wanglab/gogpt-training-data huggingface dataset:
Protein: Beta-ureidopropionase (EC 3.5.1.6) (N-carbamoyl-beta-alanine amidohydrolase) (Protein PYRIMIDINE 3) (Q8H183)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes a late step in pyrimidine degradation. Converts N-carbamoyl-beta-aminoisobutyrate and N-carbamoyl-beta-alanine (3-ureidopropanoate) to, respectively, beta-aminoisobutyrate and beta-alanine, ammonia and carbon dioxide. Involved in the recycling of nitrogen from nucleobases to general nitrogen metabolism.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19413687}.
Interaction partners:
- Dihydropyrimidinase
- Dihydropyrimidine dehydrogenase
- Alanine--glyoxylate aminotransferase 2 homolog 3, mitochondrial
- Aldehyde dehydrogenase family 2 member B4, mitochondrial
- Aldehyde dehydrogenase family 7 member B4
- Pantoate--beta-alanine ligase
- Aldehyde dehydrogenase family 3 member H1
- Alanine--glyoxylate aminotransferase 2 homolog 1, mitochondrial
- Aldehyde dehydrogenase family 3 member I1, chloroplastic
- Aldehyde dehydrogenase family 3 member F1
Sequence:
MDHMISENGETSAEGSICGYDSLHQLLSANLKPELYQEVNRLLLGRNCGRSLEQIVLPESAKALSSKHDFDLQAASFSADKEQMRNPRVVRVGLIQNSIALPTTAPFSDQTRGIFDKLKPIIDAAGVAGVNILCLQEAWTMPFAFCTRERRWCEFAEPVDGESTKFLQELAKKYNMVIVSPILERDIDHGEVLWNTAVIIGNNGNIIGKHRKNHIPRVGDFNESTYYMEGDTGHPVFETVFGKIAVNICYGRHHPLNWLAFGLNGAEIVFNPSATVGELSEPMWPIEARNAAIANSYFVGSINRVGTEVFPNPFTSGDGKPQHNDFGHFYGSSHFSAPDASCTPSLSRYKDGLLISDMDLNLCRQYKDKWGFRMTARYEVYADLLAKYIKPDFKPQVVSDPLLHKNST
Protein: Endothelial PAS domain-containing protein 1 (EPAS-1) (Hypoxia-inducible factor 2-alpha) (HIF-2-alpha) (HIF2-alpha) (Q9JHS1)
Organism: Rattus norvegicus (Rat)
Function: Transcription factor involved in the induction of oxygen regulated genes. Heterodimerizes with ARNT; heterodimer binds to core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters (By similarity). Regulates the vascular endothelial growth factor (VEGF) expression and seems to be implicated in the development of blood vessels and the tubular system of lung. May also play a role in the formation of the endothelium that gives rise to the blood brain barrier. Potent activator of the Tie-2 tyrosine kinase expression. Activation requires recruitment of transcriptional coactivators such as CREBBP and probably EP300. Interaction with redox regulatory protein APEX seems to activate CTAD (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P97481, ECO:0000255|PROSITE-ProRule:PRU00981}. Nucleus speckle {ECO:0000250|UniProtKB:P97481}. Note=Colocalizes with HIF3A in the nucleus and speckles. {ECO:0000250|UniProtKB:P97481}.
Interaction partners:
- Aryl hydrocarbon receptor nuclear translocator
- von Hippel-Lindau disease tumor suppressor
- Aryl hydrocarbon receptor nuclear translocator 2
- Egl nine homolog 1
- Hypoxia-inducible factor 1-alpha
- Prolyl hydroxylase EGLN3
- Prolyl hydroxylase EGLN2
- Histone lysine acetyltransferase CREBBP
- Hypoxia-inducible factor 3-alpha
- Fe2OG dioxygenase domain-containing protein.
Sequence:
MTADKEKKRSSSELRKEKSRDAARCRRSKETEVFYELAHELPLPHSVSSHLDKASIMRLAISFLRTHKLLSSVCSENESEAEADQQMDNLYLKALEGFIAVVTQDGDMIFLSENISKFMGLTQVELTGHSIFDFTHPCDHEEIRENLTLKTGSGFGKKNKDRSTERDFFMRMKCTVTNRGRTVNLKSATWKVLHCTGQVRVYNNCPPHSSLCGYKEPLLSCLIIMCEPIQHPSHMDIPLDSKTFLSRHSMDMKFTYCDDRILELVGYHPEELLGRSAYEFYHALDSENMTKSHQNLCTKGQVVSGQYRMLAKHGGYVWLETQGTVVYNPRNLQPQCIMCVNYVLSEIEKNDVVVSMDQTESCSSHTLMAMNSIFDTSDDVALSEKSNYLFTNLKEEPEDLAQLAPTPGDAIISLDFGSQNFDESSTYGKAILPPGQPWATELRSHSAQSESRSLPAFTVPQAGSPGNATPSATSSSSCSTPSSPEDYYSSLENHLKIEVIEKLFAMDTEAKDQCSTQTDFNELDLETLAPYIPMDGEDFQLSPICPEEPLVPESPQPNPQHCFSTMSSIFQPLTPGASQGTFFLDKYPQQLESRKTESEHWPMSTIFFDAGSKGSLPPCCGQASTPLSSMGGRSNTPWPPDPPLHLGPTKWSVGNQSAEPLGPLPLGTSQLEPPSTPPHVSMFKMRSAKDFGARGPYMMSPAMIALSNKLKLKRQLDYEEPAFQDTSGGDPPGTSSSHLMWKRMKSLMGGTCPLMPDKTVSASMAPDEFTQKSMRGLGQPLRHLPPSQPPSTRSPGENAKSGFPPQCYASPFQDYSPPGAQKGSGVASRLLGPSFEPYLLPELTRYDCEVNVPEPGSSTLLQGRDLLRALDQAT
Protein: ATP-dependent RNA helicase DbpA (EC 3.6.4.13) (P21693)
Organism: Escherichia coli (strain K12)
Function: DEAD-box RNA helicase involved in the assembly of the 50S ribosomal subunit. Has an RNA-dependent ATPase activity, which is specific for 23S rRNA, and a 3' to 5' RNA helicase activity that uses the energy of ATP hydrolysis to destabilize and unwind short rRNA duplexes. Requires a single-stranded RNA loading site on the 3' side of the substrate helix.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- RNA polymerase sigma-54 factor
- ATP-dependent RNA helicase HrpA
Sequence:
MTAFSTLNVLPPAQLTNLNELGYLTMTPVQAAALPAILAGKDVRVQAKTGSGKTAAFGLGLLQQIDASLFQTQALVLCPTRELADQVAGELRRLARFLPNTKILTLCGGQPFGMQRDSLQHAPHIIVATPGRLLDHLQKGTVSLDALNTLVMDEADRMLDMGFSDAIDDVIRFAPASRQTLLFSATWPEAIAAISGRVQRDPLAIEIDSTDALPPIEQQFYETSSKGKIPLLQRLLSLHQPSSCVVFCNTKKDCQAVCDALNEVGQSALSLHGDLEQRDRDQTLVRFANGSARVLVATDVAARGLDIKSLELVVNFELAWDPEVHVHRIGRTARAGNSGLAISFCAPEEAQRANIISDMLQIKLNWQTPPANSSIATLEAEMATLCIDGGKKAKMRPGDVLGALTGDIGLDGADIGKIAVHPAHVYVAVRQAVAHKAWKQLQGGKIKGKTCRVRLLK
Protein: Protein GrpE (HSP-70 cofactor) (Q97S73)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Function: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01151}.
Interaction partners:
Sequence:
MAQDIKNEEVEEVQEEEVVKTAEETTPEKSELDLANERADEFENKYLRAHAEMQNIQRRANEERQNLQRYRSQDLAKAILPSLDNLERALAVEGLTDDVKKGLGMVQESLIHALKEEGIEEIAADGEFDHNYHMAIQTLPADDEHPVDTIAQVFQKGYKLHDRILRPAMVVVYN
Protein: Nitrate/nitrite transporter NrtP (B2IZT6)
Organism: Nostoc punctiforme (strain ATCC 29133 / PCC 73102)
Function: Transport system for both nitrate and nitrite, with much higher affinity for nitrate than for nitrite.
Subcellular location: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Molybdopterin oxidoreductase NarB
- Nitrite and sulphite reductase 4Fe-4S subunit NirA
- Precorrin-3B synthase
- Stress protein
Sequence:
MLKKLFSFSDRYRILHQTWFAFFLTFVCWFNFAPFATTIGKELHLAPEQIKTLGICNLALTIPARLIIGMLLDRFGPRITYSILLMFAVVPCLATALAQDFNQLVISRLLMGIVGSGFVVGIRMVAEWFQPKEMGIAQGIYGGWGNFGAFGAEFALPILAISTSFFSGGASNWRLAIALVGIITAIYGVIYYNTVQDTPRGKVYKKPKKNGSLEVTSIKSFWAMMISNFGLIFALGLLAWRLEQKKIHFLTLSQMYLTWLVLAGLFAYQSYKAWQVNRELLTGKKTYPVSERFQFGQVALLEFTYITNFGSELAAVSMLPAFFEKTFGLEHVVAGMIAATYPFLNLVSRPSGGLISDKFGSRKWTMTIISVGIGVSYLMAHFINSNWPIPVAIAVTMFAAYFAQAGCGATYSIVPMIKKEATGQIAGNVGAYGNFGGVVYLTIFSLTDAPTLFSTMGIAALICAFMCAFFLKEPKGSFAPAYEGEASETATKSSVFLTEE
Protein: Ras and Rab interactor 1 (Ras interaction/interference protein 1) (Q921Q7)
Organism: Mus musculus (Mouse)
Function: Ras effector protein, which may serve as an inhibitory modulator of neuronal plasticity in aversive memory formation. Can affect Ras signaling at different levels. First, by competing with RAF1 protein for binding to activated Ras. Second, by enhancing signaling from ABL1 and ABL2, which regulate cytoskeletal remodeling. Third, by activating RAB5A, possibly by functioning as a guanine nucleotide exchange factor (GEF) for RAB5A, by exchanging bound GDP for free GTP, and facilitating Ras-activated receptor endocytosis (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Some amount is membrane-associated. {ECO:0000250}.
Interaction partners:
- GTPase HRas
- GTPase KRas
- Tyrosine-protein kinase ABL1
- Ras-related protein Rab-5B
- GTPase NRas
- Ras-related protein R-Ras2
- Ras-related protein R-Ras
- Ras-related protein M-Ras
- Ras-related protein Rab-5A
- GTP-binding protein REM 1
Sequence:
MEDPGETGAHPLGATNLNFVPGHQQKEKPSTDPLYDTPDTRGVQAGGSQQPARTVSLRERLLITRPVWLQLRANAAAALHVLRTEPPGTFLVRKSNTRQCQALCVRLPEASGPSFVSSHYIEESTGGVSLEGSELMFQDLVQLICGYCRTRAIHQAATHKELEAISHLGMEFWSSSLNTKDQQRPSEAPPIPRLKARSPQELDQGTGAALCFFNPLFPGDLGPTKREKFKRSFKVRVSTETSSPLSPPAVPPPPVPVLPGTSSSQTERLPPRQLLQRESSVGYRVPGSAASPCLPPLPSLQEVDCCSPSSSEEEGSSGSPTTSPRLSRPRHRRPLLRSMSSAFCSLLAPERQVGRAATMLMQNRYTAVGQLVQDLLTQVRAGPEPRELQGIRQALSRARAMLSAELGPEKLLPPERLELVLEKSLHRSVLKPLRPILAARLRRRLSADGSLGRLAEGFRLARTQGPGAFGSHLTLSSPVETEQVRQKLLQLLRAYSPSAQVKWLLQACKLLYTALKSQAGENAGADEFLPLLSLVLAQCDLPDLLLEAEYMSELLEPTLLTGEGGYYLTSLSASLALLSGLSQARALPLSPAQELQRSLALWEQRRLPATHSFQHLLRVAYQDPSTGCTSKTLAVPPGSSIATLSQLCATKFRVTQPDAFGLFLYKDQGYHRLPPEALAHRLPATGYLIYRRAERPETQGAVAEKAKTGSKGPEAGAWEEETGGLNREGKPRIAVDQEGKDQARGGHIGPEEQKAEGSQALEE
Protein: Cytokine-inducible SH2-containing protein (CIS) (CIS-1) (Suppressor of cytokine signaling) (SOCS) (O70512)
Organism: Rattus norvegicus (Rat)
Function: SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. CIS is involved in the negative regulation of cytokines that signal through the JAK-STAT5 pathway such as erythropoietin, prolactin and interleukin 3 (IL3) receptor. Inhibits STAT5 trans-activation by suppressing its tyrosine phosphorylation (By similarity). May be a substrate recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity).
Interaction partners:
- Cullin-5
- Signal transducer and activator of transcription 1
- Signal transducer and activator of transcription 3
- Signal transducer and activator of transcription
- Signal transducer and activator of transcription
- Signal transducer and activator of transcription 5A
- Signal transducer and activator of transcription 5B
- Prolactin receptor
- Elongin-B
- Elongin-C
Sequence:
VLCVQGSCPLLVVEQIGQRPLWAQSLELPGPAMQPLPTGAFPEEVTEETPVQSENEPKVLDPEGDLLCIAKTFSYLRESGWYWGSITASEARQHLQKMPEGTFLVRDSTHPSYLFTLSVKTTRGPTNVRIEYADSSFRLDSNCLSRPRILAFPDVVSLVQHYVASCTADTRSDSPDPAPTPALPVSKPDAPGDPVLPIPVATAVHLKLVQPFVRRSSARSLQHLCRLVINRLVTDVDCLPLPRRMADYLRQYPFQL
Protein: Protein-ribulosamine 3-kinase, chloroplastic (EC 2.7.1.172) (Fructosamine 3-kinase-related protein) (AtFN3K-RP) (Q9LEW8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Initiates a process leading to the deglycation of proteins. Phosphorylates low-molecular-mass and protein-bound erythrulosamines and ribulosamines, but not fructosamines or psicosamines, on the third carbon of the sugar moiety. Protein-bound erythrulosamine 3-phosphates and ribulosamine 3-phosphates are unstable and decompose under physiological conditions.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
Sequence:
MAVASLSICFSARPHLLLRNFSPRPKFVAMAAMSEDPIREWILTEGKATQITKIGSVGGGCINLASHYQTDAGSFFVKTNRSIGPAMFEGEALGLEAMYETRTIRVPNPHKAGELPTGGSYIIMEFIDFGGSRGNQAELGRKLAEMHKAGKTSKGFGFEVDNTIGSTPQINTWSSDWIEFYGEKRLGYQLKLARDQYGDSAIYQKGHTLIQNMAPLFENVVIEPCLLHGDLWSGNIAYDKNNEPVILDPACYYGHNEADFGMSWCAGFGESFYNAYFKVMPKQAGYEKRRDLYLLYHYLNHYNLFGSGYRSSAMSIIDDYLRMLKA
Protein: Flavodoxin YqcA (P65367)
Organism: Escherichia coli (strain K12)
Function: Probable electron transporter.
Interaction partners:
- Uncharacterized protein YqcC
- tRNA pseudouridine synthase C
- Sulfite reductase hemoprotein beta-component
Sequence:
MAEIGIFVGTMYGNSLLVAEEAEAILTAQGHKATVFEDPELSDWLPYQDKYVLVVTSTTGQGDLPDSIVPLFQGIKDSLGFQPNLRYGVIALGDSSYVNFCNGGKQFDALLQEQSAQRVGEMLLIDASENPEPETESNPWVEQWGTLLS
Protein: Carbonyl reductase, isoform A (Carbonyl reductase, isoform B (EC 1.1.1.300)) (Carbonyl reductase, isoform C) (GH19857p) (Q7K0F7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLGTLLWIFFVGLLLCAFLFSKTTKEFPKSWFEWKTEFRYQYLGIVGLVHDAQYKARDRVALYKQPDRIAVITGGNRGIGLRIVEKLLACDMTVVMGVRDPKIAETAVASIVDLNATKGKLICEQLDVGDLKSVKAFAQLIKERYSKVDLLLNNAGIMFAPFKLTADGYESHFAINFLGHFLLTHLLLPQLRAAGKEGRNSRIVNVSSCVNLIGRINYKDINGTKHYYPGTAYSQSKLAQILFTRHLQTLLDAEKSHVQVNVVHPGIVDTDLFEHSATTSVPIFKKLFFKTPERGSRTVVFAAIDPSIEGQGGTYLSNGGKGPFHPDAKKPAKCEQLFQFSCDLLKIQQYGNGEY
Protein: DNA-directed RNA polymerase subunit Rpo5 (EC 2.7.7.6) (DNA-directed RNA polymerase subunit H) (P11521)
Organism: Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
Function: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00025}.
Interaction partners:
- DNA-directed RNA polymerase subunit Rpo11
- DNA-directed RNA polymerase subunit Rpo1N
- DNA-directed RNA polymerase subunit Rpo2
- DNA-directed RNA polymerase subunit Rpo7
- DNA-directed RNA polymerase subunit Rpo6
- DNA-directed RNA polymerase subunit Rpo1C
- DNA-directed RNA polymerase subunit Rpo3
- DNA-directed RNA polymerase subunit Rpo10
- DNA-directed RNA polymerase subunit Rpo12
- DNA-directed RNA polymerase subunit Rpo4
Sequence:
MRSSSKKKIDISNHELVPKHEILQLEEAYKLVKELGIKPEQLPWIRASDPVAKSIGAKPGDIIKITRKSPFTGESVTYRYVITG
Protein: Forkhead box protein L2 (Q53ZD3)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00089}.
Interaction partners:
Sequence:
MMASYPEPEDAAGALLAPETGRTVKEPEGPPPSPGKGGGGGGGTAPEKPDPAQKPPYSYVALIAMAIRESAEKRLTLSGIYQYIIAKFPFYEKNKKGWQNSIRHNLSLNECFIKVPREGGGERKGNYWTLDPACEDMFEKGNYRRRRRMKRPFRPPPAHFQPGKGLFGAGGAAGGCGVAGAGADGYGYLAPPKYLQSGFLNNSWPLPQPPSPMPYASCQMAAAAAAAAAAAAAAGPGSPGAAAVVKGLAGPAASYGPYTRVQSMALPPGVVNSYNGLGGPPAAPPPPPHPHPHPHAHHLHAAAAPPPAPPHHGAAAPPPGQLSPASPATAAPPAPAPTSAPGLQFACARQPELAMMHCSYWDHDSKTGALHSRLDL
Protein: SNW domain-containing protein 1 (D4A8G7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU367140}.
Interaction partners:
- Peptidyl-prolyl cis-trans isomerase
- Pre-mRNA-splicing factor SYF1
- Cell division cycle 5-like protein
- Pre-mRNA-splicing factor RBM22
- Pre-mRNA-processing-splicing factor 8
- Protein BUD31 homolog
- Pre-mRNA-splicing factor SYF2
- 116 kDa U5 small nuclear ribonucleoprotein component
- Cell division cycle 40.
- Pleiotropic regulator 1
Sequence:
MALTSFLPAPTQLSQDQLEAEERARSQRSRQTSLVSSRREPPPYGYRKGWIPRLLEDFGDGGAFPEIHVAQYPLDMGRKKKMSNALAIQVDPEGKIKYDAIARQGQSKDKVIYSKYTDLVPKEVMNADDPDLQRPDEEAIKEITEKTRVALEKSVSQKVAAAMPVRAADKLAPAQYIRYTPSQQGVAFNSGAKQRVIRMVEMQKDPMEPPRFKINKKIPRGPPSPPAPVMHSPSRKMTVKEQQEWKIPPCISNWKNAKGYTIPLDKRLAADGRGLQTVHINENFAKLAEALYIADRKAREAVEMRAQVERKMAQKEKEKHEEKLREMAQKARERRAGIKTHVEKEDGEARERDEIRHDRRKERQHDRNLSRAAPDKRSKLQRNENRDISEVIALGVPNPRTSNEVQYDQRLFNQSKGMDSGFAGGEDEIYNVYDQAWRGGKDMAQSIYRPSKNLDKDMYGDDLETRIKTNRFVPDKEFSGSDGRKRGREGPVQFEEDPFGLDKFLEEAKQHGGSKRPSDSSRPKEHEHEGKKRRKE
Protein: Pleckstrin homology domain-containing family G member 5 isoform X4 (Pleckstrin homology domain-containing, family G (with RhoGef domain) member 5a) (A0A2R8RLU7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MIFDRHPRFDLQPQGSILARNVSTRSCPPRTGPPSDMEDGEDGCSDLGDRRSGGMKLVKKKTRRRHTDDPSKECFTLKFDLNFEVSMEIVPAVKKKTLREVLGAVFERKGIELSRVNLFLDQSNTPLSLGFEAYRFGGHYLRVRARPGEDLRVERCVKDPRSLSLPIMRSSSNTHSSSTDRAEHGSLGRREAADLLVGLVGHAAYIQKNGGQTRRRKNMPEFLGDSSISNQDSLSQLSGSLPGSITGPDRWRNRAASRFSGLFSSNSGNGSLGKECDRVEQLQSKLYSYTMFGLPKMPPQLSFHRDSWEEEPNLELEESWKQLLENPEILTRRQCHQQEAIWELLQTESDYIKKLHVITDLFLCGLLNLQESGLLTEVEPTRLFSNIQDIVQLHSSLWTEVMLPALEKARQKRTMLNPTELHQGFSTFGFRFKPYIRYCMEEEGCMEYMRTLLKDNELFRIYVTWAETHKQCNRLKLTDMLVKPHQRLTKYPLLLKSVLKKTDDPPTREAINRMVAAVECFINSVDSQMRHREEKQKLAAIAGRIEAYEAVEGASEEVERILKEYNNFDLMAPVMGAPPEETRQLLLEGALKMKEGKESRMDVYCFLFTDVLLITKPVKRVEKVKVIRQPLVIHNVVCRELKDPGSFLLIYLNEFGCAVASYCFQANSGAQGRSWIEAIYNAQNQLQRLRSETQRDESDEKDEDETESSMSTSSSPSIHHRETLSKSLSLSPSHSDGSTETLSVAAMDEVDEVVGSTVQTASMRNSLLSDDSFSTSDSKTLQALGDLIVTDLDPESRSLSIDSAYGTLSPQSMITELDLKGGVCQSEGEETDAGEEEEAFEDDEDDDDDGDDSITWNGSQITVNESYILDTNSEELNRRNDFSGMAQVVAGCRSQTLRRRSPVQPRPDYLQHFTLRSRSEDDLLQCLTDPLLLRPTGKNNVSKSLTHLAKQKSHSDEVFQTDEDELLEDAKTLSSKLSNTLQRAEARQVQRTLSCPNGQADSEGSDAETAPPGGMEEKKDLVVVQQTHQQHKKLTVAQLHKIRATMVLNSTLTASEV
Protein: Secretoglobin family 2A member 2 (C3.1) (Prostatein peptide C3) (Prostatic steroid-binding protein C3) (P02780)
Organism: Rattus norvegicus (Rat)
Function: Part of prostatein which is the major secretory glycoprotein of ventral prostate gland. Steroid-binding protein; can bind non-polar steroids, cholesterol and a group of small proline-rich peptides.
Subcellular location: Secreted.
Interaction partners:
- Prostatic steroid-binding protein C1
Sequence:
MKLVFLFLLVTIPICCYASGSGCSILDEVIRGTINSTVTLHDYMKLVKPYVQDHFTEKAVKQFKQCFLDQTDKTLENVGVMMEAIFNSESCQQPS
Protein: Acyl-CoA Delta(11) desaturase (EC 1.14.19.5) (Acyl-CoA Delta-11 desaturase) (Delta(11)-desaturase) (SlsZ/E11) (Q6US81)
Organism: Spodoptera littoralis (Egyptian cotton leafworm)
Function: Catalyzes the formation of delta(11) fatty acyl precursors in the pheromone gland, and has high activity towards palmitic acid and stearic acid.
Subcellular location: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MAQCVQTTTILEQKEEKTVTLLVPQAGKRKFEIVYFNIITFAYWHIAGLYGLYLCFTSTKWATVLFSFFLFVVAEVGVTAGSHRLWSHKTYKAKLPLQILLMVMNSLAFQNTVIDWVRDHRLHHKYSDTDADPHNASRGFFYSHVGWLLVRKHPDVKKRGKEIDISDIYNNPVLRFQKKYAIPFIGAVCFVLPTLIPVYGWGETWTNAWHVAMLRYIMNLNVTFLVNSAAHIYGKRPYDKKILPSQNIAVSIATFGEGFHNYHHVFPWDYRAAELGNNSLNFPTKFIDFFAWIGWAYDLKTVSKEMIKQRSKRTGDGTNLWGLEDVDTPEDLKNTKGE
Protein: C-C motif chemokine (E9PTY9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU361150}.
Interaction partners:
- C-C motif chemokine 5
- C-C chemokine receptor type 10
- C-C motif chemokine ligand 26
- C-C motif chemokine receptor 4
- Chemokine
- C-C motif chemokine receptor 8
- C-C motif chemokine
- C-X-C motif chemokine ligand 17
- C-X-C motif chemokine 14
- C-C chemokine receptor type 5
Sequence:
MKTFAWTSGTMMSLQMLLLAALLLGTSLQHASAARATNVGRECCLDYFKGAIPIRKLVTWFRTSVECPRDAIVFETVQGRLICTDPKDKHVKKAIRHLKNQRL
Protein: Arylamine N-acetyltransferase (NAT) (EC 2.3.1.5) (TBNAT) (P9WJI5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the transfer of the acetyl group from acetyl coenzyme A to the free amino group of arylamines and hydrazines. Is able to utilize not only acetyl-CoA, but also n-propionyl-CoA and acetoacetyl-CoA as acyl donors, although at a lower rate. As acetyl-CoA and propionyl-CoA are products of cholesterol catabolism and the nat gene is likely present in the same operon than genes involved in cholesterol degradation, this enzyme could have a role in the utilization and regulation of these CoA species.
Interaction partners:
- Arylamine N-acetyltransferase
- Catalase-peroxidase
- 4,5:9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1
- Flavin-dependent monooxygenase, reductase subunit HsaB-triene-9,17-dione 4-hydroxylase, reductase subunit)
Sequence:
MALDLTAYFDRINYRGATDPTLDVLQDLVTVHSRTIPFENLDPLLGVPVDDLSPQALADKLVLRRRGGYCFEHNGLMGYVLAELGYRVRRFAARVVWKLAPDAPLPPQTHTLLGVTFPGSGGCYLVDVGFGGQTPTSPLRLETGAVQPTTHEPYRLEDRVDGFVLQAMVRDTWQTLYEFTTQTRPQIDLKVASWYASTHPASKFVTGLTAAVITDDARWNLSGRDLAVHRAGGTEKIRLADAAAVVDTLSERFGINVADIGERGALETRIDELLARQPGADAP
Protein: Probable protein phosphatase 2C 27 (AtPP2C27) (EC 3.1.3.16) (Probable protein phosphatase 2C G group 1) (AtPP2CG1) (P93006)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Confers salt tolerance by triggering the expression of stress-responsive genes.
Subcellular location: Nucleus {ECO:0000269|PubMed:22627139}. Cytoplasm {ECO:0000269|PubMed:22627139}.
Interaction partners:
Sequence:
MSMDFSPLLTVLEGDFNKDNTSSATEIDTLENLDDTRQISKGKPPRHLTSSATRLQLAANADVDVCNLVMKSLDDKSEFLPVYRSGSCAEQGAKQFMEDEHICIDDLVNHLGAAIQCSSLGAFYGVFDGHGGTDAAHFVRKNILRFIVEDSSFPLCVKKAIKSAFLKADYEFADDSSLDISSGTTALTAFIFGRRLIIANAGDCRAVLGRRGRAIELSKDHKPNCTAEKVRIEKLGGVVYDGYLNGQLSVARAIGDWHMKGPKGSACPLSPEPELQETDLSEDDEFLIMGCDGLWDVMSSQCAVTIARKELMIHNDPERCSRELVREALKRNTCDNLTVIVVCFSPDPPQRIEIRMQSRVRRSISAEGLNLLKGVLDGYP
Protein: Keratin, type II cytoskeletal 71 (Cytokeratin-6G) (CK-6G) (Cytokeratin-71) (CK-71) (Keratin-6G) (K6G) (Keratin-71) (K71) (Type II inner root sheath-specific keratin-K6irs1) (mK6irs) (mK6irs1/Krt2-6g) (Type-II keratin Kb34) (Q9R0H5)
Organism: Mus musculus (Mouse)
Function: Plays a central role in hair formation. Essential component of keratin intermediate filaments in the inner root sheath (IRS) of the hair follicle.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q3SY84}.
Interaction partners:
- Keratin, type I cytoskeletal 27
- Keratin, type I cuticular Ha5
- Keratin-associated protein 6-2
- Keratin-associated protein
- Keratin, type II cytoskeletal 72
- Keratin, type I cytoskeletal 25
Sequence:
MSRQFTCKSGASNRGFSGCSAVLSGGSSSSYRAGGKGLSGGFGSRSLYSLGGGRSITLNMASGSGKNGGFGFGRNRASGFAGSIFGSVALGPVCPAVCPPGGIHQVTVNESLLAPLNVELDPEIQKVRAQEREQIKALNNKFASFIDKVRFLEQQNQVLQTKWELLQQLDLNNCKNNLEPILEGHISNMRKQLETLSGDRVRLDSELRNVRDVVEDYKKKYEEEINRRTAAENEFVLLKKDVDAAYANKVELQAKVDTMDQDIKFFKCLFEAEMAQIQSHISDMSVILSMDNNRNLDLDSIIDEVRAQYEEIALKSKAEAEALYQTKFQELQLAAGRHGDDLKNTKNEITELTRFIQRLRSEIENAKKQASNLETAIADAEQRGDSALKDARAKLDELEGALHQAKEELARMLREYQELMSLKLALDMEIATYRKLLESEECRMSGEYSSPVSISIISSTSGSGGYGFRPSTVSGGYVANSTSCISGVCSVRGGENRSRGSASDYKDTLTKGSSLSTPSKKGGR
Protein: Prss3 protein (Q4G0C2)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
NALLILALVGAAVAFPVDDDDKIVGGYTCQENSVPYQVSLNSGYHFCGGSLINDQWVVSAAHCYKTRIQVRLGEHNINVLEGNEQFVNAAKIIKHPNFNRKTLNNDIMLLKLSSPVTLNARVATVALPSSCAPAGTQCLISGWGNTLSFGVSEPDLLQCLDAPLLPQADCEASYPGKITGNMVCAGFLEGGKDSCQGDSGGPVVCNRELQGIVSWGYGCALPDNPGVYTKVCNYVDWIQDTIAAN
Protein: Large ribosomal subunit protein uL15 (60S ribosomal protein L27a) (P46776)
Organism: Homo sapiens (Human)
Function: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23636399}.
Interaction partners:
- Small ribosomal subunit protein uS17
- Large ribosomal subunit protein eL37
- Large ribosomal subunit protein eL33
- Small ribosomal subunit protein eS27
- Large ribosomal subunit protein eL28
- Large ribosomal subunit protein eL31
- Large ribosomal subunit protein uL3
- Elongation factor 2
- Large ribosomal subunit protein eL20
- Small ribosomal subunit protein eS26
Sequence:
MPSRLRKTRKLRGHVSHGHGRIGKHRKHPGGRGNAGGLHHHRINFDKYHPGYFGKVGMKHYHLKRNQSFCPTVNLDKLWTLVSEQTRVNAAKNKTGAAPIIDVVRSGYYKVLGKGKLPKQPVIVKAKFFSRRAEEKIKSVGGACVLVA
Protein: Lytic conversion lipoprotein (Q38162)
Organism: Escherichia phage T5 (Enterobacteria phage T5)
Function: Inhibits of the adsorption of T5 to its FhuA receptor. By this means, T5 within cells excludes superinfection by T5 and other phages using FhuA receptor as a ligand.
Subcellular location: Host cell outer membrane {ECO:0000269|PubMed:8057856}; Lipid-anchor {ECO:0000305}. Note=Attached to the host membrane by a lipid anchor. {ECO:0000305}.
Interaction partners:
Sequence:
MKKLFLAMAVVLLSACSTFGPKDIKCEAYYMQDHVKYKANVFDRKGDMFLVSPIMAYGSFWAPVSYFTEGNTCEGVF
Protein: RH71479p (Q86P75)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKHFLIVAFALGRWHTMRFLRRYVRKLFVFKGFTGILGMKASTKLCFILLAAITLCYFSDLGFLSIFHRVYQPTGRATAIATAMRFLSGGWNLGAVPLSAFRSLALQCSRSSLRLVSAARRRGSAGCRYAGGGPPL
Protein: Uncharacterized mitochondrial carrier PB17E12.12c (Q8TFH2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Probable thymidylate synthase
- Large ribosomal subunit protein eL18A
- Large ribosomal subunit protein eL18B
Sequence:
MQKDKFGPCAPSRIPLLSNDLISMLSGGVAATVSRTAVSPLERMKIIFQVQNNKEYTSLTSTLVKIWNREGLIGFFRGNGTNCLRAFPYGAVQFATFNMLKQRALKNRSHQNLENHERLLFGAIAGAASCATTYPLDIARTRLSIETAGLTSRSLAINNVANNSLKVKPLTLWSTLLYIVQHEGGYPALYNGLPATLLNVVPYVSICFFTFEFCKQKFFSNADLTAFQKLFLGGFTGIIGQTLTFPADVLRRRFQVNRIPGIGHNYKNIKSAIFHIYKTEGINGFFRGYSSNMLKIIPVMSITWYTYETVSKMLHDL