wanglab/gogpt-training-data huggingface dataset:
Protein: Dihydropyrimidinase-related protein 5 (DRP-5) (UNC33-like phosphoprotein 6) (ULIP-6) (Q9JHU0)
Organism: Rattus norvegicus (Rat)
Function: Involved in the negative regulation of dendrite outgrowth.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Dihydropyrimidinase-related protein 2
- Tyrosine-protein kinase
- Amphiphysin
- Leucine-rich glioma-inactivated protein 1
- Myc box-dependent-interacting protein 1
- Dihydroorotate dehydrogenase
- Dihydropyrimidine dehydrogenase [NADP
- Delta and Notch-like epidermal growth factor-related receptor
- Zic family member 4
- Dihydropyrimidinase-related protein 3
Sequence:
MLANSASVRILIKGGKVVNDDCTHEADVYIENGIIQQVGRELMIPGGAKVIDATGKLVIPGGIDTSTHFHQTFMNATCVDDFYHGTKAALVGGTTMIIGHVLPDKETSLVEAYEKCRALADPKVCCDYALHVGITWWAPKVKAEMETLVREKGVNSFQMFMTYKDLYMLRDSELYQVFHACRDFGAIPRVHAENGELVAEGAKEALDLGITGPEGIEISHPEELEAEATHRVITIANRTHCPIYLVNVSSISAGDVIAAAKMQGKVVLAETTNAHATLTGLHYYHQDWSHAAAYVTVPPLRLDTNTSTYLMSLLANDTLNIVASDHRPFTTKQKAMGKEDFTKIPHGVSGVQDRMSVVWERGVVGGKMDENRFVAVTSSNAAKILNLYPRKGRIIPGADADVVVWDPEATKTISASTQVQGGDFNLYENMRCHGVPLVTISRGRVVYENGVFMCAEGTGKFCPLRSFPDIVYKKLVQREKTLKVRGVDRTPYLGDVAVVVNPGKKEMGTPLADTPTRPVTRHGGMRDLHESSFSLSGSQIDDHVPKRASARILAPPGGRSSGIW
Protein: Dentin sialophosphoprotein-like protein (Q9SD86)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MPGNEFGERTHNFFGQEGLSQDQHQSQVVDGSWSSFSNGLVGNQRQIDPSLTADLKSYRTQQPVDPERGQSSNSQHGLNFTQQPMRSEYSRSVLQEPQQPTNGYMHGNLGLQTMPNEANVLGMDVESSRDKLSERGFTPDLHKIPTRFEMGESPVNYDFFGGQQQSNTQLPGMLQPLPRQQVSFNDMQLLKQQVMVKQMHEYQMQQQLQKQRLEARQLNSLNRNAVNGSCVSDNQSHMINGIPLQNASSNWLQPDLMTGNTNWMHRGISPAVQGSSSGLMITPDHGQANLMAQQFEPSLYGMPVSGTNAPHNAFSSSQMNRLAAQHGSANRTSSVTNQPTSFLNQGDVQDSHMLPRSTYPEKLLFSQTSVPSSNSMPNFESLQEDDSRERNISVQAKFGQMEGSGPSEQSFIKAPENINALQKSTALDPTEEKILFGSDDNLWEAFGNSTDMSLTGNLMSSSSDLFDGCPSLQSGSWSALMQSAVAETSSDDAGVHEWANNSTGPHANFHRGNMAQDLGAKTSNTLSGRVHSDSTRTAVQHLQDRGNSVADNGLLENSMAQRNLMAENIFHSSSSGVDGQNNSCSIRKNEGVEDRLGIWKAASNPNLVALKEQNPSMQRTSYGFGIAGAGNDSRHLDNNSLEKAIPHLNSRDGSQILESYSSNNAGSNEMVNTRDLSTLPGGKETQSGHVGVRPSIPRKFQYHPMGNIDVTDEPCRGKVSRFGQSQSLGQPAMNTLTDKGHVSQNDLNRTNKAFKGMGPENSPSTSASADRSVDRCNQVNSASSRLELLHKVDPSPENSSETNVTGIHEANAFADYGGQFRHNQASASQGFNLQLAPPSQLAPSPDNMQFFRNSLQPLNSFHTGPEKGGTSQSRFAPWGSNQSFHQSTHQGPFPGILGGSNMTSGFPYSRGYHQNQQMAVGTRQSAAINSVNSSSELSTPAVKERDESSDFDQRGHSAEGFRMLSASQPLVASSSPQQNSSSGMMSDPPAGISAPQLRFWNQPLPQSDILRPHPSPGNNMAVSFSRQEKTNQLSSQNGDVSLSGRDIVNMHELQSKDMGAKQTSNVASMFSKMVQSNNQSFGRSLPSNNFPKDSLRHDEQMAGSGEGDAPKMTVKRVENSAIDPQKVAPKGEQQSPSKSDSLVRDGLNHRESVNHMPYFGQNVTQSFSTKNHSASVGADHQQISPQMAPSWYSQYGTFKNGLVQPVNDTGRFTPLKIGEQSSNVGSSVDGTHSVQLSQHFKMQQMSGSTLGAEIPSSESLPHGATEQLLKVNKPKKRKTATSELIPWNKEVMQGHQRLKTLGEAEVDWARATNRFAEKVEFETLLEDSPPIKSKRRLVYTTQLMQQLCSPPPARVISLVASSNYEFVAYTAARGALGDACSSSSTDRSEGFWPPNISNPLSERTKTEKISDQYISKAAEDFISRTRKLETDFARLENGTTIPDLRVEVQDLEKFAVINRFAKFHPPSMDRTLNSVRINPQRYVTVAPMPQNIPDRVQCLSL
Protein: p44-18ES, P44 outer membrane protein expression locus with P44-18 (Q2GIP9)
Organism: Anaplasma phagocytophilum (strain HZ)
Interaction partners:
Sequence:
MRKGKIILGSVMMSMAIVMAGNDVRAHDDVSALETGGAGYFYVGLDYSPAFSKIRDFSIRESNGETKAVYPYLKDGKSVKLESHKFDWNTPDPRIGFKDNMLVAMEGSVGYGIGGARVELEIGYERFKTKGIRDSGSKEDEADTVYLLAKELAYDVVTGQTDNLAAALAKTSGKDIVQFAKAVEISNSGIGKKVCETKRKDGDTTNRFAKYIVGAGDSSNAGTSLCGGKNQKSSDTDTGVEKAQALHDFVSNTLSDGTKNWPTSSETSKSNNDNAKAVAGDLTKKLTPEEKTIVAGLLAKTIEGGEVVEIRAVSSTSVMVNACYDLLSEGLGVVPYACVGLGGNFVGVVDGHITPKLAYRLKAGLSYQLSPEISAFAGGFYHRVVGDGVYDDLPAQRLVDDTSPAGRTKDTAIANFSMAYVGGEFGVRFAF
Protein: Thioredoxin reductase NTRC (EC 1.8.1.9) (NADPH-dependent thioredoxin reductase C) (OsNTRC) (Q70G58)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Thioredoxin reductase (TR) that exhibits both TR and thioredoxin (Trx) activities. Contains a C-terminal functional Trx domain. Functions as an electron donor for the plastidial 2-Cys peroxiredoxin BAS1 and participates in a NADPH-dependent hydrogen peroxide scavenging system in chloroplasts in the dark.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:15292215}.
Interaction partners:
- 2-Cys peroxiredoxin BAS1, chloroplastic
- Probable 5'-adenylylsulfate reductase 1, chloroplastic
- Os04g0416400 protein
- glutathione-disulfide reductase
- 1-Cys peroxiredoxin A
- 1-Cys peroxiredoxin B
- Glutathione reductase
- Glutathione reductase, cytosolic
- Os05g0160000 protein
- Os03g0662000 protein
Sequence:
MAVTRLAVAAALSAAPPSSRRRRAFFHHSCRPLPSSAAAAAKALRASAAPAVDEEAPASPPPSDLGKGVENLVIIGSGPAGYTAAIYAARANLKPVVFEGYQVGGVPGGQLMTTTEVENFPGFPDGVTGPDLMDKMRKQAERWGAELHQEDVEFVNVKSRPFVIRSSDREVKCHSVIIATGAAAKRLRLPREDEFWSRGISACAICDGASPLFKGQVLAVVGGGDTATEEAIYLTKYARHVHLLVRKDQLRASKAMQDRVLNNPNITVHFNTEAVDVVSNPKGQMSGIQLKRTDTGEESVLEVKGLFYGIGHTPNSQLLQGQIDLDDAGYILVEEGTAKTSVDGVFAAGDVQDHEWRQAVTAAGSGCVAALSVERYLVANDLLVEFHQPVREEKEKEITDRDVEMGFDISHTKHRGQYALRKVYHESPRLVCVLYTSPTCGPCRTLKPILSKVIDEYNEHVHFVEIDIEEDPEIAEAAGIMGTPCVQFFKNKEMLRTVSGVKMKKEYREFIESNK
Protein: Iron-responsive element-binding protein 2 (IRE-BP 2) (Iron regulatory protein 2) (IRP2) (Q62751)
Organism: Rattus norvegicus (Rat)
Function: RNA-binding protein that binds to iron-responsive elements (IRES), which are stem-loop structures found in the 5'-UTR of ferritin, and delta aminolevulinic acid synthase mRNAs, and in the 3'-UTR of transferrin receptor mRNA. Binding to the IRE element in ferritin results in the repression of its mRNA translation. Binding of the protein to the transferrin receptor mRNA inhibits the degradation of this otherwise rapidly degraded mRNA.
Subcellular location: Cytoplasm.
Interaction partners:
- F-box/LRR-repeat protein 5
- Citrate synthase, mitochondrial
- S-phase kinase-associated protein 1
- Sentrin-specific protease 8
- Transferrin receptor protein 1
- Isocitrate dehydrogenase cytoplasmic
- Isocitrate dehydrogenase, mitochondrial
- Natural resistance-associated macrophage protein 2
- RanBP-type and C3HC4-type zinc finger-containing protein 1
- Ferroportin
Sequence:
MDSPSAGYTFEYLIETLNGSSQKKFFNVPKLGGTKYDILPYSIRVLLEAAVRNCDGFLMKKEDVINILDWKTKQSNVEVPFFPARVVLQDFTGIPAMVDFAAMREAVKTLGGDPKKVHPACPTDLTVDHSLQIDFSKCAIQNAPNPGGGDLQKAGKLSPLKVQPKKLPCRGQTTCRGSCDSGELSRNSGTFSSQIENTPVLCPFHLQPVPEPETVLKNQEVEFGRNRERLQFFKWSSGAFKNVAVIPPGTGMAHQVNLEHLSRVVFEEADLLFPDSVIGTDSHITMVNGLGILGWGVGGIETEAVMLGLPVTLTLPEVVGCELTGSSNAFVTSIDIVLGITKHLRQVGVAGKFVEFFGSGVSQLSIVDRTTIANMCPEYGAILSFFPVDNVTLRHLEHTGFDKTKLESMEEYLKAVKLFRNDENSSEPEYSQVIQINLNSIVASVSGPKRPQDRVAVTDMKSDFQACLNEKVGFKGFQVAAEKQSDTVSVRYDGSEYKLSHGSVVIAAVISCTNNCNPSVMLAAGLLAKKAVETGLRVKPYIRTSLSPGSGMVTHYLSSSGVLPYLSKLGFEIVGYGCSTCVGNTAPLSEAILNAVKQGDLVTCGVLSGNKNFEGRLCDCVRANYLASPPLVVAYAIAGTVNIDFQTEPLGTDSTGKNIYLHDIWPSREEVHQIEEEHVILSMFKALKEKVEMGNKRWNSLDAPDSVLFPWDVKSTYIRCPSFFDKLTKEPAASQPIENAHVLLYLGDSVTTDHISPAGSIARSSAAAKYLTNRGLTPREFNSYGARRGNDAVMTRGTFANIKLFNKFIGKPAPKTIHFPSGQTLDVFEAAELYQKEGIPLIILAGKKYGSGNSRDWAAKGPYLLGVKAVLAESYEKIHKDHLIGIGIAPLEFLPGENADSLGLSGREVFSLSFPEELFPGITLNIKTSTGKEFSVIAAFENDVEITLYKHGGLLNFVARKFL
Protein: Cell cycle serine/threonine-protein kinase hsk1 (EC 2.7.11.1) (Cdc7-related kinase) (Minichromosome maintenance protein kinase) (P50582)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for G1/S transition. Plays a role in DNA replication checkpoint signaling through regulating rad3 and cds1. Involved in the maintenance of mitotic chromosome structures during S phase through regulating the function of rad21. Required for initiation of mitotic DNA replication through phosphorylating mcm2/cdc19. Required for genome integrity.
Subcellular location: Nucleus {ECO:0000269|PubMed:11027263}. Note=Nuclear throughout the cell cycle.
Interaction partners:
- DNA replication licensing factor mcm2
- Hsk1-interacting molecule 1
- DNA replication licensing factor mcm4
- DNA replication licensing factor mcm5
- Serine/threonine-protein kinase cds1
- DNA replication licensing factor mcm6
- DNA replication licensing factor mcm3
- DNA replication licensing factor mcm7
- Protein kinase rad3
- Mediator of replication checkpoint protein 1
Sequence:
MAEAHITLSPKVTHEQQTDIDSECEITEVDDENVNENKSQEMIQDIPARDREEIENITRTFVELQENYRLIEKIGEGTFSSVYKAEDLHYGRYINDWDIQSEVLKESSFGKEKIPVNEDSRKPKYVAIKKIYATSSPARIYNELEILYLLRGSSVIAPLITALRNEDQVLVVLPYYEHTDFRQYYSTFSYRDMSIYFRCLFQAMQQTQTLGIIHRDIKPSNFLFDVRTKHGVLVDFGLAERYDGRQQSHSCRCTNSNAAELAHDFSIAQETSLGYIKNDTRPSKRANRAGTRGFRAPEVLFKCSSQSPKVDIWSAGVILLSFLTKRFPMFNSKDDVDALMEIACIFGKSEMRQCAALHGCTFETNVSTLTEKRVNFRKLILWASCGSASIYKEKLRHKPSQEERLCLDFLEKCLELDCNKRISAEEALDHDFLYLDNLAYEKKDDDTAFDNSFGETSFEKDEDLTAKHLSHILDFKEQEETDEPTSLSKRKRSIDEILPNDALQDGA
Protein: Palmitoyltransferase ZDHHC23 (EC 2.3.1.225) (Zinc finger DHHC domain-containing protein 23) (DHHC-23) (zDHHC23) (Q8IYP9)
Organism: Homo sapiens (Human)
Function: Palmitoyltransferase that could catalyze the addition of palmitate onto various protein substrates and be involved in a variety of cellular processes (Probable). Palmitoyltransferase that mediates palmitoylation of KCNMA1, regulating localization of KCNMA1 to the plasma membrane. May be involved in NOS1 regulation and targeting to the synaptic membrane.
Subcellular location: Golgi apparatus membrane {ECO:0000305|PubMed:22399288}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus, trans-Golgi network membrane {ECO:0000305|PubMed:22399288}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Palmitoyltransferase ZDHHC22
Sequence:
MTQKGSMKPVKKKKTEEPELEPLCCCEYIDRNGEKNHVATCLCDCQDLDEGCDRWITCKSLQPETCERIMDTISDRLRIPWLRGAKKVNISIIPPLVLLPVFLHVASWHFLLGVVVLTSLPVLALWYYYLTHRRKEQTLFFLSLGLFSLGYMYYVFLQEVVPKGRVGPVQLAVLTCGLFLILLALHRAKKNPGYLSNPASGDRSLSSSQLECLSRKGQEKTKGFPGADMSGSLNNRTTKDDPKGSSKMPAGSPTKAKEDWCAKCQLVRPARAWHCRICGICVRRMDHHCVWINSCVGESNHQAFILALLIFLLTSVYGITLTLDTICRDRSVFTALFYCPGVYANYSSALSFTCVWYSVIITAGMAYIFLIQLINISYNVTEREVQQALRQKTGRRLLCGLIVDTGLLG
Protein: Forkhead box protein E3 (Forkhead-related protein FKHL12) (Forkhead-related transcription factor 8) (FREAC-8) (Q13461)
Organism: Homo sapiens (Human)
Function: Transcription factor that controls lens epithelial cell growth through regulation of proliferation, apoptosis and cell cycle. During lens development, controls the ratio of the lens fiber cells to the cells of the anterior lens epithelium by regulating the rate of proliferation and differentiation (By similarity). Controls lens vesicle closure and subsequent separation of the lens vesicle from ectoderm (By similarity). Controls the expression of DNAJB1 in a pathway that is crucial for the development of the anterior segment of the eye.
Subcellular location: Nucleus {ECO:0000269|PubMed:25504734}.
Interaction partners:
- G-protein coupled receptor 161
- Pituitary homeobox 3
- Paired box protein Pax-6
Sequence:
MAGRSDMDPPAAFSGFPALPAVAPSGPPPSPLAGAEPGREPEEAAAGRGEAAPTPAPGPGRRRRRPLQRGKPPYSYIALIAMALAHAPGRRLTLAAIYRFITERFAFYRDSPRKWQNSIRHNLTLNDCFVKVPREPGNPGKGNYWTLDPAAADMFDNGSFLRRRKRFKRAELPAHAAAAPGPPLPFPYAPYAPAPGPALLVPPPSAGPGPSPPARLFSVDSLVNLQPELAGLGAPEPPCCAAPDAAAAAFPPCAAAASPPLYSQVPDRLVLPATRPGPGPLPAEPLLALAGPAAALGPLSPGEAYLRQPGFASGLERYL
Protein: Large ribosomal subunit protein uL18 (60S ribosomal protein L5) (Q9NIU2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
DSLYAGCTEVTGEEFNVEPVDDGPGAFRCFLDVGLARTTTGARVFGAMKGAVDGGLNIPHSVXLFPGYSAETKSFNADVHRAHIFGQHVADYMRSLEEEDEESFKRQFSRYIKLGIRADDLEDIYKKAHQAIRNDPTHKVTAKNLLPLRXKXGMLRNSXTNNXRLRLQLIRHIFCQX
Protein: Cytochrome c2 (P86319)
Organism: Fuscovulum blasticum (Rhodobacter blasticus) (Rhodopseudomonas blastica)
Function: Cytochrome c2 is found mainly in purple, non-sulfur, photosynthetic bacteria where it functions as the electron donor to the oxidized bacteriochlorophyll in the photophosphorylation pathway. However, it may also have a role in the respiratory chain and is found in some non-photosynthetic bacteria.
Subcellular location: Periplasm {ECO:0000269|PubMed:20697695}.
Interaction partners:
Sequence:
QDAPTGDAAAGAKVFNKCQTCHMVVAPDGTVLAGKAGKTGNPLYGLDGRAPASYPDFAYGDGIKELGAAGEVWNEADFLQYVADPTKFLKTKTGDTKAKGKMTFKLPNEKEAHDVWAFLNSLAPAPAAAEAAPAADAAAPAAADAAAPAEPAAEGAAT
Protein: 1,2-phenylacetyl-CoA epoxidase, subunit A (EC 1.14.13.149) (1,2-phenylacetyl-CoA epoxidase, catalytic subunit alpha) (1,2-phenylacetyl-CoA monooxygenase, subunit A) (P76077)
Organism: Escherichia coli (strain K12)
Function: Component of 1,2-phenylacetyl-CoA epoxidase multicomponent enzyme system which catalyzes the reduction of phenylacetyl-CoA (PA-CoA) to form 1,2-epoxyphenylacetyl-CoA. The subunit A is the catalytic subunit involved in the incorporation of one atom of molecular oxygen into phenylacetyl-CoA.
Interaction partners:
- 1,2-phenylacetyl-CoA epoxidase, subunit C
- 1,2-phenylacetyl-CoA epoxidase, subunit E
- 1,2-epoxyphenylacetyl-CoA isomerase
- Putative 1,2-phenylacetyl-CoA epoxidase, subunit D
- 1,2-phenylacetyl-CoA epoxidase, subunit B
- Acyl-coenzyme A thioesterase PaaI
- Phenylacetate-coenzyme A ligase
- Bifunctional protein PaaZ
- 2,3-dehydroadipyl-CoA hydratase
- 3-hydroxyadipyl-CoA dehydrogenase
Sequence:
MTQEERFEQRIAQETAIEPQDWMPDAYRKTLIRQIGQHAHSEIVGMLPEGNWITRAPTLRRKAILLAKVQDEAGHGLYLYSAAETLGCAREDIYQKMLDGRMKYSSIFNYPTLSWADIGVIGWLVDGAAIVNQVALCRTSYGPYARAMVKICKEESFHQRQGFEACMALAQGSEAQKQMLQDAINRFWWPALMMFGPNDDNSPNSARSLTWKIKRFTNDELRQRFVDNTVPQVEMLGMTVPDPDLHFDTESGHYRFGEIDWQEFNEVINGRGICNQERLDAKRKAWEEGTWVREAALAHAQKQHARKVA
Protein: Transcription elongation factor A protein 1 (Transcription elongation factor S-II protein 1) (Transcription elongation factor TFIIS.o) (P23193)
Organism: Homo sapiens (Human)
Function: Necessary for efficient RNA polymerase II transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by S-II allows the resumption of elongation from the new 3'-terminus.
Subcellular location: Nucleus.
Interaction partners:
- DNA-directed RNA polymerase II subunit RPB1
- Transcription initiation factor IIB
- DNA-directed RNA polymerase II subunit RPB2
- DNA-directed RNA polymerase II subunit RPB9
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- TATA-box-binding protein
- Transcription elongation factor SPT6
- Transcription elongation factor SPT5
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
- Transcription elongation factor SPT4
Sequence:
MEDEVVRFAKKMDKMVQKKNAAGALDLLKELKNIPMTLELLQSTRIGMSVNAIRKQSTDEEVTSLAKSLIKSWKKLLDGPSTEKDLDEKKKEPAITSQNSPEAREESTSSGNVSNRKDETNARDTYVSSFPRAPSTSDSVRLKCREMLAAALRTGDDYIAIGADEEELGSQIEEAIYQEIRNTDMKYKNRVRSRISNLKDAKNPNLRKNVLCGNIPPDLFARMTAEEMASDELKEMRKNLTKEAIREHQMAKTGGTQTDLFTCGKCKKKNCTYTQVQTRSADEPMTTFVVCNECGNRWKFC
Protein: Large ribosomal subunit protein uL4B (60S ribosomal protein L4-B) (L2) (RP2) (YL2) (P49626)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102, ECO:0000269|PubMed:25936803}. Nucleus {ECO:0000269|PubMed:25936803}.
Interaction partners:
- Small ribosomal subunit protein uS5
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein uL10
- Large ribosomal subunit protein uL3
- Large ribosomal subunit protein eL32
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein uL16
- Large ribosomal subunit protein eL29
- Small ribosomal subunit protein uS7
Sequence:
MSRPQVTVHSLTGEATANALPLPAVFSAPIRPDIVHTVFTSVNKNKRQAYAVSEKAGHQTSAESWGTGRAVARIPRVGGGGTGRSGQGAFGNMCRGGRMFAPTKTWRKWNVKVNHNEKRYATASAIAATAVASLVLARGHRVEKIPEIPLVVSTDLESIQKTKEAVAALKAVGAHSDLLKVLKSKKLRAGKGKYRNRRWTQRRGPLVVYAEDNGIVKALRNVPGVETANVASLNLLQLAPGAHLGRFVIWTEAAFTKLDQVWGSETVASSKVGYTLPSHIISTSDVTRIINSSEIQSAIRPAGQATQKRTHVLKKNPLKNKQVLLRLNPYAKVFAAEKLGSKKAEKTGTKPAAVFAETLKHD
Protein: Alsin (Amyotrophic lateral sclerosis 2 protein homolog) (Q920R0)
Organism: Mus musculus (Mouse)
Function: May act as a GTPase regulator. Controls survival and growth of spinal motoneurons.
Interaction partners:
- Ras-related protein Rab-5A
- Probable helicase senataxin
- Serine/threonine-protein kinase Nek1
- GTPase-activating protein and VPS9 domain-containing protein 1
- Rab5 GDP/GTP exchange factor
- Charged multivesicular body protein 2b
- Guanine nucleotide exchange factor C9orf72 homolog
- Vesicle-associated membrane protein-associated protein B
- Polyphosphoinositide phosphatase
- Spatacsin
Sequence:
MDSKKKSSTEAEGSKERGLVHVWQAGSFSLTPERLPGWGGKTVLQAALGVRHGVLLTEDGEVYSFGTLPWKSESAEICPSSPLLESALVGHHVITVATGSFHSGAVTESGVVYMWGENAAGQCAVANQQYVPEPSPVSISDSETSPSLAVRILQLACGEEHTLALSLSREIWAWGTGCQLGLITTTFPVTKPQKVEHLAGRVVLQVACGAFHSLALVQCLPPQDLKPVPERCNQCSQLLITMTDKEDHVIISDSHCCPLGVTLSESQAEKHASPAPSPHPEALDEQGEVFENTVVEAELNMGSSQTTSGSAISTQQNVVGTAEVSSARTAPSYPDTHAVTAYLQKLSEHSMRENHEPGEKPPQVQPLVEEAVPDLHSPPTTSTSALNSLVVSCASAVGVRVAATYEAGALSLKKVMNFYSTAPCETAAQSGSASTGPESLKDLREEQVKQESLQGKKSSSLMDIREEELEGGSRRLSLPGLLSQVSPRLLRKAARVKTRTVVLTPTYSGEADALLPSLRTEVWTWGKGKEGQLGHGDVLPRLQPLCVKCLDGKEVIHLEAGGSHSLALTAKSQVYSWGSNTFGQLGHSEFPTTVPRLSKVSSENGVWSVAAGQDYSLFLVDTEDFQPGLYYSGRQDRAEGDTLPENPSGTKTPVLLSCSKLGYISRVTAGKDSYLALVDKNIMGYIASLHELASTERRFYSKLSEIKSQILRPLLSLENLGTVTTVQLLQEVASRFSKLCYLIGQHGASLSSYLQGMKEASSLVIMKHSSLFLDSYTEYCTSVSNFLVMGGFQLLAKPAIDFLNKNQELLQDLSEVNDENTQLMEILNMLFFLPIRRLHNYAKVLLKLATCFEVTSPEYQKLQDSSSCYESLALHLGKKRKEAEYTLSFWKTFPGKMTDSLRKPERRLLCESSNRALSLQHAGRFSVNWFILFNDALVHAQFSTHHVFPLATLWAEPLSEEAGSVNGLKITTPEEQFTLISSTPQEKTKWLRAISQAVDQALRGTSDFPLYGGGSSVQRQEPPISRSAKYTFYKDTRLKDATYDGRWLSGKPHGRGVLKWPDGKMYSGMFRNGLEDGYGEYRIPNKALNKEDHYVGHWKEGKMCGQGVYSYASGEVFEGCFQDNMRHGHGLLRSGKLTSSSPSMFIGQWVMDKKAGYGVFDDITRGEKYMGMWQDDVCQGNGVVVTQFGLYYEGNFHLNKMMGNGVLLSEDDTIYEGEFSDDWTLSGKGTLTMPHGDYIEGYFSGEWGSGIKITGTYFKPSLYESDKDKPKAFRKLGNLAVAADEKWRAVFEECWRQLGCESPGQGEVWKAWDNIAVALTTNRRQHKDSPEILSRSQTQTLESLEYIPQHIGAFSVEKYDDIKKYLIKACDTPLHPLGRLVETLVAVYRMTYVGVGANRRLLQEAVKEIKSYLKRIFQLVRFLFPELPEEGSTIPLSAPLPTGRRSFCTGKSDSRSESPEPGYVVTSSGLLLPVLLPRLYPPLFMLYALDNDREEDIYWECVLRLNKQPDIALLGFLGVQKKFWPATLSILGESKKVLSTTKDACFASAVECLQQISTTFTPSDKLKVIQQTFEEISQSVLASLQEDFLWSMDDLFPVFLYVVLRARIRNLGSEVHLIEDLMDPFLQHGEQGIMFTTLKACYFQIQREKLN
Protein: Diamine oxidase [copper-containing] (Diamine oxidase) (EC 1.4.3.22) (Amiloride-binding protein 1) (Amine oxidase copper domain-containing protein 1) (Histaminase) (P36633)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the degradation of compounds such as putrescine, histamine, spermine, and spermidine, substances involved in allergic and immune responses, cell proliferation, tissue differentiation, tumor formation, and possibly apoptosis.
Subcellular location: Secreted, extracellular space {ECO:0000250|UniProtKB:P19801}. Cell membrane {ECO:0000250|UniProtKB:P19801}; Peripheral membrane protein {ECO:0000250|UniProtKB:P19801}; Extracellular side {ECO:0000250|UniProtKB:P19801}.
Interaction partners:
- Histamine N-methyltransferase
- Amine oxidase [flavin-containing] B
- Histidine decarboxylase
- Ornithine decarboxylase
- Antizyme inhibitor 2
- Amine oxidase [flavin-containing] A
- Guanidino acid hydrolase, mitochondrial
- Spermidine synthase
- Aldehyde dehydrogenase family 3 member A2
- 4-trimethylaminobutyraldehyde dehydrogenase
Sequence:
MCLAFGWAAVILVLQTVDTASAVRTPYDKARVFADLSPQEIKAVHSFLMNREELGLQPSKEPTLAKNSVFLIEMLLPKKKHVLKFLDEGRKGPNREARAVIFFGAQDYPNVTEFAVGPLPRPYYIRALSPRPGHHLSWSSRPISTAEYDLLYHTLKRATMPLHQFFLDTTGFSFLGCDDRCLTFTDVAPRGVASGQRRSWFIVQRYVEGYFLHPTGLEILLDHGSTDVQDWRVEQLWYNGKFYNNPEELARKYAVGEVDTVVLEDPLPNGTEKPPLFSSYKPRGEFHTPVNVAGPHVVQPSGPRYKLEGNTVLYGGWSFSYRLRSSSGLQIFNVLFGGERVAYEVSVQEAVALYGGHTPAGMQTKYIDVGWGLGSVTHELAPGIDCPETATFLDAFHYYDSDGPVHYPHALCLFEMPTGVPLRRHFNSNFKGGFNFYAGLKGYVLVLRTTSTVYNYDYIWDFIFYSNGVMEAKMHATGYVHATFYTPEGLRHGTRLQTHLLGNIHTHLVHYRVDMDVAGTKNSFQTLTMKLENLTNPWSPSHSLVQPTLEQTQYSQEHQAAFRFGQTLPKYLLFSSPQKNCWGHRRSYRLQIHSMAEQVLPPGWQEERAVTWARYPLAVTKYRESERYSSSLYNQNDPWDPPVVFEEFLRNNENIEDEDLVAWVTVGFLHIPHSEDVPNTATPGNSVGFLLRPFNFFPEDPSLASRDTVIVWPQDKGLNRVQRWIPEDRRCLVSPPFSYNGTYKPV
Protein: Uncharacterized protein HHRF7 (P09708)
Organism: Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5)
Interaction partners:
Sequence:
MAMYTSESERDWRRVIHDSHGLWCDCGDWREHLYCVYDSHFQRRPTTRAERRAANWRRQMRRLHRLWCFCQDWKCHALYAEWDGKESDDESSASSSGEAPEQQVPAWKTVRAFSRAYHHRINRGLRGTPPPRNLPGYEHASEGWRFCSRRERREDDLRTRAEPDRVVFQLGGVPPRRHRETYV
Protein: Syntaxin binding protein 1 (A0A1B0GWF2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAPIGLKAVVGEKIMHDVIKKVKKKGEWKVLVVDQLSMRMLSSCCKMTDIMTEGITIVEDINKRREPLPSLEAVYLITPSEKSVHSLISDFKDPPTAKYRAAHVFFTDSCPDALFNELVKSRAAKVIKTLTEINIAFLPYESQVYSLDSADSFQSFYSPHKAQMKNPILERLAEQIATLCATLKEYPAVRYRGEYKDNALLAQLIQDKLDAYKADDPTMGEGPDKARSQLLILDRGFDPSSPVLHELTFQAMSYDLLPIENDVYKYETSGIGEARVKEVLLDEDDDLWIALRHKHIAEVSQEVTRSLKDFSSSKRMNTGEKTTMRDLSQMLKKMPQYQKELSKYSTHLHLAEDCMKHYQGTVDKLCRVEQDLAMGTDAEGEKIKDPMRAIVPILLDANVSTYDKIRIILLYIFLKNGITEENLNKLIQHAQIPPEDSEIITNMAHLGVPIVTDSTLRRRSKPERKERISEQTYQLSRWTPIIKDIMEDTIEDKLDTKHYPYISTRSSASFSTTAVSARYGHWHKNKAPGEYRSGPRLIIFILGGVSLNEMRCAYEVTQANGKWEVLIVPVEAGS
Protein: ribonuclease III (EC 3.1.26.3) (A7TR32)
Organism: Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus)
Interaction partners:
- ribonuclease III
- Piwi domain-containing protein
- Small ribosomal subunit protein uS9m
- Large ribosomal subunit protein bL27m
- Small ribosomal subunit protein bS6m
- 54S ribosomal protein IMG1
- Large ribosomal subunit protein bL17m C-terminal fungi domain-containing protein
- Large ribosomal subunit protein mL46
- Large ribosomal subunit protein bL33m
- Ribosomal protein S16
Sequence:
MSDQVYVPPTSAPMSNELKVREFYRLHNACVKLKESIKLIYENPLVTDQNVLNLGTAENTIDYTILNTPTLNVAKTLLGNRYSLDLIDLFQSHDFKDSNTDVDMFIKYPVVYDENLENLAFMHKSFPNMNAHLNDAQKTQLSNERLEFLGDSWLGALVSYIVYTRFPSANEGMLSQMKESIVNNNNLFDWSTKLNFTKRLQGNIATPTRVVKDKMSKRYADCVEAYIGALVIDRFGTEFLDIKEWLEELSEKKLAKSSQMVIKEPLNKNAKNELAELLQINKLGHKLHYRKLTEMPPFRVEVKIGDILLDEAEGNSIREAEHRAAMKVLENDELLRKYSVYDLEDGNSKKYSIEETDLKHDIESSGISNENFLQNEGNGTENIESKFKQLNISNDSNKDDLVNNITNSVFSKLQDVVSKIVIDAISESIPNNPHKIEQSRNGKVGTQTNTSATTSDVLSVQTSIPKSESTSADKAPITCDPNAKQALYTLLSRSQVFPDYEMVQHSMDNFTANCIIKGSGIFLASGRGRSKKIAQQNAASAALRSPILKSILEEQNNF
Protein: DNA-binding dual transcriptional regulator OmpR (Transcriptional regulatory protein OmpR) (E0SJT3)
Organism: Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))
Interaction partners:
- Sensor histidine kinase EnvZ
- histidine kinase
- histidine kinase
- Sensor protein
- Sensor protein
- Sensor histidine kinase RcsC
- Phosphate regulon sensor protein PhoR
- histidine kinase
- histidine kinase
- NADH-quinone oxidoreductase subunit C/D
Sequence:
MQENYKILVVDDDMRLRALLERYLTEQGFQVRSVANAEQMDRLLTRESFHLMVLDLMLPGEDGLSICRRLRSQSNPMPIIMVTAKGEEVDRIVGLEIGADDYIPKPFNPRELLARIRAVLRRQANELPGAPSQEEAIIAFGKFKLNLGTREMFRDDEPMPLTSGEFAVLKALVSHPREPLSRDKLMNLARGREYSAMERSIDVQISRLRRMVEEDPAHPRYIQTVWGLGYVFVPDGSKA