wanglab/gogpt-training-data huggingface dataset:
Protein: Venom prothrombin activator hopsarin-D (vPA) (EC 3.4.21.6) (Venom coagulation factor Xa-like protease) [Cleaved into: Hopsarin-D light chain; Hopsarin-D heavy chain] (P83370)
Organism: Hoplocephalus stephensii (Stephens' banded snake)
Function: Snake prothrombin activator that attacks the hemostatic system of prey. This protein is functionally similar to blood coagulation factor Xa. The procoagulant activity of hopsarin-D is approximately 10-fold lower than that of trocarin-D and FXa.
Subcellular location: Secreted {ECO:0000269|PubMed:12403650}.
Interaction partners:
Sequence:
MAPQLLLCLILTFLWSVPEAESNVFLKSKVANRFLQRTKRSNSLFEEIRPGNIERECIEEKCSKEEAREVFEDNEKTETFWNVYVDGDQCSSNPCHYHGTCKDGIGSYTCTCLPNYEGKNCEKVLFKSCRAFNGNCWHFCKRVQSETQCSCAESYRLGVDGHSCVAEGDFSCGRNIKARNKREASLPDFVQSQKATLLKKSDNPSPDIRIVNGMDSKLGECPWQAVLINEKGEVFCGGTILSPIHVLTAAHCINQTKSVSVIVGEIDISRKETRRLLSVDKIYVHTKFVPPNYYYGHQNFDRVAYDYDIAIIRMKTPIQFSENVVPACLPTADFANEVLMKQDSGIVSGFGRIRFKEPTSNTLKVITVPYVDRHTCMLSSDFRITQNMFCAGYDTLPQDACEGDSGGPHITAYGDTHFITGIVSWGEGCARKGKYGVYTKVSRFIPWIKKIMSLK
Protein: PAN2-PAN3 deadenylation complex subunit PAN3 (PAB1P-dependent poly(A)-specific ribonuclease) (Poly(A)-nuclease deadenylation complex subunit 3) (PAN deadenylation complex subunit 3) (P36102)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Regulatory subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein PAB1. PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA decaping by DCP1-DCP2 and subsequent 5'-3' exonucleolytic degradation by XRN1. May also be involved in post-transcriptional maturation of mRNA poly(A) tails, trimming the tails from their synthesized length to the slightly shorter, apparently messenger-specific length found on newly exported mRNAs. PAN3 acts as a positive regulator for PAN activity, recruiting the catalytic subunit PAN2 to mRNA via its interaction with RNA and with PAB1. PAN cooperates with protein kinase DUN1 in the regulation of RAD5 mRNA levels and cell survival in response to replicational stress.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03181, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15894541}.
Interaction partners:
- PAN2-PAN3 deadenylation complex catalytic subunit PAN2
- Polyadenylate-binding protein, cytoplasmic and nuclear
- CCR4-Not complex 3'-5'-exoribonuclease subunit Ccr4
- Poly
- RNA exonuclease 3
- 5'-3' exoribonuclease 1
- Tubulin alpha-3 chain
- Tethering factor for nuclear proteasome STS1
- RNA exonuclease 4
- RNA exonuclease 1
Sequence:
MDKINPDWAKDIPCRNITIYGYCKKEKEGCPFKHSDNTTATTINDVPPPIDVGEATTPTMTSVPKFNAKVSASFTPMTVGSDSLTTVTNTTSAATNATGNIAMAATSATASTVNPMINPIVNSSLVNNNNNNSNISISIPTTASSSNYDPFNAPIFTPSSTSSIHTNANAHSFPFPSIANSGGININATDDNSNNMSMANNVPPPMQPPPIESSNLKYPRIYPPPHSLLQYHLYAPEQPSSLKSLLKPNERSADQLFIPNNIREDLTKKNLSILQVFPSSGKVIPSIVQDYFNLVPLNFNNNDFLNKTTLFKVFSNYDGKAYVLKRLPNIDKSMNPNKISKIYQIWSKINCTNLIKFRDIFQTTKFGDLSICLVFDYYPNSLSLYDYHFVNFPKFPITNNYLWIYLVQLTNVINSIHSQNLSIGNTLNWRKVLITGDPGRIKLSHCNFMDLLFNDDTDTVVSSGGSTIEGQQQLDYKYLGELLFNLSINIENSNNNTAPKEYRLEEITPQSIDDMRQIDDKFKDVLKYLISDNGDSKKSIHDLTSHFYDKMFMVLESSQTYTEYMESVLSRELENGRLFRLVNKLNCIFGRIESRIDINWSESGTKFPIILFYDYVFHQVDSNGKPIMDLTHVLRCLNKLDAGIQEKLMLVTPDELNCIIISYKELKDLIESTFRSITQ
Protein: 75 kDa invariant surface glycoprotein (Invariant surface glycoprotein, putative) (Q57VX7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Cyclin 3
Sequence:
MSTMPVTLRTTATVFLLCGICALDVTWAEELSVAQKQYVTAGARQLDGQGATTLCEMKKMLDGVNSRVDMFEQQAYMYVNNANANFRKISDDKGMELSFPSNKLREIQYMKSLGNGIIKYMGGTGERAKAAAANASAALDQVLTWHCVDRTASHDVLPGYGRNENCLPNAYKRDYYYEHSRLDPHKYSILCNYKVVDSVITQTTFSNMERALEIWNQVKPKPYSARVMICGAGAPAHQAAPAGRPCTVLENWLWNYRVTAHLISKVEKDATLALRVFHYSKKVLEGYKESLAQHEERRKAAEARAAEEEAKRQAAEKAAEEARKALEEAEARRVAAEEQAEARRLEAEKAEKAKEAGQPVSEEKKKMLLEAVEEAEATEKAAEKQAKDSRKAFEEAEEERVKATEDAEAAKEEKKDAEESEEKLKKDVEKLAEELKEESKESGEGDDVNADHDDEGSEAKSGWIGTTKVLIFLIPLLLLLLGLLVFFVIRGRRKAEVKDDINIGEANAKSKNTKTAAGLDSDI
Protein: 7alpha-hydroxysteroid dehydrogenase (7alpha-HSDH) (EC 1.1.1.159) (NAD-dependent 7alpha-hydroxysteroid dehydrogenase) (P0AET8)
Organism: Escherichia coli (strain K12)
Function: 7alpha-hydroxysteroid dehydrogenase involved in the metabolism of bile acids. Catalyzes the NAD(+)-dependent oxidation of the 7alpha-hydroxy group of 7alpha-hydroxysteroids, such as the major human bile acids cholate and chenodeoxycholate, to the corresponding 7-oxosteroids. To a lesser extent, can also act on taurochenodeoxycholate, taurocholate and glycocholate. Can also use glycochenodeoxycholate as substrate. Is not able to use NADP(+) instead of NAD(+) as the electron acceptor.
Interaction partners:
- Maltose regulon regulatory protein MalI
- NADH-quinone oxidoreductase subunit C/D
Sequence:
MFNSDNLRLDGKCAIITGAGAGIGKEIAITFATAGASVVVSDINADAANHVVDEIQQLGGQAFACRCDITSEQELSALADFAISKLGKVDILVNNAGGGGPKPFDMPMADFRRAYELNVFSFFHLSQLVAPEMEKNGGGVILTITSMAAENKNINMTSYASSKAAASHLVRNMAFDLGEKNIRVNGIAPGAILTDALKSVITPEIEQKMLQHTPIRRLGQPQDIANAALFLCSPAASWVSGQILTVSGGGVQELN
Protein: Protein kinase, putative (Q38BR3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- DNA repair protein RAD51 homolog
- BRCT domain-containing protein
- Protein kinase, putative
- Cell division cycle 45
- non-specific serine/threonine protein kinase
- Phosphatidylinositol 3-kinase catalytic subunit, putative
- DNA replication licensing factor MCM4
- Protein MCM10 homolog
- Exonuclease, putative
- DNA replication licensing factor MCM3
Sequence:
MSSQDSESWGNSRQHYQYSDASEEHRPEATKLKSECFQNAGRTSPNRRRDSPAIQQESSDFATTSDSPVPCHYSQRGPASQNAQQKGKDRGDVFCSTVTSSDLFPTVELGPRMLPTNSTSMKGGRYAAGDRLPQTQETDKTDKPVRNRSERSEGTPLPNCGTALRDGSRHSHSPASSCRGNDSLVTNGTASQRETNEESCDVCGSCSTHYVSVSLGLSEWETLSPNQIKLRQCFDAPIDSIAVPSSETHRSLAHEQQRQLLETIMQKHSRKRIKRVTDYILGPICGEGTLSTVRDAINISSNNVDPFRFQRVAIKCYKQSDSKLSEGAGSSDCSQLSSLASATRRQQDELQRLREAEKRNLQCFYSTNIVRSIDVFSHEGKQYIVLPAAICNLEQLVQLAKCQNRCASCDSVRGKRNMIPSSKDGVDGRFELMPSLGKPAGKLPQNDVSLCTGAASLQKMSPYRKVTSLFAAEVVRSIMNQLLRGVAYLHRQGVAHNDLKPQNILLFADGLVKIGDLASVSVNYTGHGTPMYLSPEICRYFYDAGNETNGRVAVVDALKNDMWGCGAILYYLLTGNTLWEDGANCQNVYQLYRIIAERNTPVSLSHINIPAETEDELISRLTESENISFRATGGLRRPTAFPHTSLLHLAAGLLDVNPATRLTAEEAVRHPSLQAPPVDDVHDAFPTDMTQGDVMKVMLESPYYQQLIKWDRERHLQFAAECSHVLGLQIPEEICVSAQKRAADGCGMEADVTDPLLRLPSSIYRLVGTVNPSLFLPTDEFHHYLRKLKVPNYDVSSLRANPSAVKMMEDYLHTVMMECGYTGSVNTRERSGSKEDQNGIKLSTSQLTTRSREDTSHGLATFKDDDQPETLDRVLTDMPSDGRPNFCCIIM
Protein: Xaa-Pro dipeptidase (X-Pro dipeptidase) (EC 3.4.13.9) (Imidodipeptidase) (Peptidase 4) (Peptidase D) (Proline dipeptidase) (Prolidase) (Q11136)
Organism: Mus musculus (Mouse)
Function: Splits dipeptides with a prolyl or hydroxyprolyl residue in the C-terminal position. Plays an important role in collagen metabolism because of the high level of iminoacids in collagen.
Interaction partners:
- Cytosolic non-specific dipeptidase
Sequence:
MASTVRPSFSLGNETLKVPLALFALNRQRLCERLRKNGAVQAASAVVLQGGEEMQRYCTDTSIIFRQESFFHWAFGVVESGCYGVIDVDTGKSTLFVPRLPDSYATWMGKIHSKEYFKEKYAVDDVQYTDEIASVLTSRNPSVLLTLRGVNTDSGSVCREASFEGISKFNVNNTILHPEIVECRVFKTDMELEVLRYTNRISSEAHREVMKAVKVGMKEYEMESLFQHYCYSRGGMRHTSYTCICCSGENAAVLHYGHAGAPNDRTIKDGDICLFDMGGEYYCFASDITCSFPANGKFTEDQKAIYEAVLRSCRTVMSTMKPGVWWPDMHRLADRIHLEELARIGLLSGSVDAMLQVHLGAVFMPHGLGHFLGLDVHDVGGYPEGVERIDEPGLRSLRTARHLEPGMVLTVEPGIYFIDHLLDQALADPAQACFFNQEVLQRFRNFGGVRIEEDVVVTDSGMELLTCVPRTVEEIEACMAGCDKASVPFSGQK
Protein: NAP1-related protein 1 (Nucleosome/chromatin assembly factor group A6) (Protein SET homolog 1) (Q9CA59)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as histone H2A/H2B chaperone in nucleosome assembly, playing a critical role for the correct expression of genes involved in root proliferation and patterning. Required with NRP2 for the maintenance of cell proliferation and differentiation in postembryonic root growth. Involved in both intramolecular and intermolecular somatic homologous recombination.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17122067}. Nucleus {ECO:0000269|PubMed:17122067}.
Interaction partners:
- Histone H4
- Histone H2A.6
- Histone H2B.1
- Acidic leucine-rich nuclear phosphoprotein 32-related protein
- Histone chaperone ASF1B
- Probable histone chaperone ASF1A
- Probable histone H2A variant 3
- Uncharacterized protein
- Probable histone H2A variant 2
- Histone H2A variant 1
Sequence:
MVADKSKKSKIEEKGEEENLEQIDAELVLSIEKLQEIQDDLEKINEKASDEVLEVEQKYNVIRKPVYDKRNEVIQSIPGFWMTAFLSHPALGDLLTEEDQKIFKYLNSLEVEDAKDVKSGYSITFHFTSNPFFEDAKLTKTFTFLEEGTTKITATPIKWKEGKGLPNGVNHDDKKGNKRALPEESFFTWFTDAQHKEDAGDEIHDEVADIIKEDLWSNPLTYFNNDADEEDFDGDDDGDEEGEEDDDDEEEEDGEE
Protein: Transcriptional activator HlyU (A0A3Q0L222)
Organism: Vibrio vulnificus (strain CMCP6)
Interaction partners:
Sequence:
MNLKDMEQNSAKAVVLLKAMANERRLQILCMLHNQELSVGELCAKLQLSQSALSQHLAWLRRDGLVTTRKEAQTVYYTLKSEEVKAMIKLLHSLYCEE
Protein: Sarcosine oxidase alpha subunit (Q9HTE6)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Sarcosine oxidase gamma subunit
- Sarcosine oxidase subunit beta subunit beta)
- Sarcosine oxidase delta subunit
- Glycine dehydrogenase
- Glycine dehydrogenase
- Serine hydroxymethyltransferase 1
- Glycine betaine monooxygenase reductase subunit
- Serine hydroxymethyltransferase 2
- Serine hydroxymethyltransferase 3
- Electron transfer flavoprotein alpha/beta-subunit N-terminal domain-containing protein
Sequence:
MSQINRLSSGGRIDRNRPLTFSFNGQHYQGYAGDTLAAALLANGVDIVGRSFKYSRARGIVAAGAEEPNAILQIGSREATQIPNVRATQQALYGGLVATSTNGWPNVQNDLMGIFGKVGGKLMPPGFYYKTFMYPQSMWMTYEKYIRKAAGLGRAPTEVDPDSYDWMNHHCDVLVVGAGPAGLAAALAAARSGARVILADEQEEFGGSLLDTRETLDGKPAAEWVADAVAELQGLPEVILLPRSTVNGYHDHNFLTIHERRTDHLGEVAPLGQVRQRVHRVRAKRVVLAAGAHERPLVYGNNDLPGNMLAGAVSTYVRRYGVAPGKKLVLATNNDYAYRVALDWQEAGLQVVAIADARANPRGEWVEEARQRGMRVITGSSVIEARGGKRVSGAKVARIDLQAMRASGGEWLDCDLIASSGGYSPVVHLASHLGGKPEWREEILAFVPGEGLQKRICAGAVNGVFGLAEVLADGYQAGSRAALDAGYKTAAGSLPKVQPRREEASVALFQVPHEKPTARAPKQFVDPQNDVTAAAIELACREGFESIEHVKRYTALGFGTDQGKLGNINGLAIAARAQGKSIADTGTTMFRPNYTPVTFGAVAGRHCGHLFEPVRFTALHAWHVKNGAEFEDVGQWKRPWYFPRRGEDMHAAVARECRAVREAVGLLDASTLGKIDIQGPDAREFLNRVYTNAWTKLDVGKARYGLMCKEDGMVFDDGVTACLADNHFVMTTTTGGAARVLEWLELYHQTEWPELKVYFTSVTDHYATLTLSGPNSRKLLAEVTDIDLDKDAFPFMTWKEGKVAGVPARVFRISFTGELSYEVNVQADYAMGVLEALAEHGAKYGLTPYGTETMHVLRAEKGFIIVGQDTDASVTPDDLNMGWAVGRSKPFSWIGWRGMNRADCLREDRKQLVGLRPSNPQEVLPEGAQLVFDTQQAIPMKMVGHVTSSYMSASLGHGFALAVVKGGLKRMGQKVYAPLADGRFIEAEICSSVFYDPKGERQNVD
Protein: Elongator complex protein 3 (EC 2.3.1.311) (tRNA uridine(34) acetyltransferase) (Q9CZX0)
Organism: Mus musculus (Mouse)
Function: Catalytic tRNA acetyltransferase subunit of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) (By similarity). In the elongator complex, acts as a tRNA uridine(34) acetyltransferase by mediating formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (By similarity). May also act as a protein lysine acetyltransferase by mediating acetylation of target proteins; such activity is however unclear in vivo and recent evidences suggest that ELP3 primarily acts as a tRNA acetyltransferase (By similarity). Involved in neurogenesis: regulates the migration and branching of projection neurons in the developing cerebral cortex, through a process depending on alpha-tubulin acetylation. Required for acetylation of GJA1 in the developing cerebral cortex.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19185337}. Nucleus {ECO:0000250|UniProtKB:Q9H9T3}.
Interaction partners:
- Elongator complex protein 1
- Elongator complex protein 4
- Elongator complex protein 5
- Elongator complex protein 2
- Elongator complex protein 6
- Cytoplasmic tRNA 2-thiolation protein 1
- Diphthamide biosynthesis protein 3
- Protein KTI12 homolog
- WD repeat-containing protein 43
- Histone acetyltransferase KAT2A
Sequence:
MRQKRKGDLSPAELMMLTIGDVIKQLVEAHEQGKDVDLNKMKTKTAAKYGLASQPRLVDIIAAVPPHYRKILIPKLKAKPVRTASGIAVVAVMCKPHRCPHISFTGNICIYCPGGPDSDFEYSTQSYTGYEPTSMRAIRARYDPFLQTRHRIEQLKQLGHSVDKVEFIVMGGTFMALPEEYRDYFIRSLHDALSGHTSNNIHEAIKYSERSFTKCVGITIETRPDYCMKRHLSDMLTYGCTRLEIGVQSVYEDVARDTNRGHTVKAACESFHLAKDSGFKVVTHMMPDLPNVGLERDIEQFIEFFENPAFRPDGLKLYPTLVIRGTGLYELWKSGRYRSYSPSDLIELVARILALVPPWTRVYRVQRDIPMPLVSSGVEHGNLRELAFARMKDLGIQCRDVRTREVGIQEIHHRVRPYQVELVRRDYVANGGWETFLSYEDPDQDILIGLLRLRKCSEETFRFELGGGVSIVRELHVYGSVVPVSSRDPTKFQHQGFGMLLMEEAERIAREEHGSGKMAVISGVGTRNYYRKIGYRLQGPYMVKMLK
Protein: Pro-glucagon [Cleaved into: Glicentin; Glicentin-related polypeptide (GRPP); Oxyntomodulin (OXM) (OXY); Glucagon; Glucagon-like peptide 1 (GLP-1) (Incretin hormone); Glucagon-like peptide 1(7-37) (GLP-1(7-37)); Glucagon-like peptide 1(7-36) (GLP-1(7-36)); Glucagon-like peptide 2 (GLP-2)] (P01275)
Organism: Homo sapiens (Human)
Function: Plays a key role in glucose metabolism and homeostasis. Regulates blood glucose by increasing gluconeogenesis and decreasing glycolysis. A counterregulatory hormone of insulin, raises plasma glucose levels in response to insulin-induced hypoglycemia. Plays an important role in initiating and maintaining hyperglycemic conditions in diabetes.
Subcellular location: Secreted {ECO:0000305}.; SUBCELLULAR LOCATION: [Glucagon-like peptide 1]: Secreted {ECO:0000269|PubMed:22037645}.
Interaction partners:
- Gastric inhibitory polypeptide receptor
- Glucagon-like peptide 1 receptor
- Glucagon receptor
- Insulin
- Glucagon-like peptide 2 receptor
- Dipeptidyl peptidase 4
- Somatostatin
- Gastric inhibitory polypeptide
- Secretin
- Glucose-dependent insulinotropic receptor
Sequence:
MKSIYFVAGLFVMLVQGSWQRSLQDTEEKSRSFSASQADPLSDPDQMNEDKRHSQGTFTSDYSKYLDSRRAQDFVQWLMNTKRNRNNIAKRHDEFERHAEGTFTSDVSSYLEGQAAKEFIAWLVKGRGRRDFPEEVAIVEELGRRHADGSFSDEMNTILDNLAARDFINWLIQTKITDRK
Protein: T3SS secretion switching protein SepL (Type III secretion system protein SepL) (Q7DB79)
Organism: Escherichia coli O157:H7
Interaction partners:
- EspA
- T3SS secretion switching protein SepD
- EspA
- Translocated intimin receptor Tir
- T3SS structure protein EscD
- T3SS structure protein EscD
- EspD
- EspD
- T3SS structure protein EscV
- Type 3 secretion system secretin
Sequence:
MANGIEFNQNPASVFNSNSLDFELESQQLTQKNSSNISSPLINLQNELAMITSSSLSETIEGLSLGYRKGSARKEEEGSTIEKLLNDMQELLTLTDSDKIKELSLKNSGLLEQHDPTLAMFGNMPKGEIVALISSLLQSKFVKIELKKKYARLLLDLLGEDDWELALLSWLGVGELNQEGIQKIKKLYEKAKDEDSENGASLLDWFMEIKDLPEREKHLKVIIRALSFDLSYMSSFEDKVKTSSIISDLCRVIIFLSLDNYADIISISIKKDKDIILNEVLSIIEHVWLTEDWLLESPSRVSIVEDKHIYYFHLLKDFFTSLPDACFIDSEQRENALLMIGKVIDYKEEII
Protein: D-alanyl-D-alanine dipeptidase (D-Ala-D-Ala dipeptidase) (EC 3.4.13.22) (O53850)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Secreted protein
- Methyltransferase domain-containing protein
Sequence:
MRLIGRLRLLMVGLVVICGACACDRVSAGRWSESPSATSWPVRPVNTTTPSGPVPPVSEAARAAGLVDVRGVVPDAAIDLRYATANNFTGTQLYPPGARCLVHESMAEGLAAAAAVLRPHGQVLVFWDCYRPHDVQVRMFDVVPNPAWVARPGKYAHSHEAGRSVDVTFASAQRQCPSVRRSGELCLADMGTDFDDFSSRATAFATQGVSAEAQANRAHLRAAMQAGGLTVYSGEWWHFDGPGAGVDRPILEVPVD
Protein: Large ribosomal subunit protein uL4m (54S ribosomal protein YmL6, mitochondrial) (P51998)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}. Note=Mitoribosomes are tethered to the mitochondrial inner membrane and spatially aligned with the membrane insertion machinery through two distinct membrane contact sites, formed by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein MBA1. {ECO:0000269|PubMed:25609543}.
Interaction partners:
- Large ribosomal subunit protein uL22m
- Large ribosomal subunit protein uL3m
- Large ribosomal subunit protein uL16m
- Large ribosomal subunit protein bL17m
- Large ribosomal subunit protein bL19m
- Large ribosomal subunit protein uL13m
- Large ribosomal subunit protein bL28m
- Large ribosomal subunit protein uL15m
- Small ribosomal subunit protein uS9m
- Large ribosomal subunit protein uL23m
Sequence:
MTIKRNLVKTLQSIRYQATTATAHAESTLNPLPNAAIPPKYALVTVRSFPSLEPLTFVPVPTSTVAAPLRRDILWRAVVYENDNRRVGASNPPGRSENGFSRRKLMPQKGSGRARVGDANSPTRHNGGRALARTAPNDYTTELPSKVYSMAFNNALSHQYKSGKLFVIGGEKVDLISPTPELDLNRLDLVNTNTVEGKEIFEGEVIFRKFLEEFQLKGKRLLFITDKTREGLIKSSDPYKQKVDVIQKELVEVNDILRAQAVFIELEALEYLAMAHQKEILHSVSN
Protein: Major strawberry allergen Fra a 1-E (Class 10 plant pathogenesis-related protein Fra a 1.01) (PR10-related protein Fra a 1.01) (Fra a 1.01E) (allergen Fra a 1) (Q256S2)
Organism: Fragaria ananassa (Strawberry) (Fragaria chiloensis x Fragaria virginiana)
Function: Involved in the control of flavonoid biosynthesis in fruits, probably by binding directly to natural flavonoids. Binds the natural flavonoid quercetin-3-O-glucuronide with affinities in the low micromolar range.
Interaction partners:
Sequence:
MGVYTYENEFTSDIPAPKLFKAFVLDADNLIPKIAPQAVKCAEILEGDGGPGTIKKITFGEGSHYGYVKHKIHSIDKVNHTYSYSLIEGDALSENIEKIDYETKLVSAPHGGTIIKTTSKYHTKGDVEIKEEHVKAGKEKAAHLFKLIEGYLKDHPSEYN
Protein: Transcriptional regulator (DNA-binding protein) (A4FBF9)
Organism: Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL 2338)
Interaction partners:
- Aerial mycelium formation
- Sporulation and cell division regulator protein
- Sporulation-specific cell division protein SsgB
Sequence:
MGDYAKALGGKLRAIRQQQGLSLHGVEQKSGGRWKAVVVGSYERGDRAVTVQKLAELADFYGVPVAELLPEGRVPSGAEPATKVVINLERLQQLPAEKVGPLARYAATIQSQRGDYNGKVLSIRTEDLRSLAIIYDMTPGELTEQLIDWGVLPPEARPAREE
Protein: Purotoxin-1 (PT1) (OMICRON-lycotoxin-Am1a) (OMICRON-LCTX-Am1a) (P86269)
Organism: Alopecosa marikovskyi (Wolf spider) (Lycosa kazakhstanicus)
Function: Inhibits P2RX3 receptors. Has an analgesic effect in rat. Enhances the high-affinity desensitization of P2RX3 purinoceptors. At 50 nM, decreases the IC(50) for ambient ATP from 46.5 nM to 12.7 nM in mouse P2RX3.
Subcellular location: Secreted {ECO:0000269|PubMed:20437566}.
Interaction partners:
Sequence:
GYCAEKGIRCDDIHCCTGLKCKCNASGYNCVCRKK
Protein: F-box/kelch-repeat protein SKIP25 (SKP1-interacting partner 25) (Q8GX29)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Protein SMAX1-LIKE 2
- Probable esterase KAI2
- Protein SUPPRESSOR OF MAX2 1
- B-box zinc finger protein 20
- RNI-like superfamily protein
- 2-oxoglutarate
- F-box protein MAX2
- Alpha/beta-Hydrolases superfamily protein
- F-box protein At4g02760
- F-box/kelch-repeat protein At5g42350
Sequence:
MEKKLKRRESMSTTAAESPPAKRRRTVTGNENSALIEGLPDHISEICLSLVHRPSLLSAVCTRWRRLLYSPEFPSFPSLYALFVDSTSDTGRVNPSVRFMCFNPVSSKWYPLPPPPPDPPLHRILYRHPSFISFNLPIQCVSAAGKLILIAGSNQQLSPAISHPLIFDPISSSWSSGPRIGSPRRWCATGACDGAIYIASGISSQFSSTVAKSVEKLDLTEQNRNNHRFNWEKLRDMRDLRFSREAIDAVGYRRKLLMVNVKGDAVKEGAIYDVVKDDWEPMPEEMLVGWRGPVAAMEEEILYSVDERRGTVRKYDDEKREWREVVVVEGGEEMLKGATQVTADSGKLCVVTGDGKIVVVDVAAEPAKIWNVEIPDGLEPVSVHVLPRMSQPNFC
Protein: Inosine-5'-monophosphate dehydrogenase (IMP dehydrogenase) (IMPD) (IMPDH) (EC 1.1.1.205) (Mycophenolic acid biosynthesis cluster protein F) (F1DBB2)
Organism: Penicillium brevicompactum
Function: Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth (By similarity). Part of the gene cluster that mediates the biosynthesis of mycophenolic acid (MPA), the first isolated antibiotic natural product in the world. Does not play a role in the biosynthesis of MPA, but is involved in self resistance to MPA, since MPA acts as an inhibitor of IMP dehydrogenases.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03156}.
Interaction partners:
Sequence:
MVEILDYTKALEVLKEYPSGDGLHVDTLLDSDNHGALTYNDFLILPGSITFSAADVSLDTKVTRRFTIKAPLLSSPMDTVTEHNMAIHMALLGGLGVIHNNCPPDDQAEMVRKVKRYENGFILDPVVLSPSTTVAEAKELKTKWNFGGFPVTEKGTLHSKLLGIVTSRDIQFHKTPEDPVTAVMSTDLVTAPAGTTLAEANEVLRSSKKGKLPIVDKDGLLVSLLSRSDLMKNIHYPLASKLPSKQLLCAAAISTHDADKVRLQKLVDAGLDIVVVDSSQGNSMYQIAMIKWIKSTFPDIDIIAGNIVTREQAAALIAAGADGLRIGMGSGSACITQEVMAVGRPQAASVRSVSAFAARFGVPTIADGGVQNLGHIVKGLALGASAVMMGSLLAGTTESPGEYYVSNEGQLVKAFRGMGSIAVMEDKGKSGGGKNAGASRYFSENDKVKVAQGVAGSVVDRGSITQYVPYLVAGIQHSLQDIGVQDLEALHTGVNNGQVRFEMRSASAQTEGNVHGLHSHEKKLYSS
Protein: Secretory 16, isoform H (X2JJP5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}.
Interaction partners:
Sequence:
MLHNNAPWLPPHQQQQQQAPQQHPTPQQQHAMPQQQQTLPAQQQQQQVYASQMFQQHQPNYWPEDQHQQQQQPQSLNYNNYFPGQQQQHPMQQQQLPPQQQLPPQQQQPTQQQHTIQQQLYYPTQQQPQVPAPAEPALDSFDNNNSGGGGGGGRSDGWGDWGDWNDNSNNNNSNGTDGLLEPTGQLLEDSFNVQSSQGSWQAFATSNNVNNNGELPPPANPQSTSLQQQPLNQQSIPLLHQQPQSPPELGQEPELDAIVPPQAFQNQPPTAAPPPTSLTSFSAQMTAVGSPIYAVGASSAHSAGVGASPAPPTGVVAPPAHLAGIGAPPAHLAGVGASPAPSALVGASPAPIIGVGAPPVGAPPVGAPPADATTIAPPAALPPSIVPSSGSNPFKRSTGLNKRVNIMADPAAGAPSPPAPAAAIAPVAPVAPIPPPADQLFGMPAEAHGEGFNLIAAPPVEASLGTPLSAPIPAPIPVPNASLYASPAVPQAFAHLEPDNQEVLSAPNDERAQYLQTSHLSEQLGEGEADQDAGLLPPPGLSRLVLGQPELDSQQQRQVTGATEQPPLNVAQAAALHMQERRADGEDTSDGEQQVRNIQTPPRRVVTGVETNAPSLREQREVVLDGENLEDREAIPPPTLAELPTTSVHHNILPDEAEQLHHNNPPQAMTPLNAQQPHQQQSTLQQQHQQHSTTQQEKKRAAVGRRTTASLDLESDESDEFLQSERERDRERERRDLMEERHSRGRSHSHYPYEGETEDSVRGAAHHETKSLRETHHKRNHDSARSRRHQDPKVERERERDRERDRTWRRRSNKYHSGGEDPDRSYDHSRRYNNSNYEGESDNPEYNHMGDAELDGSGGRSSKTSRHRRSAAEEDFDDYERERNRSRRSTKPQSSAEKSRSSGGRRNYENSGRSARADDGRRRYQDQRNPGAQYPVSATGYVPYGMYEQMSRNPQVYADMYAKFYGQMINSMNAAVSAAASKGGVPAGAGVIPGLMPSAVPVSAAQLVAATSGGSVSGSSEAAMLRERERAAADAAPSTYGGVAGTAGPVTNTAVARPPRRRTPLQFSRPHLVASYAMSLLLKVKPKYAGRGRLRNDVEVAPPRIRDGTSSLLRMYPGPLQGRKLHKDKIISFCKEQIRLGPTKGCTALYATQKKPQGSVTKYRASHALMWHLLILLLRQNGYIADTDVGDLLLENQQEYPYDPSEFEAENEPDADAEQDAAAPADKTVDSDLDSESAAGVTPAEPLAAGAATSSINGADAANAATPLSEQAATDKFRSYVLRGNVEEALQWATDNGLWTHAFFLALYEDRYALTDVAQKFLNRAIKANDPLQTLYQMKSCHTPACVSQLRDEQWGDWRSHLSILVTNKSRQPEYDRSSVVALGDTLFQRGDIYAAHFCYLVAQEEFGRYDSSATELTTLTANVPRLILLGSSHYKHFNEFASNEAIIMTEIYEYARSLFDPKFSIAHFQHYKFLLATRILDYGQHFRCTNYLEQIARHIELKPESYDSNFIQRVCGLAERLRYHDPILINRVSFASPPNATSKDSAAAEEKAWLRQLRSLAYVPQQEQLQQLQQNQQVQQEQNDIDQQFAEVNKQFRELNMQYESNSNMENTLQPQLPPVDQQPPQQQQQVLSESYQQPTQQYYEPPPQAPTESDPYGQGQPSYYDPNAGQLHYDPNAAQHQYDQQQPQPQPTPSYGQIEPGTEAYQPGQATADPAAVPSGYGYDYWSGTQQPPYGDEPNENQAALKDEEEEDEEQDEQQILQYAKQQILQQTKQQQLQQEQHTRSNGAASINNRFKSNALKQERSSGSLRKRQEASRTATIAAAAAAIAQITPATVAAAATPPAASAKAFNLNDLQQQTRPAISMPKSKSYGDEDDGGSGGVADPGQKTKPVGSSEAAGKQQASGKQANSGSDLGAPGNKNAGWFGGLWNKLSLKPKNQMILPDDKNPAIVWDKERKCWTNTEGNGDEAESFKPPPKMSDLGMALGGPPAAPIGNAGLGMGLMPVANNAPGSHQSAPLMDQQTPSQPQTYGSPIDYTAAPAPELIPTVPSPAPLSVPSSAPAALAAPNPAAVPGGPQPKLQSNMFKMQRNRTLKNSYVDVFNPSGAPMSAAPENVLAPMMAPAAVPQGGYFVPQQ
Protein: Tachykinin-like peptide-X (P.nigriventer tachykinin peptides X) (PnTkP-X) (U29-ctenitoxin-Pn1j) (U29-CNTX-Pn1j) (P86307)
Organism: Phoneutria nigriventer (Brazilian armed spider) (Ctenus nigriventer)
Subcellular location: Secreted {ECO:0000269|PubMed:15573368}.
Interaction partners:
Sequence:
QKKDKKDKFYGLM