wanglab/gogpt-training-data huggingface dataset:
Protein: FAD-dependent urate hydroxylase (EC 1.14.13.-) (EC 1.14.13.113) (Flavoprotein urate hydroxylase) (Q8PDQ6)
Organism: Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
Function: Catalyzes the hydroxylation of urate to 5-hydroxyisourate (HIU). Is likely to be involved in the urate degradation pathway to allantoin. Is slightly more efficient (about 2.6 times) with NADPH than NADH as the electron donor.
Interaction partners:
- Hydroxylase molybdopterin-containing subunit
- Aldehyde oxidoreductase iron-sulfur-binding subunit PaoA
- Oxidoreductase
- Oxidoreductase
- Ferredoxin
- Oxidoreductase
- Hydroxylase large subunit
- Oxalurate catabolism protein HpxZ
- Serine-pyruvate aminotransferase
- NodB homology domain-containing protein
Sequence:
MSLAQLEHALQHDLQRLAHGGEPWVRPRVHPAGHVYDVVIVGAGQSGLGAAFALQRERVHNVLVIDENPPGQEGPWVTYARMQTLRTPKQITSIDLGVPTLTFRAWWEAQHGAAGWDALDKIPRGTWMDYLRWYRAALRLPVRNATQLVRIEPDAAPGIHRLHLAMGAPLMARKIILATGIQGGGQWQVPEWITQALPAQRYAHTSGPIDYAALAGKRVGILGGGASAFDNACFALDQGVARAEVFVRRAALPRVNPIRHMEQAGIIPRFAALPDADKYRMMASFFGRNQPPTNDTFQRACAHAGFALHLDAPWLGVEEHNDVVVVRTPQGEHRFDFLAIATGLVTDPRLRPELAALSGRIACWADRYQAPPGQANPVLDAHPYLGPGFELLPRTPDDAAAVDGLFAFNYSALINHGLSAAALSGLKVALPRLARAVADQLFLDDRQAMVEAYLGYDQAEFVGQWPQPTQAVA
Protein: alpha-amylase (EC 3.2.1.1) (Q9NKZ5)
Organism: Drosophila kikkawai (Fruit fly)
Interaction partners:
Sequence:
MFLTKSIVCLAILALASAQFDTNYASGRSGMVHLFEWKWDDIAAECENFLGPNGFAGVQVSPVNENAVKDSRPWWERYQPISYKLVTRSGNEEQFASMTRRCNAVGVRIYVDVIFNHMAANGGTYGTGGSTASPSSKSYPGVPYSSLDFNPTCAISNYNDANQVRNCELVGLRDLNQGNSYVQEKIAEFLNHLIDLGVAGFRVDAAKHMWPADLGVIYGRLKNLNTDHGFSSGSKAYIVQEVIDMGGEAISKSEYTGLGAITEFRHSDSIGKAFRGKDQLRYLSNWGTAWGFAASDRSLVFVDNHDNQRGHGAGGADVLTYKVPKQYKMASAFMLAHSFGTPRVMSSFSFSDTDQGPPTTDGHNIASPSFNSDNSCSGGWVCEHRWRQIYNMVAFRNAVGSDAIQNWWDNGSNQIAFSRGSRGFVAFNNDNYDLNSSLQTGLPAGTYCDVISGTKNGSSCTGKTVTVGSDGRASIYLGNSEDDGVLAIHVNAKL
Protein: Charged multivesicular body protein 5 (Vacuolar protein-sorting-associated protein 60) (Q9VVI9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Probable peripherally associated component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and are delivered to lysosomes enabling degradation of membrane proteins (By similarity). Specifically down-regulates Notch signaling activity in the germarium, probably by facilitating Notch endocytosis.
Subcellular location: Endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Vacuolar protein sorting-associated protein VTA1 homolog
- RH72336p
- GH14561p
- IST1 homolog
- Charged multivesicular body protein 4
- Vacuolar protein sorting 20, isoform A
- Charged multivesicular body protein 1, isoform A
- Vacuolar protein sorting-associated protein 28 homolog
- Tumor suppressor protein 101
- vesicle-fusing ATPase
Sequence:
MNRLFGRGKPKEPGPSLNDCIAGVDARATNIEEKISNLEAELRKYREQMSKMREGPAKNSVKQKALRVLKQKKAYEQQAESLRNQSFNMEQANYAAQSLKDTQATVAAMKDGVKQMKTEYKKINIDQIEDIQDDMADMFEQADEVQEALGRTYGMPEVDDDDLQAELDALGDEIALDDDTSYLDDVVKAPEAPSREPGADSIVPGKSTIETDEFGLPKIPTSLKTT
Protein: Small vasohibin-binding protein (Coiled coil domain-containing protein 23) (Q99LQ4)
Organism: Mus musculus (Mouse)
Function: Enhances the tyrosine carboxypeptidase activity of VASH1 and VASH2, thereby promoting the removal of the C-terminal tyrosine residue of alpha-tubulin. Also required to enhance the solubility and secretion of VASH1 and VASH2 (By similarity). Plays a role in axon and excitatory synapse formation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:20736312}. Secreted {ECO:0000269|PubMed:20736312}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q8N300}. Note=Detected both intracellularly and extracellularly (PubMed:20736312). Within cells, localizes mainly to the apical part of the cell (PubMed:20736312). {ECO:0000269|PubMed:20736312}.
Interaction partners:
- Tubulinyl-Tyr carboxypeptidase 1
- Tubulinyl-Tyr carboxypeptidase 2
- Tubulin alpha-1B chain
- Tubulin alpha-1A chain
- Tubulin--tyrosine ligase
Sequence:
MDPPARKEKSKVKEPAFRVEKAKQKSAQQELKQRQRAEIYALNRVMTELEQQQFDEFCKQMQPPGE
Protein: Ectodermal-neural cortex 1 (Q2V9T0)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MSVRVHENRKSRASSGSINIYLFHKSSYADSVLTHLNLLRQQRLFTDVLLHAGNRTFPCHRAVLAACSRYFEAMFSGGLKESQDSEVNFDNSIHPEVLELLLDYAYSSRVIINEENAESLLEAGDMLEFQDIRDACAEFLEKNLHPTNCLGMLLLSDAHQCTKLYELSWRMCLSNFQTIRKNEDFLQLPQDMVVQLLSSEELETEDERLVYESAMNWISYDLKKRYCYLPELLQTVRLALLPAIYLMENVAMEELITKQRKSKEIVEEAIRCKLKILQNDGVVTSLCARPRKTGHALFLLGGQTFMCDKLYLVDQKAKEIIPKADIPSPRKEFSACAIGCKVYITGGRGSENGVSKDVWVYDTLHEEWSKAAPMLVARFGHGSAELKHCLYVVGGHTAATGCLPASPSVSLKQVEQYDPTTNKWTMVAPLREGVSNAAVVSAKLKLFAFGGTSVSHDKLPKVQCYDQCENRWTVPATCPQPWRYTAAAVLGNQIFIMGGDTEFSACSAYKFNSETYQWTKVGDVTAKRMSCHAVASGNKLYVVGGYFGIQRCKTLDCYDPTLDVWNSITTVPYSLIPTAFVSTWKHLPS
Protein: Integrin alpha-PS1 (Position-specific antigen subunit alpha-1) (Protein multiple edematous wings) [Cleaved into: Integrin alpha-PS1 heavy chain; Integrin alpha-PS1 light chain] (Q24247)
Organism: Drosophila melanogaster (Fruit fly)
Function: Integrin alpha-PS1/beta-PS is a receptor for laminin.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:19035354}; Single-pass type I membrane protein {ECO:0000269|PubMed:19035354}. Lateral cell membrane {ECO:0000269|PubMed:19035354}; Single-pass type I membrane protein {ECO:0000269|PubMed:19035354}. Basal cell membrane {ECO:0000269|PubMed:19035354}; Single-pass type I membrane protein {ECO:0000269|PubMed:19035354}. Note=During mid-oogenesis, localizes to the apical, to the lateral and to the basal membranes of follicle cells. Apical membrane localization peaks at oogenesis stages 9 and 10A in columnar follicle cells overlying the oocyte while decreases in the most posterior follicle cells. Localization to lateral and basal membranes persists during dorsal appendage morphogenesis, although diminished and often absent.
Interaction partners:
- Integrin beta-PS
- Integrin alpha-PS2
- Integrin beta-nu
- Integrin alpha-PS5
- Integrin alpha-PS3
- Integrin alpha-PS4
- Laminin subunit alpha
Sequence:
MLELPFTTIRPNCRLRQNLGILIILQCVLTCYNFNLEQRLPIVKYGHPHSHFGYSVATHTIGEANGPNKTNCVLVGAPLDQNRQPNTTHSGALWRCPMTQRFDDCEQVITDGRRNFDSEILSPPGNDEIKEDQWMGVTVRSNPLQANGSGGKVIVCAHRYMYIVRENRYGQGLCYLLTNDLQFEEVHEPCKGRPVQRQHEDYGLCQAGTSAALLDDDTMVLGSPGPYTWRGSIWVTQVGGEYLQRDKTTYYSDHSDLNSPVDKYSYLGMSVTGGRFFGHMSYAAGAPRSEGHGQVVIFDKSTDNPIPVHSILDGEQFGSSFGYELATADINGDHRPDLIVAAPLYFTKTEGGAVYVYQNIQDTLPMKYTLKLTGPLESRFGLALANIGDLNKDNCEDLAVGAPYEGNGVVYIYLGSSQGLNSKPAQKIQASELGGTIPNGQPIRTFGISISGNTDLDDNSYPDVVIGAFNSSAAVILLARPIISIQTSVQRKELHNMDPNTPGCLDDPASNLTCFTFRACCSIEPYDEKNKELRLAYSVEAETFDHLKKFSRVFFFDRENKRTNVLSRVVRVHTNGRTECQAVTGYIKANTRDIQTPVRFRLKYSLVEPPLADSALVRLNPILDQTQAHVDFEGTFQKDCGDDDLCESNLIIRVEPNITESSGNEYTLILDETELEVRINVSNLADSAYEAQLFIAHQAGVSYVATKKPTNATCNSYNTTLVACSLGNPMLRDTTTFVTIRFQPKGLEPSEKIMLFHIFANTTSKLVGPERPERDLRVNVVRRAKLNFRGWAIPEQSFYSGSSVANSVANTAATDIEGHGPMGMDDVGSQVHHMFTIFNEGPSTAPKVQMVIHWPYSLYSDPQSGRPVQYLLYLEQVPTVEVSQGECHVAKEYVNPLNLASGSRENPAYLSAPAQMRMFPSQSRHSFNKSLIHSQRSYYSSSHRDDHSDDTQSNRNRVRRSFLERVTRLERLMYDPESSNAANGKKQDIVELDCNKGATNCVRIECDILNMPALSEAQVVVKARLWNSTLVSEYPRVERVRIFSTATAQIPESYGVEVMDHNNIEVETRAYPELRNQQRDTSIPWLIIILGIVGGLLLLALVTYVLWKVGFFKRIRPTDPTLSGNLEKMNEEKPFLAPSKNTHHVF
Protein: C-X-C motif chemokine (Q6I9S7)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU361149}.
Interaction partners:
Sequence:
MSLLSSRAARVPGPSSSLCALLVLLLLLTQPGPIASAGPAAAVLRELRCVCLQTTQGVHPKMISNLQVFAIGPQCSKVEVVASLKNGKEICLDPEAPFLKKVIQKILDGGNKEN
Protein: Disks large homolog 5 N-terminal domain-containing protein (Q3TQT7)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MRNCICNIRHHVTAADLNRKTTEASKNLKMLEEEIGFYRNLHSQLRMAQAQLKNKVNMLKQENRRIWGRCATLQQNLEELKMIYKNQLEDTSDPQTQQQQDPERTEELLQDSHKQKKLGIQEKNLAEKQQYYFEVRRKSHLYSCFLTELNQLKKKLEMLSQ
Protein: Resuscitation-promoting factor RpfB (EC 3.-.-.-) (P9WG29)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Factor that stimulates resuscitation of dormant cells. Has peptidoglycan (PG) hydrolytic activity. Active in the pM concentration range. Has little to no effect on actively-growing cells. PG fragments could either directly activate the resuscitation pathway of dormant bacteria or serve as a substrate for endogenous Rpf, resulting in low molecular weight products with resuscitation activity.
Subcellular location: Cell membrane {ECO:0000255|PROSITE-ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}. Note=Localizes to the septa upon expression in M.smegmatis. {ECO:0000269|PubMed:17919286}.
Interaction partners:
- Ribosomal RNA small subunit methyltransferase A
- Peptidoglycan endopeptidase RipA
- Uncharacterized metal-dependent hydrolase TatD
- Diacylglycerol acyltransferase/mycolyltransferase Ag85B
- Antitoxin VapB47
- 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase
- Peptidoglycan endopeptidase RipB
- Probable endopeptidase Rv2190c
Sequence:
MLRLVVGALLLVLAFAGGYAVAACKTVTLTVDGTAMRVTTMKSRVIDIVEENGFSVDDRDDLYPAAGVQVHDADTIVLRRSRPLQISLDGHDAKQVWTTASTVDEALAQLAMTDTAPAAASRASRVPLSGMALPVVSAKTVQLNDGGLVRTVHLPAPNVAGLLSAAGVPLLQSDHVVPAATAPIVEGMQIQVTRNRIKKVTERLPLPPNARRVEDPEMNMSREVVEDPGVPGTQDVTFAVAEVNGVETGRLPVANVVVTPAHEAVVRVGTKPGTEVPPVIDGSIWDAIAGCEAGGNWAINTGNGYYGGVQFDQGTWEANGGLRYAPRADLATREEQIAVAEVTRLRQGWGAWPVCAARAGAR
Protein: Hydroxymethylglutaryl-CoA synthase, cytoplasmic (HMG-CoA synthase) (EC 2.3.3.10) (3-hydroxy-3-methylglutaryl coenzyme A synthase) (Q01581)
Organism: Homo sapiens (Human)
Function: Catalyzes the condensation of acetyl-CoA with acetoacetyl-CoA to form HMG-CoA, which is converted by HMG-CoA reductase (HMGCR) into mevalonate, a precursor for cholesterol synthesis.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:1358203}.
Interaction partners:
- 3-hydroxy-3-methylglutaryl-coenzyme A reductase
- Acetyl-CoA acetyltransferase, cytosolic
- Farnesyl pyrophosphate synthase
- Acetyl-CoA acetyltransferase, mitochondrial
- 3-ketoacyl-CoA thiolase, mitochondrial
- Trifunctional enzyme subunit beta, mitochondrial
- 3-ketoacyl-CoA thiolase, peroxisomal
- Squalene synthase
- Hydroxymethylglutaryl-CoA lyase, mitochondrial
- Squalene monooxygenase
Sequence:
MPGSLPLNAEACWPKDVGIVALEIYFPSQYVDQAELEKYDGVDAGKYTIGLGQAKMGFCTDREDINSLCMTVVQNLMERNNLSYDCIGRLEVGTETIIDKSKSVKTNLMQLFEESGNTDIEGIDTTNACYGGTAAVFNAVNWIESSSWDGRYALVVAGDIAVYATGNARPTGGVGAVALLIGPNAPLIFERGLRGTHMQHAYDFYKPDMLSEYPIVDGKLSIQCYLSALDRCYSVYCKKIHAQWQKEGNDKDFTLNDFGFMIFHSPYCKLVQKSLARMLLNDFLNDQNRDKNSIYSGLEAFGDVKLEDTYFDRDVEKAFMKASSELFSQKTKASLLVSNQNGNMYTSSVYGSLASVLAQYSPQQLAGKRIGVFSYGSGLAATLYSLKVTQDATPGSALDKITASLCDLKSRLDSRTGVAPDVFAENMKLREDTHHLVNYIPQGSIDSLFEGTWYLVRVDEKHRRTYARRPTPNDDTLDEGVGLVHSNIATEHIPSPAKKVPRLPATAAEPEAAVISNGEH
Protein: MLP-like protein 329 (Q9ZVF2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Cysteine-rich receptor-like protein kinase 25
- Exocyst subunit Exo70 family protein
- Putative defensin-like protein 131
- Putative defensin-like protein 162
- Putative cytochrome P450 71A28
- Cytochrome P450 71B8
- Defensin-like protein 151
- Cytochrome P450 710A3
- MLO-like protein 5
Sequence:
MATSGTYVTEVPLKGSADKHYKRWRDENHLFPDAIGHHIQGVTVHDGEWDSHEAIKIWNYTCDGKPEVFKERKEIDDENMVITFRGLEGHVMEQLKVYDLIYQFSQKSPDDIVCKITMIWEKRTDDSPEPSNYMKFLKSVVADMDEHVLKA
Protein: Zinc finger protein Pegasus (Ikaros family zinc finger protein 5) (Q9H5V7)
Organism: Homo sapiens (Human)
Function: Transcriptional repressor that binds the core 5'GNNTGTNG-3' DNA consensus sequence. Involved in megakaryocyte differentiation.
Subcellular location: Nucleus {ECO:0000269|PubMed:31217188}.
Interaction partners:
- Zinc finger protein Aiolos
- DNA-binding protein Ikaros
- Zinc finger protein Eos
Sequence:
MGEKKPEPLDFVKDFQEYLTQQTHHVNMISGSVSGDKEAEALQGAGTDGDQNGLDHPSVEVSLDENSGMLVDGFERTFDGKLKCRYCNYASKGTARLIEHIRIHTGEKPHRCHLCPFASAYERHLEAHMRSHTGEKPYKCELCSFRCSDRSNLSHHRRRKHKMVPIKGTRSSLSSKKMWGVLQKKTSNLGYSRRALINLSPPSMVVQKPDYLNDFTHEIPNIQTDSYESMAKTTPTGGLPRDPQELMVDNPLNQLSTLAGQLSSLPPENQNPASPDVVPCPDEKPFMIQQPSTQAVVSAVSASIPQSSSPTSPEPRPSHSQRNYSPVAGPSSEPSAHTSTPSIGNSQPSTPAPALPVQDPQLLHHCQHCDMYFADNILYTIHMGCHGYENPFQCNICGCKCKNKYDFACHFARGQHNQH
Protein: SRSF protein kinase 3 (EC 2.7.11.1) (Muscle-specific serine kinase 1) (MSSK-1) (Serine/arginine-rich protein-specific kinase 3) (SR-protein-specific kinase 3) (Serine/threonine-protein kinase 23) (Q9Z0G2)
Organism: Mus musculus (Mouse)
Function: Serine/arginine-rich protein-specific kinase which specifically phosphorylates its substrates at serine residues located in regions rich in arginine/serine dipeptides, known as RS domains. Phosphorylates the SR splicing factor SRSF1 and the lamin-B receptor (LBR) in vitro. Required for normal muscle development.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9UPE1}. Cytoplasm {ECO:0000250|UniProtKB:Q9UPE1}.
Interaction partners:
Sequence:
MSANAGGSGSVDCGGSSSSSQTSCGPESSGSELTPATPAPRLLQGLLGSDDEEQEDPKDYCKGGYYPVKIGDLFNGRYHVVRKLGWGHFSTVWLCWDIQRKRFVALKVVKSAGHYTETAVDEIKLLKCVRDSDPSDPKRETIVQLIDDFRISGVNGVHVCMVLEVLGHQLLKWIIKSNYQGLPVPCVKSIVRQVLHGLDYLHTKCKIIHTDIKPENILLCVGDAYIRRLAAEATEWQQSGAQPPSRSTVSTAPQEVLIGKLSKNKRKKMRRKRKQQKRLLEERLRDLQRLEAMEAAVQAEDSSSRLERGSGSTSSSGCHPEGTRAGPSPASSSPVPGGERSLSPSSQTSGFSGSLFSTASCSILSGSSNQRETGGLLSPSTPFGASNLLVNPLEPQNADKIKIKIADLGNACWVHKHFTEDIQTRQYRAVEVLIGAEYGPPADIWSTACMAFELATGDYLFEPHSGEDYSRDEDHIAHIVELLGDIPPAFALSGRYSREFFNRRGELRHIPNLKHWGLYEVLMEKYEWPLEQATQFSAFLLPMMEYIPEKRASAADCLQHPWLNP
Protein: Ferrichrome receptor FiuA (Q9I648)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Cell outer membrane {ECO:0000256|ARBA:ARBA00004571, ECO:0000256|PROSITE-ProRule:PRU01360}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004571, ECO:0000256|PROSITE-ProRule:PRU01360}.
Interaction partners:
- Anti-sigma factor FoxR
- Probable transmembrane sensor
- Protein TonB
- Ferric enterobactin receptor
- Probable sigma-70 factor, ECF subfamily
- Protein tonB2
- VreA
- Tol-Pal system protein TolA
Sequence:
MPRPTFRPGLLALAIALAVPAPFLHAAPAEQASVRDYRIAAGPLAGTLNRIAAQAGLVLTLDPALAEGRSAHAVQGRFDAPGALREALKGSGLELVENAGGTYSLRKVPEDTLSLQAMTVSGAEEDPLGPTSGYVAKRSMTGTKTDTPILETPRSISVATRQQMTDRAVHNLDDAVRYMPGVVASSFGSDSRSDWLKVRGFKPTQFLDGLPMAVGVYNNPKLETWNLERVALLRGPASSVYGQTPPGGMLDMVSLRPQNVASHEVKAEVGNYNHKQVSFDSTGPLDDEGRFLYRVSGVVRDSNTQVDHIDDKRYNIAPSLTWNIDDDTRLTFLGQFNRDDTGITSQFLPLRGTKYDAPFGKVSHHKNLGDPDWEYYDRTYYWLGYAFERRINDVWQFRQNLRYLRNDLSFQALTPASYYAAASDDGTLQRTSTSVDEDVSQFVVDNNFQADFDTGALRHTLLLGLDHNRTTNEYTSIFGFNVPPTNINNPIYGQPIPKPPRSDAYYDYKQKTYQTGLYVQDQIALDNWRLTLGGREDWVHTGATFYNKGDATNTSRDKKFSGNAALSYIFDNGVAPYISYAESFQPTTGADMNSTSSLKPTEGKQWEIGVKYQPVGSDSLFTAAVYDLRQENVSVSQNIGGTPVTSQTGEVKVSGIELEATSNVTDNLKMIGAYSYADTEVKKGQYAGNRLQQAPRNQASLWADYTWHEGTLNGFSVGAGARYVGSTYGDQANTYDGYAGSYTLYDAAVRYDLGQLNGSLKGVSVAVNANNLFNKDYLASCDGYYCYYGDQRSVVGSVSYKW
Protein: Galactose-binding lectin (CCL) (C0HLX7)
Organism: Chondrilla caribensis (Chicken liver sponge)
Function: Galactose-binding lectin. Displays antibacterial and hemagglutinin activity. Inhibits the growth of L.infantum promastigotes by damaging their membrane integrity and inducing cell apoptosis via the production of reactive oxygen species (ROS). Inhibition of L.infantum promastigotes appears to increase with time (MIC=1.2 uM/ml after 24 hours, MIC=0.9 uM/ml after 48 hours and MIC=0.6 uM/ml after 72 hours). Agglutinates Gram-negative and Gram-positive bacteria including E.coli, S.aureus and S.epidermidis, and inhibits biofilm formation by S.aureus and S.epidermidis. Displays hemagglutination activity towards all types of human erythrocytes (O, A and B) and rabbit erythrocytes.
Interaction partners:
Sequence:
TYAEVESFGVGQSATAVYTAPGDGRDLNITIDADGGYVIHMDYRFDWGGNPSTGKPWEDILILNSKPAQTWGPQQHVNNFYFTPGTHVTLGDKSNDGHFAIIADGIQVATYDHRLPVNSVKEVKFSTTAGSGTDIWDLLLLP
Protein: Thimet oligopeptidase (EC 3.4.24.15) (Endopeptidase 24.15) (MP78) (P52888)
Organism: Homo sapiens (Human)
Function: Involved in the metabolism of neuropeptides under 20 amino acid residues long. Involved in cytoplasmic peptide degradation. Able to degrade the amyloid-beta precursor protein and generate amyloidogenic fragments. Also acts as a regulator of cannabinoid signaling pathway by mediating degradation of hemopressin, an antagonist peptide of the cannabinoid receptor CNR1 (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P47788}.
Interaction partners:
- Kininogen-1
- Calmodulin-1
- Prolyl endopeptidase
- Syntaxin-6
Sequence:
MKPPAACAGDMADAASPCSVVNDLRWDLSAQQIEERTRELIEQTKRVYDQVGTQEFEDVSYESTLKALADVEVTYTVQRNILDFPQHVSPSKDIRTASTEADKKLSEFDVEMSMREDVYQRIVWLQEKVQKDSLRPEAARYLERLIKLGRRNGLHLPRETQENIKRIKKKLSLLCIDFNKNLNEDTTFLPFTLQELGGLPEDFLNSLEKMEDGKLKVTLKYPHYFPLLKKCHVPETRRKVEEAFNCRCKEENCAILKELVTLRAQKSRLLGFHTHADYVLEMNMAKTSQTVATFLDELAQKLKPLGEQERAVILELKRAECERRGLPFDGRIRAWDMRYYMNQVEETRYCVDQNLLKEYFPVQVVTHGLLGIYQELLGLAFHHEEGASAWHEDVRLYTARDAASGEVVGKFYLDLYPREGKYGHAACFGLQPGCLRQDGSRQIAIAAMVANFTKPTADAPSLLQHDEVETYFHEFGHVMHQLCSQAEFAMFSGTHVERDFVEAPSQMLENWVWEQEPLLRMSRHYRTGSAVPRELLEKLIESRQANTGLFNLRQIVLAKVDQALHTQTDADPAEEYARLCQEILGVPATPGTNMPATFGHLAGGYDAQYYGYLWSEVYSMDMFHTRFKQEGVLNSKVGMDYRSCILRPGGSEDASAMLRRFLGRDPKQDAFLLSKGLQVGGCEPEPQVC
Protein: Chordin-like protein 1 (Neuralin-1) (Neurogenesin-1) (Ventroptin) (Q920C1)
Organism: Mus musculus (Mouse)
Function: Seems to antagonize the function of BMP4 by binding to it and preventing its interaction with receptors. Alters the fate commitment of neural stem cells from gliogenesis to neurogenesis. Contributes to neuronal differentiation of neural stem cells in the brain by preventing the adoption of a glial fate. May play a crucial role in dorsoventral axis formation (By similarity). Antagonizes the function of BMP7 and may thus play an important role in the embryonic bone formation. Shows no inhibitory effect on the inducing activity of BMP2. Plays a role during anterior segment eye development (By similarity).
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MDGMKYIISLFFIFVFLEGSKTEQVKHSDTYCVFQDKKYRVGEKWHPYLEPYGLVYCVNCICSENGNVLCSRVRCPSLHCLSPVHIPHLCCPRCPDSLPPVNNKVTSKSCEYNGTTYQHGELFIAEGLFQNRQPNQCSQCSCSEGNVYCGLKTCPKLTCAFPVSVPDSCCRVCRGDAELSWEHADGDIFRQPANREARHSYLRSPYDPPPNRQAGGLPRFPGSRSHRGAVIDSQQASGTIVQIVINNKHKHGQVCVSNGKTYSHGESWHPNLRAFGIVECVLCTCNVTKQECKKIHCPNRYPCKYPQKIDGKCCKVCPEEPPSQNFDSKGSFCGEETMPVYESVFMEDGETTRKVALETERPPQVEVHVWTIQKGILQHFHIEKISKRMFGELHHFKLVTRTTLNQWKLFTEGEAQLSQMCSSQVCRTELEDLVQVLYLGRPEKDHC
Protein: Small ribosomal subunit protein mS26 (28S ribosomal protein S13, mitochondrial) (MRP-S13) (S13mt) (28S ribosomal protein S26, mitochondrial) (MRP-S26) (S26mt) (Q9BYN8)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:25838379}.
Interaction partners:
- Small ribosomal subunit protein mS34
- Small ribosomal subunit protein mS22
- Small ribosomal subunit protein uS15m
- Small ribosomal subunit protein bS16m
- Small ribosomal subunit protein mS25
- Small ribosomal subunit protein mS40
- Small ribosomal subunit protein uS5m
- Small ribosomal subunit protein uS17m
- Small ribosomal subunit protein mS27
- Small ribosomal subunit protein mS31
Sequence:
MLRALSRLGAGTPCRPRAPLVLPARGRKTRHDPLAKSKIERVNMPPAVDPAEFFVLMERYQHYRQTVRALRMEFVSEVQRKVHEARAGVLAERKALKDAAEHRELMAWNQAENRRLHELRIARLRQEEREQEQRQALEQARKAEEVQAWAQRKEREVLQLQEEVKNFITRENLEARVEAALDSRKNYNWAITREGLVVRPQRRDS
Protein: ATP-dependent RNA helicase (EC 3.6.4.13) (Q4GZ57)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Ribosome biogenesis protein BOP1 homolog
- Sas10 C-terminal domain-containing protein
- U3 small nucleolar RNA-associated protein 14
- Nrap protein domain-containing protein
- U3 small nucleolar RNA-associated protein 25
- RNA helicase
- RNA helicase
- Peter pan protein, putative
- HEAT repeat-containing protein 1
- RNA-binding protein, putative
Sequence:
MLSPWNDCVGDDHQWILKPLQNRLRYERPLPVQQAVVPTVRRALLSGLPMDVCLTAPTGSGKTLCYLLPLLQMITEAKKGTNHTRLLALVLVPTKALGQQVTHELQRLTRGTTITTVSLCDEMSVKEEAAALVRTVRLVGSGTHQTQGHYRNVPYMNIYNGDSVSLPSNAAGVAHNEDESEDGASSSDGGNGEEVGYDSMVDSSLHYYSRADIVISTPQRLLRHLDGTPGFTLLHLRLLVIDEADQVLSGNFANFVAKVVERFEEEQASRVGSTGDRRRLTQLTYSLHKFLCSATLSSHITRISEVRLRNCRHFTLDSFGTEIQREDEGEPLPLPSTDDTGSRKKNKRDQERGNANTKNKRGDDVGKGGEEDSCEDGNEEVKLPLSRQQLVRTSFALPPRLQEHVVFVEDWYRHAVLLKLVRAIVDKQKKAEALVKEHKRREEGLAAQDDESEGTGLGSNGYGTFSRENVRECESTEFRALPHRRRGASKLVGASDPSYPSCDDDAGRRIVIFCRSADEARVMGHFLLSAGVQATEFTTLATESERRRALLKSRPDSCVVASDALMRGVDVPNVGHVIMYNPPETLSQYVHRAGRTARAMRAGHLHLLLQKLGPSGTMKDGEVAMFKAISAAVSRMQPVRYERHFFMFDVAPTQLGKVAIESSPEGGNNGEGRGLVKDKARLLIEEADRYLKETQLRLTGRWVSALESARRGDAVGNKPSSATFGGSRRFISQTKRERG
Protein: Serine/threonine-protein phosphatase 1 regulatory subunit 10 (MHC class I region proline-rich protein CAT53) (PP1-binding protein of 114 kDa) (Phosphatase 1 nuclear targeting subunit) (Protein FB19) (p99) (Q96QC0)
Organism: Homo sapiens (Human)
Function: Scaffold protein which mediates the formation of the PTW/PP1 phosphatase complex by providing a binding platform to each component of the complex. The PTW/PP1 phosphatase complex plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. Mediates interaction of WDR82 and PPP1CA. Inhibitor of PPP1CA and PPP1CC phosphatase activities. Has inhibitory activity on PPP1CA only when phosphorylated. Binds to mRNA, single-stranded DNA (ssDNA), poly(A) and poly(G) homopolymers (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00649, ECO:0000269|PubMed:9450550}. Note=Found in discrete nucleoplasmic bodies and within nucleoli. Associates with chromatin during interphase, excluded from condensed chromosomes during early mitosis and is reloaded onto chromosomes at the late telophase (By similarity). {ECO:0000250}.
Interaction partners:
- Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
- WD repeat-containing protein 82
- Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
- Serine/threonine-protein phosphatase PP1-beta catalytic subunit
- TOX high mobility group box family member 4
- Protein phosphatase 1 regulatory subunit 12A
- Smad nuclear-interacting protein 1
- Telomeric repeat-binding factor 2
- Nuclear inhibitor of protein phosphatase 1
- Cell division cycle-associated protein 2
Sequence:
MGSGPIDPKELLKGLDSFLNRDGEVKSVDGISKIFSLMKEARKMVSRCTYLNILLQTRSPEILVKFIDVGGYKLLNNWLTYSKTTNNIPLLQQILLTLQHLPLTVDHLKQNNTAKLVKQLSKSSEDEELRKLASVLVSDWMAVIRSQSSTQPAEKDKKKRKDEGKSRTTLPERPLTEVKAETRAEEAPEKKREKPKSLRTTAPSHAKFRSTGLELETPSLVPVKKNASTVVVSDKYNLKPIPLKRQSNVAAPGDATPPAEKKYKPLNTTPNATKEIKVKIIPPQPMEGLGFLDALNSAPVPGIKIKKKKKVLSPTAAKPSPFEGKTSTEPSTAKPSSPEPAPPSEAMDADRPGTPVPPVEVPELMDTASLEPGALDAKPVESPGDPNQLTRKGRKRKSVTWPEEGKLREYFYFELDETERVNVNKIKDFGEAAKREILSDRHAFETARRLSHDNMEEKVPWVCPRPLVLPSPLVTPGSNSQERYIQAEREKGILQELFLNKESPHEPDPEPYEPIPPKLIPLDEECSMDETPYVETLEPGGSGGSPDGAGGSKLPPVLANLMGSMGAGKGPQGPGGGGINVQEILTSIMGSPNSHPSEELLKQPDYSDKIKQMLVPHGLLGPGPIANGFPPGGPGGPKGMQHFPPGPGGPMPGPHGGPGGPVGPRLLGPPPPPRGGDPFWDGPGDPMRGGPMRGGPGPGPGPYHRGRGGRGGNEPPPPPPPFRGARGGRSGGGPPNGRGGPGGGMVGGGGHRPHEGPGGGMGNSSGHRPHEGPGGGMGSGHRPHEGPGGSMGGGGGHRPHEGPGGGISGGSGHRPHEGPGGGMGAGGGHRPHEGPGGSMGGSGGHRPHEGPGHGGPHGHRPHDVPGHRGHDHRGPPPHEHRGHDGPGHGGGGHRGHDGGHSHGGDMSNRPVCRHFMMKGNCRYENNCAFYHPGVNGPPLP