wanglab/gogpt-training-data huggingface dataset:
Protein: LD20463p (Scaffold protein containing ankyrin repeats and SAM domain, isoform A) (Scaffold protein containing ankyrin repeats and SAM domain, isoform B) (Q7JQL2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Uncharacterized protein, isoform D
- Oxidative stress-responsive serine-rich protein 1
- Myosin-VIIa
- Eukaryotic translation initiation factor 4 gamma 2
- Myosin 28B1, isoform B
Sequence:
MSSDRFHKAAKDGLLDVLAAATRKDTNAKDSDSMTPVMWAAFEGRLDALRLLCGRGGDPDKCDQFGNTALHLASAKGHLHCVDFLVKFGVNIYALDIDKHSAKDLAAINGRDEILRYLDVAFTNFEATEKKKSKALKELAEKNCEKRVREYMKRQNQQQQRQDPEYSDLSAPSGSSKTGNMLSTLKQKIWSSQGNLNKTPRDTPPPTKFSDLVGNGSSSSGGSTIASRAGTVQKRPSQLQKQHSSTCPHSKISSDTDGGFKVREVEPDGKRTITSLTGLQRDSEVLYVGTFSSNEDSVGKRGKISDVFECMEADELDHSDNRSGYSSTLARSFSQPDILGDGQLTQELSEEVTLQRPVGLFDRPTMLGSIAFRRSVTAALSQLQLHTDTSSTSTMRNAGSNPPKTRNGGGKGRLYLNLSDDTDSEGGGHDIYSDDDDDDRDAGGSALQRFLAVWALEEYLPVFQKQEIDLETLMLLTESDLKSLGLPLGPFRKLTFAIQERRNALANPGPLVDSRL
Protein: SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 4 (A0A2R8Y523)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
XDEGHRMKNHHCKLTQVLNTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLHKVLRPFLLRRLKKEVEAQLPEKVEYVIKCDMSALQRVLYRHMQAKGVLLTDGSEKDKKGKGGTKTLMNTIMQLRKICNHPYMFQHIEESFSEHLGFTGGIVQGLDLYRASGKFELLDRILPKLRATNHKVLLFCQMTSLMTIMEDYFAYRGFKYLRLDGTTKAEDRGMLLKTFNEPGSEYFIFLLSTRAGGLGLNLQSADTVIIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILAAAKYKLNVDQKVIQAGMFDQKSSSHERRAFLQAILEHEEQDESRHCSTGSGSASFAHTAPPPAGVNPDLEEPPLKEEDEVPDDETVNQMIARHEEEFDLFMRMDLDRRREEARNPKRKPRLMEEDELPSWIIKDDAEVERLTCEEEEEKMFGRGSRHRKEVDYSDSLTEKQWLKKITGKDIHDTASSVARGLQFQRGLQFCTRASKAIEEGTLEEIEEEVRQKKSSRKRKRDSDAGSSTPTTSTRSRDKDDESKKQKKRGRPPAEKLSPNPPNLTKKMKKIVDAVIKYKDSSGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFTSVRQKIEKEDDSEGEESEEEEEGEEEGSESESRSVKVKIKLGRKEKAQDRLKGGRRRPSRGSRAKPVVSDDDSEEEQEEDRSGSGSEED
Protein: Protease (EC 3.4.22.39) (Adenain) (Adenovirus protease) (AVP) (Adenovirus proteinase) (Endoprotease) (P03252)
Organism: Human adenovirus C serotype 2 (HAdV-2) (Human adenovirus 2)
Function: Cleaves viral precursor proteins (pTP, pIIIa, pVI, pVII, pVIII, and pX) inside newly assembled particles giving rise to mature virions. Protease complexed to its cofactor slides along the viral DNA to specifically locate and cleave the viral precursors. Mature virions have a weakened organization compared to the unmature virions, thereby facilitating subsequent uncoating. Without maturation, the particle lacks infectivity and is unable to uncoat. Late in adenovirus infection, in the cytoplasm, may participate in the cytoskeleton destruction. Cleaves host cell cytoskeletal keratins K7 and K18.
Subcellular location: Virion {ECO:0000255|HAMAP-Rule:MF_04059, ECO:0000269|PubMed:12645618}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04059, ECO:0000305|PubMed:12645618}. Note=Present in about 10 copies per virion. {ECO:0000255|HAMAP-Rule:MF_04059}.
Interaction partners:
Sequence:
MGSSEQELKAIVKDLGCGPYFLGTYDKRFPGFVSPHKLACAIVNTAGRETGGVHWMAFAWNPRSKTCYLFEPFGFSDQRLKQVYQFEYESLLRRSAIASSPDRCITLEKSTQSVQGPNSAACGLFCCMFLHAFANWPQTPMDHNPTMNLITGVPNSMLNSPQVQPTLRRNQEQLYSFLERHSPYFRSHSAQIRSATSFCHLKNM
Protein: IP10876p (Q9VBS8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAEDSLADQLNVPEWLNEQFVTDVLRSHEKEPDLRVTKLDFTPGSAKGDNYASVIIRARVEYITQKGFFSKSLIIKTVLEMFAGSALFKTEIGMYRKVLPEFARILRENNDTSRLYAECIYYSLEPSQVMIFEDLGEMDYAMVRDRVLTHGEICGAYSKLAKFHALSMKIINERPEFVKEFKDGICLVDIPYMSSGMGPFKDFLGRIPELDRYKTHFEKIEVHFIDRLRDIMKEYQTNPQPGYYVLCHGDYHTRNIMVKHNKESGGFEDCMLLDYQGCYVAPLAFDLMYSIYMLMNREQRIGELETLLNYYFSVLRETLRKIGYQGKLPDPPAFWKEMYRLKDYEFLFLSTYLPMSVGLSLETATNEETDDKLQDFIEECKSILARFERSGYFENL
Protein: Galectin (Q7SXJ0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MEMKISGKVKPGCDAFSINIGHDDDAIALHFNPRFNAHGDSNTIVCNSKQGGWGSEHREHCFPFQQGEEFKLSITFNNETFYIKLPEGTMMSFPNRFGDDAFTHVHVKGDVKIISVKAK
Protein: Ethylene-responsive transcription factor ERF120 (Q9SK67)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probably acts as a transcriptional activator. Binds to the GCC-box pathogenesis-related promoter element. May be involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Ethylene-responsive transcription factor ERF025
Sequence:
MENSENVPSYDQNINFTPNLTRDQEHVIMVSALQQVISNVGGDTNSNAWEADLPPLNAGPCPLCSVTGCYGCVFPRHEAIIKKEKKHKGVRKKPSGKWAAEIWDPSLKVRRWLGTFPTAEMAAKAYNDAAAEFVGRRSARRGTKNGEEASTKKTTEKN
Protein: ATP-dependent helicase/nuclease subunit A (EC 3.1.-.-) (EC 5.6.2.4) (ATP-dependent helicase/nuclease AddA) (DNA 3'-5' helicase AddA) (P23478)
Organism: Bacillus subtilis (strain 168)
Function: An essential component of the DNA double-stranded break repair machinery, the heterodimer acts as both an ATP-dependent DNA helicase and an ATP-dependent, dual-direction single-stranded exonuclease. Recognizes the B.subtilis chi site (5'-AGCGG-3') which transforms the enzyme from a helicase which degrades both DNA strands to one with only 5' -> 3' exonuclease activity. This generates a double-stranded DNA with a protruding 3'-terminated single-stranded tail suitable for the initiation of homologous recombination (chi fragment). The AddA nuclease domain in particular is required for chi fragment generation; this subunit has 3' -> 5' nuclease and helicase activity. RecA thread formation during DNA double-strand break repair requires RecJ or AddAB.
Interaction partners:
- ATP-dependent helicase/deoxyribonuclease subunit B
- Nuclease SbcCD subunit D
- Nuclease SbcCD subunit C
- Single-stranded-DNA-specific exonuclease RecJ
- DNA replication and repair protein RecF
- Probable ATP-dependent DNA helicase RecS
- DNA repair protein RecN
- ATP-dependent RecD2 DNA helicase
- Holliday junction resolvase RecU
- Protein RecA
Sequence:
MNIPKPADSTWTDDQWNAIVSTGQDILVAAAAGSGKTAVLVERMIRKITAEENPIDVDRLLVVTFTNASAAEMKHRIAEALEKELVQRPGSLHIRRQLSLLNRASISTLHSFCLQVLKKYYYLIDLDPGFRIADQTEGELIGDEVLDELFEDEYAKGEKAFFELVDRYTTDRHDLDLQFLVKQVYEYSRSHPNPEAWLESFVHLYDVSEKSAIEELPFYQYVKEDIAMVLNGAKEKLLRALELTKAPGGPAPRADNFLDDLAQIDELIQHQDDFSELYKRVPAVSFKRAKAVKGDEFDPALLDEATDLRNGAKKLLEKLKTDYFTRSPEQHLKSLAEMKPVIETLVQLVISYGKRFEAAKQEKSIIDFSDLEHYCLAILTAENDKGEREPSEAARFYQEQFHEVLVDEYQDTNLVQESILQLVTSGPEETGNLFMVGDVKQSIYRFRLAEPLLFLSKYKRFTESGEGTGRKIDLNKNFRSRADILDSTNFLFKQLMGGKIGEVDYDEQAELKLGAAYPDNDETETELLLIDNAEDTDASEEAEELETVQFEAKAIAKEIRKLISSPFKVYDGKKKTHRNIQYRDIVILLRSMPWAPQIMEELRAQGIPVYANLTSGYFEAVEVAVALSVLKVIDNPYQDIPLASVLRSPIVGADENELSLIRLENKKAPYYEAMKDYLAAGDRSDELYQKLNTFYGHLQKWRAFSKNHSVSELIWEVYRDTKYMDYVGGMPGGKQRQANLRVLYDRARQYESTAFRGLFRFLRFIERMQERGDDLGTARALSEQEDVVRLMTIHSSKGLEFPVVFVAGLGRNFNMMDLNKSYLLDKELGFGTKYIHPQLRISYPTLPLIAMKKKMRRELLSEELRVLYVALTRAKEKLFLIGSCKDHQKQLAKWQASASQTDWLLPEFDRYQARTYLDFIGPALARHRDLGDLAGVPAHADISGHPARFAVQMIHSYDLLDDDLEERMEEKSERLEAIRRGEPVPGSFAFDEKAREQLSWTYPHQEVTQIRTKQSVSEIKRKREYEDEYSGRAPVKPADGSILYRRPAFMMKKGLTAAEKGTAMHTVMQHIPLSHVPSIEEAEQTVHRLYEKELLTEEQKDAIDIEEIVQFFHTEIGGQLIGAKWKDREIPFSLALPAKEIYPDAHEADEPLLVQGIIDCLYETEDGLYLLDYKSDRIEGKFQHGFEGAAPILKKRYETQIQLYTKAVEQIAKTKVKGCALYFFDGGHILTL
Protein: Collagen alpha-2(IX) chain (Q14055)
Organism: Homo sapiens (Human)
Function: Structural component of hyaline cartilage and vitreous of the eye.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
Interaction partners:
- Collagen alpha-3
- Collagen alpha-1
- Matrilin-3
- CD44 antigen
- Platelet glycoprotein VI
- Sulfate transporter
- Cartilage intermediate layer protein 1
- Multifunctional procollagen lysine hydroxylase and glycosyltransferase LH3
- Collagen alpha-1
- Hyaluronan and proteoglycan link protein 1
Sequence:
MAAATASPRSLLVLLQVVVLALAQIRGPPGERGPPGPPGPPGVPGSDGIDGDNGPPGKAGPPGPKGEPGKAGPDGPDGKPGIDGLTGAKGEPGPMGIPGVKGQPGLPGPPGLPGPGFAGPPGPPGPVGLPGEIGIRGPKGDPGPDGPSGPPGPPGKPGRPGTIQGLEGSADFLCPTNCPPGMKGPPGLQGVKGHAGKRGILGDPGHQGKPGPKGDVGASGEQGIPGPPGPQGIRGYPGMAGPKGETGPHGYKGMVGAIGATGPPGEEGPRGPPGRAGEKGDEGSPGIRGPQGITGPKGATGPPGINGKDGTPGTPGMKGSAGQAGQPGSPGHQGLAGVPGQPGTKGGPGDQGEPGPQGLPGFSGPPGKEGEPGPRGEIGPQGIMGQKGDQGERGPVGQPGPQGRQGPKGEQGPPGIPGPQGLPGVKGDKGSPGKTGPRGKVGDPGVAGLPGEKGEKGESGEPGPKGQQGVRGEPGYPGPSGDAGAPGVQGYPGPPGPRGLAGNRGVPGQPGRQGVEGRDATDQHIVDVALKMLQEQLAEVAVSAKREALGAVGMMGPPGPPGPPGYPGKQGPHGHPGPRGVPGIVGAVGQIGNTGPKGKRGEKGDPGEVGRGHPGMPGPPGIPGLPGRPGQAINGKDGDRGSPGAPGEAGRPGLPGPVGLPGFCEPAACLGASAYASARLTEPGSIKGP
Protein: Gamma-synuclein (Persyn) (Q9Z0F7)
Organism: Mus musculus (Mouse)
Function: Plays a role in neurofilament network integrity. May be involved in modulating axonal architecture during development and in the adult. In vitro, increases the susceptibility of neurofilament-H to calcium-dependent proteases. May also function in modulating the keratin network in skin. Activates the MAPK and Elk-1 signal transduction pathway (By similarity).
Subcellular location: Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Associated with centrosomes in several interphase cells. In mitotic cells, localized to the poles of the spindle (By similarity). {ECO:0000250}.
Interaction partners:
Sequence:
MDVFKKGFSIAKEGVVGAVEKTKQGVTEAAEKTKEGVMYVGTKTKENVVQSVTSVAEKTKEQANAVSEAVVSSVNTVANKTVEEAENIVVTTGVVRKEDLEPPAQDQEAKEQEENEEAKSGED
Protein: Diaminopimelate decarboxylase (DAP decarboxylase) (DAPDC) (EC 4.1.1.20) (P19572)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine.
Interaction partners:
- Diaminopimelate epimerase
- 4-hydroxy-tetrahydrodipicolinate reductase
- 4-hydroxy-tetrahydrodipicolinate synthase
- UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
- Aspartokinase
- 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase
- Lipopeptide
- Argininosuccinate synthase
- DUF484 family protein
- Argininosuccinate lyase
Sequence:
MDTFSYRDAELFAEGVALSRIAERFGTPTYVYSRAHIEAQYRAYADALAGMPHLVCFAVKANSNLGVLNVLARLGAGFDIVSRGELERVLAAGGDPAKVVFSGVGKTRDDMRRALEVGVHCFNVESGEELERLQRVAAELGVKAPVSLRVNPDVDAQTHPYISTGLKENKFGIAIDEAEAVYARAAELDHLEVIGVDCHIGSQLTQLEPFLDALERLLGLVDRLAGKGIGIRHLDLGGGLGVRYRDEQPPLAGDYIRAIRERLHGRDLTLVFEPGRSIVANAGVLLTRVEYLKHTEHKDFAIVDAAMNDLIRPALYQAWMDVQAVRPRDAAPRRYDLVGPICETGDFLAKDRDLALAEGDLLAVRSAGAYGFVMSSNYNTRGRAAEVLVDGEQTHEVRRRETVQELYAGESLLPQ
Protein: Superinfection exclusion protein A (Q38674)
Organism: Salmonella phage P22 (Bacteriophage P22)
Function: Probably blocks the subsequent transfer of the phage DNA across the inner membrane into the cytoplasm. By this means, P22 excludes superinfection by the phages of the same family and also against DNA coming from oter phages.
Subcellular location: Host cell inner membrane {ECO:0000269|PubMed:7768804}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MSDSMSYAVLVAATLFLGIGLQIAWLFFSNFIKRKRLESRISEVSIAIGKNAKNPENEAYVLNYLKEKFSPERFENRITDALGLIISVIHIPLSLLITVWYFAMIAGRIFGFMNIEPVVLWVPMILQLLLSIAIFIFSVFIKIVFGRYPGEANGFNKEFIKTIK
Protein: Polypeptide N-acetylgalactosaminyltransferase 10 (F2Z2M7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRRKEKRLLQAVALVLAALVLLPNVGLWALYRERQPDGTPGGSGAAVAPAAGQGSHSRQKKTFFLGDGQKLKDWHDKEAIRRDAQRVGNGEQGRPYPMTDAERVDQAYRENGFNIYVSDKISLNRSLPDIRHPNCNSKRYLETLPNTSIIIPFHNEGWSSLLRTVHSVLNRSPPELVAEIVLVDDFSDRDLPTASTPSPFVC
Protein: Protein YIPF5 (Five-pass transmembrane protein localizing in the Golgi apparatus and the endoplasmic reticulum 5) (Smooth muscle cell-associated protein 5) (SMAP-5) (YIP1 family member 5) (YPT-interacting protein 1 A) (Q969M3)
Organism: Homo sapiens (Human)
Function: Plays a role in transport between endoplasmic reticulum and Golgi. In pancreatic beta cells, required to transport proinsulin from endoplasmic reticulum into the Golgi.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9EQQ2}; Multi-pass membrane protein. Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:27999994}; Multi-pass membrane protein. Cytoplasmic vesicle, COPII-coated vesicle {ECO:0000250|UniProtKB:Q5XID0}. Note=Enriched at the endoplasmic reticulum exit sites (By similarity). Incorporated into COPII-coated vesicles (By similarity). {ECO:0000250|UniProtKB:Q5XID0, ECO:0000250|UniProtKB:Q9EQQ2}.
Interaction partners:
- Protein YIF1A
- Protein transport protein Sec24B
- Protein YIF1B
- Sorting and assembly machinery component 50 homolog
- Protein YIPF3
- Immediate early response 3-interacting protein 1
- Serine/threonine-protein kinase/endoribonuclease IRE1
Sequence:
MSGFENLNTDFYQTSYSIDDQSQQSYDYGGSGGPYSKQYAGYDYSQQGRFVPPDMMQPQQPYTGQIYQPTQAYTPASPQPFYGNNFEDEPPLLEELGINFDHIWQKTLTVLHPLKVADGSIMNETDLAGPMVFCLAFGATLLLAGKIQFGYVYGISAIGCLGMFCLLNLMSMTGVSFGCVASVLGYCLLPMILLSSFAVIFSLQGMVGIILTAGIIGWCSFSASKIFISALAMEGQQLLVAYPCALLYGVFALISVF
Protein: Tyrosine specific protein phosphatases domain-containing protein (P96830)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MAVRELPGAWNFRDVADTATALRPGRLFRSSELSRLDDAGRATLRRLGITDVADLRSSREVARRGPGRVPDGIDVHLLPFPDLADDDADDSAPHETAFKRLLTNDGSNGESGESSQSINDAATRYMTDEYRQFPTRNGAQRALHRVVTLLAAGRPVLTHCFAGKDRTGFVVALVLEAVGLDRDVIVADYLRSNDSVPQLRARISEMIQQRFDTELAPEVVTFTKARLSDGVLGVRAEYLAAARQTIDETYGSLGGYLRDAGISQATVNRMRGVLLG
Protein: Adrenodoxin-like protein 1, mitochondrial (Mitochondrial ferredoxin 1) (AtMFDX1) (Q9M0V0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Associates in vitro with the adrenodoxin reductase MFDR to form an efficient low potential electron transfer chain that is able to reduce cytochrome C. Functions as accessory mitochondrial protein involved with BIO2 in the plant biotin synthase reaction.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:12714594, ECO:0000269|PubMed:13677469}.
Interaction partners:
- NADPH:adrenodoxin oxidoreductase, mitochondrial
- Frataxin, mitochondrial
- Iron-sulfur cluster assembly protein 1
- RING/FYVE/PHD zinc finger superfamily protein
- Cysteine desulfurase, mitochondrial
- Iron-sulfur cluster assembly protein 3
- Iron-sulfur cluster assembly protein 2
- Biotin synthase, mitochondrial
- Monothiol glutaredoxin-S15, mitochondrial
- NifU-like protein 1, chloroplastic
Sequence:
MIGHRISRLGSTIVKQLAREGYLATYGTKNLHRSYGHYLQSLPVVPRQARTSQEAWFLKSHKFCTSSTTSSENGDEETEKITIIFVDKDGEEIPVKVPIGMSVLEAAHENDIDLEGACEASLACSTCHVIVMDTEYYNKLEEPTDEENDMLDLAFGLTETSRLGCQVIARPELDGVRLAIPSATRNFAVDGFVPKPH
Protein: Tripartite motif containing 39 (H0Y735)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XTSRYRSLRPNRQLGSMVEIAKQLQAVKRKIRDESLCPQHHEALSLFCYEDQEAVCLICAISHTHRAHTVVPLDDATQEYKEKLQKCLEPLEQKLQEITRCKSSEEKKPGELKRLVESRRQQILREFEELHRRLDEEQQVLLSRLEEEEQDILQRLRENAAHLGDKRRDLAHLAAEVEGKCLQSGFEMLKDVKSTLEKCEKVKTMEVTSTTPCTSLHSEINDNVRGR
Protein: Methylesterase 2 (AtMES2) (EC 3.1.1.-) (Protein METHYLESTERASE 8) (AtME8) (O80476)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Methylesterase shown to have carboxylesterase activity, methyl indole-3-acetic acid (MeIAA) esterase activity, methyl salicylate (MeSA) esterase activity and methyl jasmonate (MeJA) esterase activity in vitro.
Interaction partners:
- Alpha/beta-Hydrolases superfamily protein
- S-adenosyl-L-methionine-dependent methyltransferases superfamily protein
- Probable carboxylesterase 12
- Prolyl endopeptidase
- Serine carboxypeptidase-like 11
- Alpha/beta-Hydrolases superfamily protein
- Prolyl endopeptidase
- Acylamino-acid-releasing enzyme
- Probable carboxylesterase 8
Sequence:
MSEEKRKQHFVLVHGACHGAWCWYKVKPLLEALGHRVTALDLAASGIDTTRSITDISTCEQYSEPLMQLMTSLPNDEKVVLVGHSFGGLSLALAMDKFPDKISVSVFVTAFMPDTKHSPSFVEEKFASSMTPEGWMGSELETYGSDNSGLSVFFSTDFMKHRLYQLSPVEDLELGLLLKRPSSLFINELSKMENFSEKGYGSVPRAYIVCKEDNIISEDHQRWMIHNYPANLVIEMEETDHMPMFCKPQLLSDHLLAIADNFC
Protein: Small ribosomal subunit protein uS19 (40S ribosomal protein S15) (RIG protein) (P62844)
Organism: Sus scrofa (Pig)
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P62841}.
Interaction partners:
- Small ribosomal subunit protein uS9
- Small ribosomal subunit protein uS13
- Small ribosomal subunit protein uS2
- Small ribosomal subunit protein uS7
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS14
- 40S ribosomal protein S30
- Small ribosomal subunit protein uS12
- Small ribosomal subunit protein eS21
- Ubiquitin-like protein FUBI
Sequence:
MAEVEQKKKRTFRKFTYRGVDLDQLLDMSYEQLMQLYSARQRRRLNRGLRRKQHSLLKRLRKAKKEAPPMEKPEVVKTHLRDMIILPEMVGSMVGVYNGKTFNQVEIKPEMIGHYLGEFSITYKPVKHGRPGIGATHSSRFIPLK
Protein: Glycogen phosphorylase (EC 2.4.1.1) (P9WMW1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties (By similarity).
Interaction partners:
- Glucose-1-phosphate adenylyltransferase
- 1,4-alpha-glucan branching enzyme GlgB
- Glycogen operon protein GlgX homolog
- Alpha-maltose-1-phosphate synthase
- Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase
- Probable phosphoglucomutase PgmA
- 4-alpha-glucanotransferase
- Trehalose synthase/amylase TreS
- Probable 1,4-alpha-glucan branching enzyme Rv3031
- UTP--glucose-1-phosphate uridylyltransferase
Sequence:
MKALRRFTVRAHLPERLAALDQLSTNLRWSWDKPTQDLFAAIDPALWEQCGHDPVALLGAVNPARLDELALDAEFLGALDELAADLNDYLSRPLWYQEQQDAGVAAQALPTGIAYFSLEFGVAEVLPNYSGGLGILAGDHLKSASDLGVPLIAVGLYYRSGYFRQSLTADGWQHETYPSLDPQGLPLRLLTDANGDPVLVEVALGDNAVLRARIWVAQVGRVPLLLLDSDIPENEHDLRNVTDRLYGGDQEHRIKQEILAGIGGVRAIRAYTAVEKLTPPEVFHMNEGHAGFLGIERIRELVTDAGLDFDTALTVVRSSTVFTTHTPVPAGIDRFPLEMVQRYVNDQRGDGRSRLLPGLPADRIVALGAEDDPAKFNMAHMGLRLAQRANGVSLLHGRVSRAMFNELWAGFDPDEVPIGSVTNGVHAPTWAAPQWLQLGRELAGSDSLREPVVWQRLHQVDPAHLWWIRSQLRSMLVEDVRARLRQSWLERGATDAELGWIATAFDPNVLTVGFARRVPTYKRLTLMLRDPDRLEQLLLDEQRPIQLIVAGKSHPADDGGKALIQQVVRFADRPQVRHRIAFLPNYDMSMARLLYWGCDVWLNNPLRPLEACGTSGMKSALNGGLNLSIRDGWWDEWYDGENGWEIPSADGVADENRRDDLEAGALYDLLAQAVAPKFYERDERGVPQRWVEMVRHTLQTLGPKVLASRMVRDYVEHYYAPAAQSFRRTAGAQFDAARELADYRRRAEEAWPKIEIADVDSTGLPDTPLLGSQLTLTATVRLAGLRPNDVTVQGVLGRVDAGDVLMDPVTVEMAHTGTGDGGYEIFSTTTPLPLAGPVGYTVRVLPRHPMLAASNELGLVTLA
Protein: Sigma factor binding protein 2, chloroplastic (Sigma factor binding protein II) (VQ motif-containing protein 16) (AtVQ16) (O80669)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Functions as activator of WRKY33 in plant defense against necrotrophic pathogens by stimulating the DNA-binding activity of WRKY33.
Subcellular location: Plastid, chloroplast {ECO:0000250|UniProtKB:Q9LDH1}. Nucleus {ECO:0000269|PubMed:21990940}. Note=Can localize to both chloroplast and nucleus. {ECO:0000305}.
Interaction partners:
- Probable WRKY transcription factor 33
- Protein MKS1
- VQ motif-containing protein 22
- VQ motif-containing protein 9
- VQ motif-containing protein 29
- Calmodulin-binding protein 25
- VQ motif-containing protein 20
- Protein HAIKU1
- VQ motif-containing protein 4
- VQ motif-containing protein 8, chloroplastic
Sequence:
MDQSSSTLLINQRKSSSSPTRIPPKQKRKSTTTHKPIKVRYISNPMRVETCPSKFRELVQELTGQDAADLPPSPTTFTAVDLHRPCESEMNLEPLDGEVRGEYYSPLDEEVFNAPQMSAGLSGFFSSGFYNVNALGSIGSL
Protein: Proline-rich antimicrobial peptide 2 (P85212)
Organism: Galleria mellonella (Greater wax moth)
Function: Antimicrobial protein. Has antibacterial activity against the Gram-positive bacterium M.luteus (MIC=8.6 uM). Lacks antibacterial activity against the Gram-positive bacteria B.circulans, L.monocytogenes, S.aureus, and S.lutea, and the Gram-negative bacteria E.coli D31, E.coli ATCC 25922, and S.typhimurium. Lacks antifungal activity against S.cerevisiae, P.pastoris, Z.marxianus, C.albicans, C.fructus, C.wickerhamii, A.niger, F.oxysporum, and T.harizianum.
Subcellular location: Secreted {ECO:0000269|PubMed:17194500}.
Interaction partners:
Sequence:
EIRLPEPFRFPSPTVPKPIDIDPILPHPWSPRQTYPIIARRS
Protein: GDP-mannose 4,6 dehydratase 1 (EC 4.2.1.47) (GDP-D-mannose dehydratase 1) (GMD 1) (Q9SNY3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the conversion of GDP-D-mannose to GDP-4-dehydro-6-deoxy-D-mannose.
Interaction partners:
- Putative GDP-L-fucose synthase 2
- GDP-L-fucose synthase 1
- Mannose-1-phosphate guanylyltransferase 1
- ADP-glucose pyrophosphorylase family protein
- Probable mannose-1-phosphate guanylyltransferase 2
- Probable mannose-1-phosphate guanylyltransferase 3
- ADP-glucose pyrophosphorylase family protein
- GDP-mannose 3,5-epimerase
- GDP-mannose 4,6 dehydratase 2
- Dolichol-phosphate mannosyltransferase subunit 1
Sequence:
MASRSLNGDSDIVKPRKIALVTGITGQDGSYLTEFLLEKGYEVHGLIRRSSNFNTQRLNHIYVDPHNVNKALMKLHYGDLSDASSLRRWLDVIKPDEVYNLAAQSHVAVSFEIPDYTADVVATGALRLLEAVRSHNIDNGRAIKYYQAGSSEMFGSTPPPQSETTPFHPRSPYAASKCAAHWYTVNYREAYGLYACNGILFNHESPRRGENFVTRKITRALGRIKVGLQTKLFLGNIQASRDWGFAGDYVEAMWLMLQQEKPDDYVVATEESHTVKEFLDVSFGYVGLNWKDHVEIDKRYFRPTEVDNLKGDASKAKEMLGWKPKVGFEKLVKMMVDEDLELAKREKVLADAGYMDAQQQP
Protein: Inositol-3-phosphate synthase (MIP synthase) (EC 5.5.1.4) (Myo-inositol 1-phosphate synthase) (IPS) (MI-1-P synthase) (O97477)
Organism: Drosophila melanogaster (Fruit fly)
Function: Key enzyme in myo-inositol biosynthesis pathway that catalyzes the conversion of glucose 6-phosphate to 1-myo-inositol 1-phosphate in a NAD-dependent manner. Rate-limiting enzyme in the synthesis of all inositol-containing compounds (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P11986}.
Interaction partners:
- Inositol-1-monophosphatase
- Inositol-1-monophosphatase
- Inositol-1-monophosphatase
- Inositol-1-monophosphatase
- inositol-phosphate phosphatase
- Inositol-1-monophosphatase
- phosphatidylinositol-3,4-bisphosphate 4-phosphatase
- Delta-1-pyrroline-5-carboxylate synthase
Sequence:
MKPTNNSTLEVISPKVQVDDEFITTDYDYQTSHVKRTADGQLQVHPQTTSLKIRTGRHVPKLGVMLVGWGGNNGSTLTAALEANRRQLKWRKRTGVQEANWYGSITQASTVFIGSDEDGGDVYVPMKELLPMVEPDNIIVDGWDISGLHLGDAMRRAEVLDVALQDQIYDQLAQLRPRPSIYDPDFIAANQSDRADNVIRGTRLEQYEQIRKDIRDFRERSGVDSVIVLWTANTERFADVQPGLNTTSQELIASLEANHSEVSPSTIFAMASIAEGCTYINGSPQNTFVPGLIQLAEEKNVFIAGDDFKSGQTKIKSVLVDFLVGAGIKPVSIASYNHLGNNDGKNLSAPQQFRSKEISKSNVVDDMVASNRLLYGPDEHPDHVVVIKYVPYVGDSKRAMDEYTSEIMMGGHNTLVIHNTCEDSLLATPLILDLVILGELSTRIQLRNAEKESAPWVPFKPVLSLLSYLCKAPLVPQGSQVVNSLFRQRAAIENILRGCIGLPPISHMTLEQRFDFSTITNEPPLKRVKILGQPCSVESVTNGKKLHANGHSNGSAKLATNGNGH
Protein: Mitochondrial import inner membrane translocase subunit TIM50 (Q38D43)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|RuleBase:RU365079}; Single-pass membrane protein {ECO:0000256|RuleBase:RU365079}.
Interaction partners:
Sequence:
MEHFAPCAIRTKRFEVDQYVRVQLSNGRSEIGVVVSLDEVNDTAVIATRHGYDVTVRLDSVHRAFLLVLDLNGVLVARGRGSFADRPGVEEFVRFVMNNFVVAVWTSGLERTSIPIIDKVLNGYQDRLLFQLYRDSCGARPTPDKPYHTVKNLQRIFDSYPKSFNAVNTIIVDDSPDKCSHPDIALCPESFNDPERQANDRGLEMAMEVLKEVLRTDSHEPLIRAAQERLLAIAKRKEEAKEKQLNEGAKLSDVTDHMKGAAYNNANANTNGNGSGNGNDDDDNNNNNRNRNDDRSNSRKRSEGNNAKKDRSEHRSSDRREEPDTDAAAMKPSETFFWETRLCCENISVGCTRDACRFSHDPDDGKRPCSRKDKCRRGHANRWSTPVMGQKQKEKYQKVAVVRSSKSPQQATKAAGCTAVRGGGGMLDVLGLPEDVPLFSTHPDLQKGPDSRHPAVEPQLTASEELRQLIGLQSQQWKRPASGTVAQKPSGALHFKSDGGNGVSLLRQLQATVGAVSGGSEKVNRRKHRNR