCQSSSSRAARSAMSPFQHAQPNTCIYSSSGSSREGRNLLEEVLQQQRMLQLQHHQLLQPACPQTSQTSATNGLPPSDSAGTCKASNSLLLSELQRENSFELAFGGNSQLLQPHFFGVSVSPVSSAAHLLDTHLYISSNVSPVGTTFSQQQSFSAQSPSYDAVTLQHGDCEMEDLTSNQLGKFVLVK
Protein: ORF 41 (P88929)
Organism: Human herpesvirus 8 type M
Interaction partners:
Sequence:
MAGFTLKGGTSGDLVFSSHANLLFSTSMGYFLHAGSPRSTAGTGGEPNPRHITGPDTEGNGEHRNSPNLCGFVTWLQSLTTCIERALNMPPDTSWLQLIEEVIPLYFHRRRQTSFWLIPLSHCEGIPVCPPLPFDCLAPRLFIVTKSGPMCYRAGFSLPVDVNYLFYLEQTLKAVRQVSPQEHNPQDAKEMTLQLEAWTRLLSLF
Protein: thioredoxin-dependent peroxiredoxin (EC 1.11.1.24) (A2AWE1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Sulfiredoxin
- Thioredoxin
- Peroxiredoxin-2
- Peroxiredoxin
- Thioredoxin
- Glutathione S-transferase
- Glutamate--cysteine ligase
- Glutathione reductase
- Superoxide dismutase
- Endoplasmic reticulum protein 44)
Sequence:
MAAGNAHIGKPAPDFTAKAVMPDGQFGDVRLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSDAAEEFRKINCEIIGASVDSHFCHLAWTKTPRKQGGLGPMNVPLVADTLRSISKDYGVLKEDEGIAYRGLFIIDDKGILRQITINDLPVGRSIDETLRLVQAFQFTDKHGEVCPAGWKPGKDTIKPDVNQSKDFFSKQN
Protein: Centriole protein (A9CQL4)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|ARBA:ARBA00004300}.
Interaction partners:
- Uncharacterized protein
- 3'-5' exonuclease domain-containing protein
- Basal body protein 10
- Replication protein A subunit
- Replication protein A subunit
- DNA primase large subunit
- Proliferating cell nuclear antigen
- Uncharacterized protein
- Histone H1
- DNA primase
Sequence:
MPLLLDDGDPKAQTGFDLSTATTLFWRPVPVHVKQQDREDVLEELTFRILTGVAKQNHNLRILRIHISSDSDLFFLHTLEVSEEDFQSLKNDQGILVDFASFPGKIISLLEKCILAQPGDSPRFQAVLTIRGGESVFKIVEINDFKQLPHITLAFRPGNDSVVKQFLAFRLSEVKGTCHDLSDDLSRTRDDRDSMVAQLAQCRQQLAQLREQYDKHLLEVQAQAKTQQASAHEERIREKSQLKDQFEKERGEMEGRYRDQIAALNTRLGELDTENRKLREVKYELDTKVSELSHKLGSSEGSNRSLEEETARLRSLNQQLSSSKHELEIQLNEAKAKVLALDEKAQSQGDVIEQQRGRLRDMEAALRQTEQRCADLRDTLASAEGRAKEAQAEVLKGNQAIEKLTNDLRLAKEKTKRKAAIILRQEEELQEREQSLANATRDVGVLGQQAESLRKDVASLHSENDSLRSKLEDSKQQLQSNEQMIRWLNQQVTEAQLHASGATVAGSRYAFRPSAALPGSMPPPSVAATPAVGLLAAPGPSTAYKPGGTTSRYASTLGVTGLSSGLSGAGATSVGAAVAGGSYGAGGDSSYRPGVGGAYASSGGAGGFGGSVGGGGQVGGSGSAIGAATGAGSALGTYRSSYAASTHPSPGGVTAGMGSTLTTPAVNRYAAGSYSSVSSSLSFGGGLGAARAVDATPAASKYGVGFSNAAMGVVGTVGGAGGTDAQRA
Protein: Transcription factor MYB62 (Myb-related protein 62) (AtMYB62) (Q9C9G7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription repressor of phosphate (Pi) starvation-induced genes. Regulates negatively Pi starvation responses via the repression of gibberellic acid (GA) biosynthesis and signaling. Modulates root architecture, phosphatase activity, and Pi uptake and accumulation.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:19529828}.
Interaction partners:
- Zinc finger protein ZAT6
- Probable WRKY transcription factor 75
- Protein PHOSPHATE STARVATION RESPONSE 1
- Transcription factor AIG1
- Inorganic phosphate transporter 1-1
- Phosphate transporter PHO1
- Probable WRKY transcription factor 45
- Probable ubiquitin-conjugating enzyme E2 24
- WRKY transcription factor 6
- WRKY transcription factor 42
Sequence:
MENSMKKKKSFKESEDEELRRGPWTLEEDTLLTNYILHNGEGRWNHVAKCAGLKRTGKSCRLRWLNYLKPDIRRGNLTPQEQLLILELHSKWGNRWSKIAQYLPGRTDNEIKNYWRTRVQKQARQLNIESNSDKFFDAVRSFWVPRLIEKMEQNSSTTTTYCCPQNNNNNSLLLPSQSHDSLSMQKDIDYSGFSNIDGSSSTSTCMSHLTTVPHFMDQSNTNIIDGSMCFHEGNVQEFGGYVPGMEDYMVNSDISMECHVADGYSAYEDVTQDPMWNVDDIWQFRE
Protein: Photosynthetic apparatus regulatory protein RegA (P42508)
Organism: Rhodobacter capsulatus (Rhodopseudomonas capsulata)
Function: Member of the two-component regulatory system RegB/RegA. Involved in transactivating anaerobic expression of the photosynthetic apparatus. It is a transcriptional regulator that is responsible for activating expression of the puf, puh, and puc operons in response to a decrease in oxygen tension.
Interaction partners:
Sequence:
MAEEEFAELGSDRSLLLVDDDNAFLTRLARAMEKRGFQTEIAETVSAGKAIVQNRAPAYAVIDLRLEDGNGLEVVEALRERRPEARIVVLTGYGAIATAVAAVKMGATDYLSKPADANDITNALLAKGEALPPPPENPMSADRVRWEHIQRVYELCDRNVSETARRLNMHRRTLQRILAKRSPR
Protein: Probable conserved membrane protein (O69658)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Uncharacterized membrane protein Rv3691
- Probable conserved transmembrane protein
- Possible conserved membrane protein
- Probable methanol dehydrogenase transcriptional regulatory protein MoxR2
- Possible conserved transmembrane protein
- Possible conserved membrane protein
- Conserved protein
Sequence:
MPSIDIDREAAHQAAQRELDKPIYPKDSLTKELTDWIDEQLYRILEKGSSIPGGWFTITVLLILLMIAVTAAVQIARRTMRTNRGGDYQLFDAGQLTAAQHRSTAESYAAEGNWAAAIRHRLQAVARELEETGMLNPAAGRTANELASDAGEVLPHLAGELTQAATAFNDVTYGERPGTQGAYQMIADLDDHLRSRSPAVVSAVQHPAVFDSWAQVR
Protein: Oxysterol-binding protein-related protein 2 (ORP-2) (OSBP-related protein 2) (Q9H1P3)
Organism: Homo sapiens (Human)
Function: Intracellular transport protein that binds sterols and phospholipids and mediates lipid transport between intracellular compartments. Increases plasma membrane cholesterol levels and decreases phosphatidylinositol-4,5-bisphosphate levels in the cell membrane. Binds phosphoinositides, such as phosphatidylinositol-4,5-bisphosphate. Exhibits strong binding to phosphatidic acid and weak binding to phosphatidylinositol 3-phosphate. Binds cholesterol, dehydroergosterol, 22(R)-hydroxycholesterol and 25-hydroxycholesterol (in vitro).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:19224871, ECO:0000269|PubMed:30581148}. Lipid droplet {ECO:0000269|PubMed:19224871}. Cell membrane {ECO:0000269|PubMed:30581148}; Peripheral membrane protein {ECO:0000269|PubMed:30581148}; Cytoplasmic side {ECO:0000269|PubMed:30581148}. Note=Detected on the surface of cytosolic lipid droplets (PubMed:19224871). Recruited to the cell membrane by phosphatidylinositol-phosphate binding (PubMed:30581148). {ECO:0000269|PubMed:19224871, ECO:0000269|PubMed:30581148}.
Interaction partners:
- Proteasomal ubiquitin receptor ADRM1
- Vesicle-associated membrane protein-associated protein B/C
- Vesicle-associated membrane protein-associated protein A
Sequence:
MNGEEEFFDAVTGFDSDNSSGEFSEANQKVTGMIDLDTSKNNRIGKTGERPSQENGIQKHRTSLPAPMFSRSDFSVWTILKKCVGLELSKITMPIAFNEPLSFLQRITEYMEHVYLIHRASCQPQPLERMQSVAAFAVSAVASQWERTGKPFNPLLGETYELIREDLGFRFISEQVSHHPPISAFHSEGLNHDFLFHGSIYPKLKFWGKSVEAEPRGTITLELLKHNEAYTWTNPTCCVHNVIIGKLWIEQYGTVEILNHRTGHKCVLHFKPCGLFGKELHKVEGHIQDKNKKKLFMIYGKWTECLWGIDPVSYESFKKQERRGDHLRKAKLDEDSGKADSDVADDVPVAQETVQVIPGSKLLWRINTRPPNSAQMYNFTSFTVSLNELETGMEKTLPPTDCRLRPDIRGMENGNMDLASQEKERLEEKQREARRERAKEEAEWQTRWFYPGNNPYTGTPDWLYAGDYFERNFSDCPDIY
Protein: Sodium/pantothenate symporter (Pantothenate permease) (P16256)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the sodium-dependent uptake of extracellular pantothenate.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Uncharacterized membrane protein YhdT
- Ribosomal protein L11 methyltransferase
- DNA-binding protein Fis
- tRNA-dihydrouridine synthase B
- Pantothenate synthetase
- Biotin carboxylase
Sequence:
MQLEVILPLVAYLVVVFGISVYAMRKRSTGTFLNEYFLGSRSMGGIVLAMTLTATYISASSFIGGPGAAYKYGLGWVLLAMIQLPAVWLSLGILGKKFAILARRYNAVTLNDMLFARYQSRLLVWLASLSLLVAFVGAMTVQFIGGARLLETAAGIPYETGLLIFGISIALYTAFGGFRASVLNDTMQGLVMLIGTVVLLIGVVHAAGGLSNAVQTLQTIDPQLVTPQGADDILSPAFMTSFWVLVCFGVIGLPHTAVRCISYKDSKAVHRGIIIGTIVVAILMFGMHLAGALGRAVIPDLTVPDLVIPTLMVKVLPPFAAGIFLAAPMAAIMSTINAQLLQSSATIIKDLYLNIRPDQMQNETRLKRMSAVITLVLGALLLLAAWKPPEMIIWLNLLAFGGLEAVFLWPLVLGLYWERANAKGALSAMIVGGVLYAVLATLNIQYLGFHPIVPSLLLSLLAFLVGNRFGTSVPQATVLTTDK
Protein: DNA polymerase delta catalytic subunit (EC 2.7.7.7) (3'-5' exodeoxyribonuclease) (EC 3.1.11.-) (DNA polymerase III) (P15436)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalytic component of DNA polymerase delta (DNA polymerase III) which participates in chromosomal DNA replication. Required during synthesis of the lagging DNA strands at the replication fork, binds at/or near replication origins and moves along DNA with the replication fork. Participates in leading strand synthesis during replication initiation and termination. Has 3'-5' proofreading exonuclease activity that corrects errors arising during DNA replication.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- DNA polymerase delta subunit 3
- Proliferating cell nuclear antigen
- DNA polymerase epsilon catalytic subunit A
- DNA polymerase delta small subunit
- DNA primase large subunit
- Flap endonuclease 1
- DNA primase small subunit
- DNA polymerase alpha subunit B
- DNA polymerase epsilon subunit B
- DNA polymerase zeta processivity subunit
Sequence:
MSEKRSLPMVDVKIDDEDTPQLEKKIKRQSIDHGVGSEPVSTIEIIPSDSFRKYNSQGFKAKDTDLMGTQLESTFEQELSQMEHDMADQEEHDLSSFERKKLPTDFDPSLYDISFQQIDAEQSVLNGIKDENTSTVVRFFGVTSEGHSVLCNVTGFKNYLYVPAPNSSDANDQEQINKFVHYLNETFDHAIDSIEVVSKQSIWGYSGDTKLPFWKIYVTYPHMVNKLRTAFERGHLSFNSWFSNGTTTYDNIAYTLRLMVDCGIVGMSWITLPKGKYSMIEPNNRVSSCQLEVSINYRNLIAHPAEGDWSHTAPLRIMSFDIECAGRIGVFPEPEYDPVIQIANVVSIAGAKKPFIRNVFTLNTCSPITGSMIFSHATEEEMLSNWRNFIIKVDPDVIIGYNTTNFDIPYLLNRAKALKVNDFPYFGRLKTVKQEIKESVFSSKAYGTRETKNVNIDGRLQLDLLQFIQREYKLRSYTLNAVSAHFLGEQKEDVHYSIISDLQNGDSETRRRLAVYCLKDAYLPLRLMEKLMALVNYTEMARVTGVPFSYLLARGQQIKVVSQLFRKCLEIDTVIPNMQSQASDDQYEGATVIEPIRGYYDVPIATLDFNSLYPSIMMAHNLCYTTLCNKATVERLNLKIDEDYVITPNGDYFVTTKRRRGILPIILDELISARKRAKKDLRDEKDPFKRDVLNGRQLALKISANSVYGFTGATVGKLPCLAISSSVTAYGRTMILKTKTAVQEKYCIKNGYKHDAVVVYGDTDSVMVKFGTTDLKEAMDLGTEAAKYVSTLFKHPINLEFEKAYFPYLLINKKRYAGLFWTNPDKFDKLDQKGLASVRRDSCSLVSIVMNKVLKKILIERNVDGALAFVRETINDILHNRVDISKLIISKTLAPNYTNPQPHAVLAERMKRREGVGPNVGDRVDYVIIGGNDKLYNRAEDPLFVLENNIQVDSRYYLTNQLQNPIISIVAPIIGDKQANGMFVVKSIKINTGSQKGGLMSFIKKVEACKSCKGPLRKGEGPLCSNCLARSGELYIKALYDVRDLEEKYSRLWTQCQRCAGNLHSEVLCSNKNCDIFYMRVKVKKELQEKVEQLSKW
Protein: Non-structural maintenance of chromosome element 4 (Non-SMC element 4) (Protein QRI2) (P43124)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acts in a DNA repair pathway for removal of UV-induced DNA damage that is distinct from classical nucleotide excision repair and in repair of ionizing radiation damage. Functions in homologous recombination repair of DNA double strand breaks and in recovery of stalled replication forks.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15752197}.
Interaction partners:
- Structural maintenance of chromosomes protein 5
- E3 SUMO-protein ligase MMS21
- Non-structural maintenance of chromosome element 3
- Structural maintenance of chromosomes protein 6
- Non-structural maintenance of chromosomes element 1
- DNA repair protein KRE29
- Non-structural maintenance of chromosome element 5
- Structural maintenance of chromosomes protein 3
- Altered inheritance of mitochondria protein 18, mitochondrial
- Altered inheritance of mitochondria protein 46, mitochondrial
Sequence:
MSSTVISRKRRNSTVTEPDSSGETRKQKKSRSDEKSSSSKDGDPQLEFKVLQGYRDLESEMHKGRAQVTRTGDIGVAMDNLNAVDSLFNKVIGIKNNGLFAHDARAMVSISELAQISVRNLKFDDSRSMVNLENIVNSLKRYMLKEHFKLNNIAENRNDLTLAADEQSAADQQEESDGDIDRTPDDNHTDKATSSFKATSMRHSYLQQFSHYNEFSQFNWFRIGALYNTISKNAPITDHLMGPLSIEKKPRVLTQRRRNNDQVGEKITAEKITQHSLNSTQQETTPEQVKKCFKKLSKKLGPEGSINLFKFIIDPNSFSRSIENLFYTSFLIKEGKLLMEHDEEGLPTIKIKQSISHTDSRSKEIERQRRRAAHQNHIIFQMDMPTWRKLIKKYNITSPFLD